A protein complex composed of three identical PCNA monomers, each comprising two similar domains, which are joined in a head-to-tail arrangement to form a homotrimer. Forms a ring-like structure in solution, with a central hole sufficiently large to accommodate the double helix of DNA. Originally characterized as a DNA sliding clamp for replicative DNA polymerases and as an essential component of the replisome, and has also been shown to be involved in other processes including Okazaki fragment processing, DNA repair, translesion DNA synthesis, DNA methylation, chromatin remodeling and cell cycle regulation.
A protein complex composed of three identical PCNA monomers, each comprising two similar domains, which are joined in a head-to-tail arrangement to form a homotrimer. Forms a ring-like structure in solution, with a central hole sufficiently large to accommodate the double helix of DNA. Originally characterized as a DNA sliding clamp for replicative DNA polymerases and as an essential component of the replisome, and has also been shown to be involved in other processes including Okazaki fragment processing, DNA repair, translesion DNA synthesis, DNA methylation, chromatin remodeling and cell cycle regulation.
A conserved heterotrimeric complex that binds nonspecifically to single-stranded DNA and is required for multiple processes in eukaryotic DNA metabolism, including DNA replication, DNA repair, and recombination. In all eukaryotic organisms examined the complex is composed of subunits of approximately 70, 30, and 14 kDa.
A conserved heterotrimeric complex that binds nonspecifically to single-stranded DNA and is required for multiple processes in eukaryotic DNA metabolism, including DNA replication, DNA repair, and recombination. In all eukaryotic organisms examined the complex is composed of subunits of approximately 70, 30, and 14 kDa.
A multisubunit complex that is located at the replication origins of a chromosome in the nucleus.
A multisubunit complex that is located at the replication origins of a chromosome in the nucleus.
RNA polymerase II, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces mRNAs, snoRNAs, and some of the snRNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The largest subunit of RNA polymerase II contains an essential carboxyl-terminal domain (CTD) composed of a variable number of heptapeptide repeats (YSPTSPS). The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerases I and III. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
RNA polymerase II, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces mRNAs, snoRNAs, and some of the snRNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The largest subunit of RNA polymerase II contains an essential carboxyl-terminal domain (CTD) composed of a variable number of heptapeptide repeats (YSPTSPS). The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerases I and III. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
RNA polymerase II, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces mRNAs, snoRNAs, and some of the snRNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The largest subunit of RNA polymerase II contains an essential carboxyl-terminal domain (CTD) composed of a variable number of heptapeptide repeats (YSPTSPS). The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerases I and III. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
RNA polymerase III, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces 5S rRNA, tRNAs and some of the small nuclear RNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerase I and others of which are also found in RNA polymerases I and II. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
RNA polymerase III, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces 5S rRNA, tRNAs and some of the small nuclear RNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerase I and others of which are also found in RNA polymerases I and II. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
A protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription.
A RNA polymerase I-specific transcription factor complex that contains the TATA-box-binding protein (TBP) and at least three TBP-associated factors including proteins known in mammals as TAFI110, TAFI63 and TAFI48.
A RNA polymerase I-specific transcription factor complex that contains the TATA-box-binding protein (TBP) and at least three TBP-associated factors including proteins known in mammals as TAFI110, TAFI63 and TAFI48.
A complex composed of TATA binding protein (TBP) and TBP associated factors (TAFs); the total mass is typically about 800 kDa. Most of the TAFs are conserved across species. In TATA-containing promoters for RNA polymerase II (Pol II), TFIID is believed to recognize at least two distinct elements, the TATA element and a downstream promoter element. TFIID is also involved in recognition of TATA-less Pol II promoters. Binding of TFIID to DNA is necessary but not sufficient for transcription initiation from most RNA polymerase II promoters.
A multiprotein complex that possesses histone acetyltransferase and is involved in regulation of transcription. Contains either GCN5 or PCAF in a mutually exclusive manner. The budding yeast complex includes Gcn5p, two proteins of the Ada family, and two TBP-associate proteins (TAFs); analogous complexes in other species have analogous compositions, and usually contain homologs of the yeast proteins. Both ATAC- or SAGA (see GO:0000124, SAGA complex) are involved in the acetylation of histone H3K9 and K14 residues.
A multiprotein complex that possesses histone acetyltransferase and is involved in regulation of transcription. Contains either GCN5 or PCAF in a mutually exclusive manner. The budding yeast complex includes Gcn5p, two proteins of the Ada family, and two TBP-associate proteins (TAFs); analogous complexes in other species have analogous compositions, and usually contain homologs of the yeast proteins. Both ATAC- or SAGA (see GO:0000124, SAGA complex) are involved in the acetylation of histone H3K9 and K14 residues.
A multiprotein complex that possesses histone acetyltransferase and is involved in regulation of transcription. Contains either GCN5 or PCAF in a mutually exclusive manner. The budding yeast complex includes Gcn5p, two proteins of the Ada family, and two TBP-associate proteins (TAFs); analogous complexes in other species have analogous compositions, and usually contain homologs of the yeast proteins. Both ATAC- or SAGA (see GO:0000124, SAGA complex) are involved in the acetylation of histone H3K9 and K14 residues.
A multiprotein complex that possesses histone acetyltransferase and is involved in regulation of transcription. Contains either GCN5 or PCAF in a mutually exclusive manner. The budding yeast complex includes Gcn5p, two proteins of the Ada family, and two TBP-associate proteins (TAFs); analogous complexes in other species have analogous compositions, and usually contain homologs of the yeast proteins. Both ATAC- or SAGA (see GO:0000124, SAGA complex) are involved in the acetylation of histone H3K9 and K14 residues.
A component of the transcription machinery of RNA Polymerase II. In humans, TFIIA is a heterotrimer composed of an alpha (P35), beta (P19) and gamma subunits (P12).
A transcription factor which in humans consists of a complex of two alpha and two beta chains. Recruits TFIIH to the initiation complex and helps activate both RNA polymerase II and TFIIH.
A general transcription initiation factor which in humans consists of a heterodimer of an alpha and a beta subunit. Helps recruit RNA polymerase II to the initiation complex and promotes translation elongation.
A complex that is capable of kinase activity directed towards the C-terminal Domain (CTD) of the largest subunit of RNA polymerase II and is essential for initiation at RNA polymerase II promoters in vitro. It is composed of  the core TFIIH complex and the TFIIK complex.
Any protein complex that mediates changes in chromatin structure that result in transcriptional silencing.
The assembly of DNA, histone proteins, other associated proteins, and sometimes RNA, into chromatin structure, beginning with the formation of the basic unit, the nucleosome, followed by organization of the nucleosomes into higher order structures, ultimately giving rise to a complex organization of specific domains within the nucleus.
A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B.
A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B.
A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B.
Any of a series of ribonucleoprotein complexes that contain snRNA(s) and small nuclear ribonucleoproteins (snRNPs), and are formed sequentially during the spliceosomal splicing of one or more substrate RNAs, and which also contain the RNA substrate(s) from the initial target RNAs of splicing, the splicing intermediate RNA(s), to the final RNA products. During cis-splicing, the initial target RNA is a single, contiguous RNA transcript, whether mRNA, snoRNA, etc., and the released products are a spliced RNA and an excised intron, generally as a lariat structure. During trans-splicing, there are two initial substrate RNAs, the spliced leader RNA and a pre-mRNA.
Any of a series of ribonucleoprotein complexes that contain snRNA(s) and small nuclear ribonucleoproteins (snRNPs), and are formed sequentially during the spliceosomal splicing of one or more substrate RNAs, and which also contain the RNA substrate(s) from the initial target RNAs of splicing, the splicing intermediate RNA(s), to the final RNA products. During cis-splicing, the initial target RNA is a single, contiguous RNA transcript, whether mRNA, snoRNA, etc., and the released products are a spliced RNA and an excised intron, generally as a lariat structure. During trans-splicing, there are two initial substrate RNAs, the spliced leader RNA and a pre-mRNA.
A ribonucleoprotein complex that contains small nuclear RNA U5.
A ribonucleoprotein complex that contains the U7 snRNA and is required for the 3'-end processing of replication-dependent histone pre-mRNAs.
Any spliceosomal complex that forms during the splicing of a messenger RNA primary transcript to excise an intron that has canonical consensus sequences near the 5' and 3' ends.
Any spliceosomal complex that forms during the splicing of a messenger RNA primary transcript to excise an intron that has canonical consensus sequences near the 5' and 3' ends.
Any spliceosomal complex that forms during the splicing of a messenger RNA primary transcript to excise an intron that has canonical consensus sequences near the 5' and 3' ends.
A ribonucleoprotein complex that contains small nuclear RNA U1.
A ribonucleoprotein complex that contains small nuclear RNA U2.
A ribonucleoprotein complex that contains small nuclear RNA U2.
A ribonucleoprotein complex that contains small nuclear RNA U4.
A ribonucleoprotein complex that contains small nuclear RNA U6.
Any spliceosomal complex that forms during the splicing of a messenger RNA primary transcript to excise an intron; the series of U12-type spliceosomal complexes is involved in the splicing of the majority of introns that contain atypical AT-AC terminal dinucleotides, as well as other non-canonical introns. The entire splice site signal, not just the terminal dinucleotides, is involved in determining which spliceosome utilizes the site.
Any spliceosomal complex that forms during the splicing of a messenger RNA primary transcript to excise an intron; the series of U12-type spliceosomal complexes is involved in the splicing of the majority of introns that contain atypical AT-AC terminal dinucleotides, as well as other non-canonical introns. The entire splice site signal, not just the terminal dinucleotides, is involved in determining which spliceosome utilizes the site.
Any spliceosomal complex that forms during the splicing of a messenger RNA primary transcript to excise an intron; the series of U12-type spliceosomal complexes is involved in the splicing of the majority of introns that contain atypical AT-AC terminal dinucleotides, as well as other non-canonical introns. The entire splice site signal, not just the terminal dinucleotides, is involved in determining which spliceosome utilizes the site.
A ribonucleoprotein complex that contains small nuclear RNA U4atac.
A ribonucleoprotein complex that contains small nuclear RNA U6atac.
A ribonucleoprotein complex that contains small nuclear RNA U11.
A ribonucleoprotein complex that contains small nuclear RNA U11.
A ribonucleoprotein complex that contains small nuclear RNA U12.
A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
Telomerase is a ribonucleoprotein enzyme complex, with a minimal catalytic core composed of a catalytic reverse transcriptase subunit and an RNA subunit that provides the template for telomeric DNA addition. In vivo, the holoenzyme complex often contains additional subunits.
A type of chromosome in a polyploid cell, formed when multiple copies of homologous chromosomes are aligned side by side to give a giant chromosome in which distinct chromosome bands are readily visible.
A region at which the centric regions of polytene chromosomes are joined together.
A region of the polytene chromosome where the diameter is considerably decreased, probably resulting from local differences in chromosome organization.
A swelling at a site along the length of a polytene chromosome, thought to be the site of active transcription.
A stretch of densely packed chromatin along the polytene chromosome, visible as a morphologically distinct band.
A stretch of less tightly packed chromatin along the polytene chromosome, found between bands.
A thread-like connection joining two regions of ectopically paired polytene chromosomes.
A connection formed between chromatids, visible during meiosis, thought to be the point of the interchange involved in crossing-over.
An electron dense structure that is associated with meiotic chromosomes.
An electron dense structure that is associated with meiotic chromosomes in leptotene or zygotene during meiosis I.
An electron dense structure that is associated with meiotic chromosomes in pachytene during meiosis I.
The dispersed less dense form of chromatin in the interphase nucleus. It exists in at least two forms, a some being in the form of transcriptionally active chromatin which is the least condensed, while the rest is inactive euchromatin which is more condensed than active chromatin but less condensed than heterochromatin.
A condensed form of chromatin, occurring in the nucleus during interphase, that stains strongly with basophilic dyes. The DNA of heterochromatin is typically replicated at a later stage in the cell-division cycle than euchromatin.
Heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
Heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
A diffusely banded region of heterochromatin located between euchromatin and alpha-heterochromatin in the polytene chromosome chromocenter; normally replicated during polytenization.
A small, compact region of heterochromatin located in the middle of the polytene chromosome chromocenter, which undergoes little or no replication during polytenization.
Heterochromatic regions of the chromosome found at the telomeres of a chromosome in the nucleus.
Any of the regions of heterochromatin that form a reproducible set of dense bands scattered along the euchromatic arms in polytene chromosomes.
Structures of variable diameter visible in the nucleoplasm by electron microscopy, mainly observed near the border of condensed chromatin. The fibrils are enriched in RNA, and are believed to be sites of pre-mRNA splicing and polyadenylylation representing the in situ form of nascent transcripts.
Circular DNA molecules encoding ribosomal RNA that are replicated independently of chromosomal replication. These molecules originate in the chromosome but are excised and circularized, often by intramolecular homologous recombination between direct tandem repeats.
A plasmid commonly found in Saccharomyces, inherited in a non-Mendelian manner and often present in 100-400 copies.
A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
A region of a chromosome where nucleoli form during interphase, and where genes encoding the largest rRNA precursor transcript are tandemly arrayed.
A region of a chromosome where nucleoli form during interphase, and where genes encoding the largest rRNA precursor transcript are tandemly arrayed.
A region of a chromosome where nucleoli form during interphase, and where genes encoding the largest rRNA precursor transcript are tandemly arrayed.
A ribonucleoprotein complex that contains an RNA molecule of the small nucleolar RNA (snoRNA) family and associated proteins. Most are involved in a step of processing of rRNA: cleavage, 2'-O-methylation, or pseudouridylation. The majority, though not all, fall into one of two classes, box C/D type or box H/ACA type.
A ribonucleoprotein complex that contains an RNA molecule of the small nucleolar RNA (snoRNA) family and associated proteins. Most are involved in a step of processing of rRNA: cleavage, 2'-O-methylation, or pseudouridylation. The majority, though not all, fall into one of two classes, box C/D type or box H/ACA type.
RNA polymerase I, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces rRNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerase III and others of which are also found in RNA polymerases II and III. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
RNA polymerase I, one of three nuclear DNA-directed RNA polymerases found in all eukaryotes, is a multisubunit complex; typically it produces rRNAs. Two large subunits comprise the most conserved portion including the catalytic site and share similarity with other eukaryotic and bacterial multisubunit RNA polymerases. The remainder of the complex is composed of smaller subunits (generally ten or more), some of which are also found in RNA polymerase III and others of which are also found in RNA polymerases II and III. Although the core is competent to mediate ribonucleic acid synthesis, it requires additional factors to select the appropriate template.
The double lipid bilayer enclosing the mitochondrion and separating its contents from the cell cytoplasm; includes the intermembrane space.
The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
A large complex of the mitochondrial outer membrane that mediates transport of proteins into all mitochondrial compartments.
A large complex of the mitochondrial outer membrane that mediates transport of proteins into all mitochondrial compartments.
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
The protein transport machinery of the mitochondrial inner membrane that typically transports proteins that possess a matrix-targeting N-terminal presequence. The TIM23 complex contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.
The protein transport machinery of the mitochondrial inner membrane that typically transports proteins that possess a matrix-targeting N-terminal presequence. The TIM23 complex contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.
The protein transport machinery of the mitochondrial inner membrane that typically transports proteins that possess a matrix-targeting N-terminal presequence. The TIM23 complex contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.
The protein transport machinery of the mitochondrial inner membrane that typically transports proteins that possess a matrix-targeting N-terminal presequence. The TIM23 complex contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.
Protease complex of the mitochondrial inner membrane that is involved in mitochondrial protein turnover and in processing of proteins imported into mitochondria.
The protein complexes that form the mitochondrial electron transport system (the respiratory chain), associated with the inner mitochondrial membrane. The respiratory chain complexes transfer electrons from an electron donor to an electron acceptor and are associated with a proton pump to create a transmembrane electrochemical gradient.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. It contains about 25 different polypeptide subunits, including NADH dehydrogenase (ubiquinone), flavin mononucleotide and several different iron-sulfur clusters containing non-heme iron. The iron undergoes oxidation-reduction between Fe(II) and Fe(III), and catalyzes proton translocation linked to the oxidation of NADH by ubiquinone.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2).
A proton-transporting ATP synthase complex found in the mitochondrial membrane.
A proton-transporting ATP synthase complex found in the mitochondrial membrane.
The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.
All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.
All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.
All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.
One of two stalks that connect the catalytic core of the hydrogen-transporting ATP synthase to the mitochondrial membrane-associated F0 proteins; rotates within the catalytic core during catalysis.
A protein complex that connects the inner and outer membranes of animal mitochondria and acts as a pore that can open transiently to allow free diffusion of solutes between the mitochondrial matrix and the cytosol. The pore complex is formed of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocase (ANT) and cyclophilin-D (CyP-D).
A protein complex that connects the inner and outer membranes of animal mitochondria and acts as a pore that can open transiently to allow free diffusion of solutes between the mitochondrial matrix and the cytosol. The pore complex is formed of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocase (ANT) and cyclophilin-D (CyP-D).
A protein complex that connects the inner and outer membranes of animal mitochondria and acts as a pore that can open transiently to allow free diffusion of solutes between the mitochondrial matrix and the cytosol. The pore complex is formed of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocase (ANT) and cyclophilin-D (CyP-D).
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
The region between the inner and outer lipid bilayers of the mitochondrial envelope.
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
A DNA polymerase complex consisting of a large subunit, responsible for the catalytic activities, and a small accessory subunit. Functions in the replication and repair of mitochondrial DNA.
A ribosome found in the mitochondrion of a eukaryotic cell; contains a characteristic set of proteins distinct from those of cytosolic ribosomes.
The larger of the two subunits of a mitochondrial ribosome. Two sites on the ribosomal large subunit are involved in translation: the aminoacyl site (A site) and peptidyl site (P site).
The smaller of the two subunits of a mitochondrial ribosome.
The smaller of the two subunits of a mitochondrial ribosome.
The smaller of the two subunits of a mitochondrial ribosome.
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
A lysosome before it has fused with a vesicle or vacuole.
Vacuole formed by the fusion of a lysosome with an organelle (autosome) or with a primary phagosome.
A vacuole to which materials ingested by endocytosis are delivered.
A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell.
The volume enclosed within the vacuolar membrane.
A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy.
The lipid bilayer surrounding a peroxisome.
The component of the peroxisomal membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of the intraperoxisomal membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
The component of the intraperoxisomal membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
The process of directing proteins towards the peroxisome, usually using signals contained within the protein.
Any constituent part of a peroxisome, a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules; contains some enzymes that produce and others that degrade hydrogen peroxide (H2O2).
The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
A translocon complex that contains a core heterotrimer of conserved alpha, beta and gamma subunits, and may contain additional proteins (translocon-associated proteins or TRAPs); in budding yeast the core proteins are Sec61p, Sbh1p, and Sss1p. The Sec61 translocon complex functions in cotranslational and posttranslational translocation events.
A transmembrane heterodimeric protein located in the membrane of the rough endoplasmic reticulum. Both subunits contain GTPase domains with which signal recognition particle interacts. In the presence of GTP and SRP receptor, SRP is released from the ribosome-nascent chain complex.
A transmembrane heterodimeric protein located in the membrane of the rough endoplasmic reticulum. Both subunits contain GTPase domains with which signal recognition particle interacts. In the presence of GTP and SRP receptor, SRP is released from the ribosome-nascent chain complex.
A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana.
A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana.
A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana.
A protein complex that is located in the endoplasmic reticulum membrane and cleaves the signal sequence from precursor proteins following their transport out of the cytoplasmic space.
The volume enclosed by the membranes of the endoplasmic reticulum.
The volume enclosed by the membranes of the endoplasmic reticulum.
The volume enclosed by the membranes of the endoplasmic reticulum.
The volume enclosed by the membranes of the endoplasmic reticulum.
The volume enclosed by the membranes of the endoplasmic reticulum.
The lipid bilayer surrounding the endoplasmic reticulum.
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi  and Golgi-to-ER transport.
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks.
The middle Golgi cisterna (or cisternae).
Any vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell.
Any vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell.
One of two multimeric complexes that forms a membrane vesicle coat. The mammalian COPI subunits are called alpha-, beta-, beta'-, gamma-, delta-, epsilon- and zeta-COP. Vesicles with COPI coats are found associated with Golgi membranes at steady state.
One of two multimeric complexes that forms a membrane vesicle coat. The mammalian COPI subunits are called alpha-, beta-, beta'-, gamma-, delta-, epsilon- and zeta-COP. Vesicles with COPI coats are found associated with Golgi membranes at steady state.
A vesicle with a coat formed of the COPI coat complex proteins. COPI-coated vesicles are found associated with Golgi membranes at steady state, are involved in Golgi to endoplasmic reticulum (retrograde) vesicle transport, and possibly also in intra-Golgi transport.
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
A vesicle with a coat formed of the COPII coat complex proteins. The COPII coat complex is formed by the Sec23p/Sec24p and the Sec13p/Sec31p heterodimers. COPII-associated vesicles transport proteins from the rough endoplasmic reticulum to the Golgi apparatus (anterograde transport).
The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum.
The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum.
The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum.
The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum.
The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
Any of the vesicles of the constitutive secretory pathway, which carry cargo from the endoplasmic reticulum to the Golgi, between Golgi cisternae, from the Golgi to the ER (retrograde transport) or to destinations within or outside the cell.
Any of the vesicles of the constitutive secretory pathway, which carry cargo from the endoplasmic reticulum to the Golgi, between Golgi cisternae, from the Golgi to the ER (retrograde transport) or to destinations within or outside the cell.
Any of the vesicles of the constitutive secretory pathway, which carry cargo from the endoplasmic reticulum to the Golgi, between Golgi cisternae, from the Golgi to the ER (retrograde transport) or to destinations within or outside the cell.
Any of the vesicles of the constitutive secretory pathway, which carry cargo from the endoplasmic reticulum to the Golgi, between Golgi cisternae, from the Golgi to the ER (retrograde transport) or to destinations within or outside the cell.
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
The lipid bilayer surrounding a transport vesicle.
The lipid bilayer surrounding a transport vesicle.
The lipid bilayer surrounding a secretory granule.
A vesicle that mediates transport from the Golgi to the endoplasmic reticulum.
A vesicle that mediates transport from the Golgi to the endoplasmic reticulum.
A vesicle that mediates transport from the Golgi to the endoplasmic reticulum.
A vesicle that mediates transport from the Golgi to the endoplasmic reticulum.
A vesicle that mediates transport from the Golgi to the endoplasmic reticulum.
A membrane-bounded intracellular vesicle formed by invagination of the plasma membrane around an extracellular substance. Endocytic vesicles fuse with early endosomes to deliver the cargo for further sorting.
A membrane-bounded intracellular vesicle formed by invagination of the plasma membrane around an extracellular substance. Endocytic vesicles fuse with early endosomes to deliver the cargo for further sorting.
An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.
A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle.
A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle.
An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.
An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.
The microtubule organizing center in fungi; functionally homologous to the animal cell centrosome.
An array of microtubules emanating from a spindle pole MTOC that do not connect to kinetochores.
The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart.
Structure between the central and outer plaques of the spindle pole body.
One of three laminate structures that form the spindle pole body; the inner plaque is in the nucleus.
One of three laminate structures that form the spindle pole body; the central plaque is embedded in the nuclear envelope.
One of three laminate structures that form the spindle pole body; the outer plaque is in the cytoplasm.
Structure adjacent to the plaques of the spindle pole body.
A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane.  In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane.  In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane.  In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane.  In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane.  In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
A cytoskeletal structure composed of actin filaments and myosin that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the spindle, i.e. the cell division plane.  In animal cells, the contractile ring is located at the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the contractile ring forms at the mother-bud neck before mitosis.
Any of the spindle microtubules that come from each pole and overlap at the spindle midzone. This interdigitating structure consisting of antiparallel microtubules is responsible for pushing the poles of the spindle apart.
Any of the spindle microtubules that attach to the kinetochores of chromosomes by their plus ends, and maneuver the chromosomes during mitotic or meiotic chromosome segregation.
A protein complex consisting of a steroid receptor associated with nonreceptor proteins, minimally a dimer of Hsp90 and a monomer of hsp56/FKBP59; forms in the absence of bound ligand.
A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor.
A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor.
An iron-containing, oxygen carrying complex. In vertebrates it is made up of two pairs of associated globin polypeptide chains, each chain carrying a noncovalently bound heme prosthetic group.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A multienzyme complex that catalyses the synthesis of fatty acids from acetyl CoA.
A protein complex that possesses fatty-acyl-CoA synthase activity.
A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes and unfolds ubiquitinated proteins, and translocates them to the proteasome core complex.
A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes and unfolds ubiquitinated proteins, and translocates them to the proteasome core complex.
A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes and unfolds ubiquitinated proteins, and translocates them to the proteasome core complex.
A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes and unfolds ubiquitinated proteins, and translocates them to the proteasome core complex.
A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro.
Any protein complex that binds to an mRNA cap at any time in the lifetime of the mRNA.
A conserved heterodimeric protein complex that binds to the 5' terminal cap structure m7G(5')ppp(5')N of nascent eukaryotic RNA polymerase II transcripts such as pre-mRNA and U snRNA. The consists of proteins known as CBP20 and CBP80, binds to cap structures in the nucleus, and is involved in pre-mRNA splicing, 3'-end formation, and RNA nuclear export.
A conserved heterodimeric protein complex that binds to the 5' terminal cap structure m7G(5')ppp(5')N of nascent eukaryotic RNA polymerase II transcripts such as pre-mRNA and U snRNA. The consists of proteins known as CBP20 and CBP80, binds to cap structures in the nucleus, and is involved in pre-mRNA splicing, 3'-end formation, and RNA nuclear export.
A conserved heterodimeric protein complex that binds to the 5' terminal cap structure m7G(5')ppp(5')N of nascent eukaryotic RNA polymerase II transcripts such as pre-mRNA and U snRNA. The consists of proteins known as CBP20 and CBP80, binds to cap structures in the nucleus, and is involved in pre-mRNA splicing, 3'-end formation, and RNA nuclear export.
A conserved heterodimeric protein complex that binds to the 5' terminal cap structure m7G(5')ppp(5')N of nascent eukaryotic RNA polymerase II transcripts such as pre-mRNA and U snRNA. The consists of proteins known as CBP20 and CBP80, binds to cap structures in the nucleus, and is involved in pre-mRNA splicing, 3'-end formation, and RNA nuclear export.
A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.
A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.
A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.
A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.
A protein complex required for mRNA cleavage but not for poly(A) addition.
A protein complex required for mRNA cleavage but not for poly(A) addition.
Any macromolecular complex involved in cleavage or polyadenylation of mRNA molecules.
Complex of three heterogeneous polypeptide chains, that form a ternary complex with initiator methionyl-tRNA and GTP. This ternary complex binds to free 40S subunit, which subsequently binds the 5' end of mRNA.
Complex of three heterogeneous polypeptide chains, that form a ternary complex with initiator methionyl-tRNA and GTP. This ternary complex binds to free 40S subunit, which subsequently binds the 5' end of mRNA.
A multisubunit guanine nucleotide exchange factor which catalyzes the exchange of GDP bound to initiation factor eIF2 for GTP, generating active eIF2-GTP. In humans, it is composed of five subunits, alpha, beta, delta, gamma and epsilon.
A multisubunit guanine nucleotide exchange factor which catalyzes the exchange of GDP bound to initiation factor eIF2 for GTP, generating active eIF2-GTP. In humans, it is composed of five subunits, alpha, beta, delta, gamma and epsilon.
A complex of several polypeptides that plays at least two important roles in protein synthesis: First, eIF3 binds to the 40S ribosome and facilitates loading of the Met-tRNA/eIF2.GTP ternary complex to form the 43S preinitiation complex. Subsequently, eIF3 apparently assists eIF4 in recruiting mRNAs to the 43S complex. The eIF3 complex contains five conserved core subunits, and may contain several additional proteins; the non-core subunits are thought to mediate association of the complex with specific sets of mRNAs.
A complex of several polypeptides that plays at least two important roles in protein synthesis: First, eIF3 binds to the 40S ribosome and facilitates loading of the Met-tRNA/eIF2.GTP ternary complex to form the 43S preinitiation complex. Subsequently, eIF3 apparently assists eIF4 in recruiting mRNAs to the 43S complex. The eIF3 complex contains five conserved core subunits, and may contain several additional proteins; the non-core subunits are thought to mediate association of the complex with specific sets of mRNAs.
A multisubunit nucleotide exchange complex that binds GTP and aminoacyl-tRNAs, and catalyzes their codon-dependent placement at the A-site of the ribosome. In humans, the complex is composed of four subunits, alpha, beta, delta and gamma.
A heterodimeric protein complex that can reversibly bind to ribosomes, and is located in direct proximity to newly synthesized polypeptide chains as they emerge from the ribosome.
A heterodimeric protein complex that can reversibly bind to ribosomes, and is located in direct proximity to newly synthesized polypeptide chains as they emerge from the ribosome.
Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
A filament of myosin found in a muscle cell of any type.
A complex of accessory proteins (typically troponin T, troponin I and troponin C) found associated with actin in muscle thin filaments; involved in calcium regulation of muscle contraction.
A form of the tropomyosin dimer found associated with actin and the troponin complex in muscle thin filaments.
Bipolar filaments formed of polymers of a muscle-specific myosin II isoform, found in the middle of sarcomeres in myofibrils.
Filaments formed of actin and associated proteins; attached to Z discs at either end of sarcomeres in myofibrils.
A 20S multiprotein assembly of total mass about 1.2 MDa that activates dynein-based activity in vivo. A large structural component of the complex is an actin-like 40 nm filament composed of actin-related protein, to which other components attach.
A heterodimer consisting of alpha and beta subunits that binds to and caps the barbed ends of actin filaments, nucleates the polymerization of actin monomers but does not sever actin filaments, and which is a part of the dynactin complex.
Any complex that includes a dimer of molecules from the kinesin superfamily, a group of related proteins that contain an extended region of predicted alpha-helical coiled coil in the main chain that likely produces dimerization. The native complexes of several kinesin family members have also been shown to contain additional peptides, often designated light chains as all of the noncatalytic subunits that are currently known are smaller than the chain that contains the motor unit. Kinesin complexes generally possess a force-generating enzymatic activity, or motor, which converts the free energy of the gamma phosphate bond of ATP into mechanical work.
Any complex that includes a dimer of molecules from the kinesin superfamily and any associated proteins, and moves towards the minus end of a microtubule.
Any complex that includes a dimer of molecules from the kinesin superfamily and any associated proteins, and moves towards the plus end of a microtubule.
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
Any multimeric complex connected to a microtubule.
Any microtubule that is part of a mitotic or meiotic spindle; anchored at one spindle pole.
A microtubule in the axoneme of a eukaryotic cilium or flagellum; an axoneme contains nine modified doublet microtubules, which may or may not surround a pair of single microtubules.
Any microtubule in the nucleus of a cell.
Any microtubule in the cytoplasm of a cell.
A type of intermediate filament found in the core of neuronal axons. Neurofilaments are heteropolymers composed of three type IV polypeptides: NF-L, NF-M, and NF-H (for low, middle, and high molecular weight). Neurofilaments are responsible for the radial growth of an axon and determine axonal diameter.
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
A stable protein complex that contains two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5), and functions in the nucleation of branched actin filaments.
A protein complex that possesses hydrogen:potassium-exchanging ATPase activity; characterized in animal cells, where it maintains ionic gradients of K+ at the expense of ATP hydrolysis; The complex contains two obligatory subunits, the catalytic alpha subunit and a glycosylated beta subunit; two additional subunits, gamma and channel-inducing factor (CHIF), may also be present.
A protein complex that possesses hydrogen:potassium-exchanging ATPase activity; characterized in animal cells, where it maintains ionic gradients of K+ at the expense of ATP hydrolysis; The complex contains two obligatory subunits, the catalytic alpha subunit and a glycosylated beta subunit; two additional subunits, gamma and channel-inducing factor (CHIF), may also be present.
A protein complex that possesses hydrogen:potassium-exchanging ATPase activity; characterized in animal cells, where it maintains ionic gradients of K+ at the expense of ATP hydrolysis; The complex contains two obligatory subunits, the catalytic alpha subunit and a glycosylated beta subunit; two additional subunits, gamma and channel-inducing factor (CHIF), may also be present.
Sodium:potassium-exchanging ATPases are tetrameric proteins, consisting of two large alpha subunits and two smaller beta subunits. The alpha subunits bear the active site and penetrate the membrane, while the beta subunits carry oligosaccharide groups and face the cell exterior.
Sodium:potassium-exchanging ATPases are tetrameric proteins, consisting of two large alpha subunits and two smaller beta subunits. The alpha subunits bear the active site and penetrate the membrane, while the beta subunits carry oligosaccharide groups and face the cell exterior.
A protein complex that forms a transmembrane channel through which calcium ions may pass in response to changes in membrane potential.
A protein complex that forms a transmembrane channel through which calcium ions may pass in response to changes in membrane potential.
A protein complex that forms a transmembrane channel through which calcium ions may pass in response to changes in membrane potential.
A homo- or hetero-pentameric protein complex that forms a transmembrane channel through which ions may pass in response to acetylcholine binding.
A homo- or hetero-pentameric protein complex that forms a transmembrane channel through which ions may pass in response to acetylcholine binding.
A protein complex that binds interleukin-2; comprises alpha, beta, and gamma subunits.
A protein complex that binds interleukin-3; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-3 receptor, whereas the beta chain is shared with the receptors for granulocyte-macrophage colony-stimulating factor and interleukin-5.
A protein complex that binds interleukin-3; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-5 receptor, whereas the beta chain is shared with the receptors for granulocyte-macrophage colony-stimulating factor and interleukin-3.
A hexameric protein complex consisting of two molecules each of interleukin-6, interleukin-6 receptor alpha chain, and gp-130.
A protein complex that binds interleukin-9; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-9 receptor, whereas the beta chain is shared with the receptors for several other interleukins.
A protein complex that binds interleukin-13; consists of two chains, interleukin-13 receptor alpha1 chain and interleukin-4 receptor alpha chain.
A disulfide-bonded, heterotetrameric receptor complex. The alpha chains are entirely extracellular, while each beta chain has one transmembrane domain. The ligand binds to the alpha subunit extracellular domain and the kinase is associated with the beta subunit intracellular domain.
A heterodimeric receptor for the cytokine oncostatin-M (OSM). In humans the receptor complex is made up of the gene products gp130 and OSMR-beta.
A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis.  Caveolae may be pinched off to form free vesicles within the cytoplasm.
A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis.  Caveolae may be pinched off to form free vesicles within the cytoplasm.
A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis.  Caveolae may be pinched off to form free vesicles within the cytoplasm.
Thin cylindrical membrane-covered projections on the surface of an animal cell containing a core bundle of actin filaments. Present in especially large numbers on the absorptive surface of intestinal cells.
The dense covering of microvilli on the apical surface of a epithelial cells in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes.
Any of several heterotetrameric complexes that link clathrin (or another coat-forming molecule, as hypothesized for AP-3 and AP-4) to a membrane surface; they are found on coated pits and coated vesicles, and mediate sorting of cargo proteins into vesicles. Each AP complex contains two large (a beta and one of either an alpha, gamma, delta, or epsilon) subunits (110-130 kDa), a medium (mu) subunit (approximately 50 kDa), and a small (sigma) subunit (15-20 kDa).
A heterotetrameric AP-type membrane coat adaptor complex that consists of beta1, gamma, mu1 and sigma1 subunits and links clathrin to the membrane surface of a vesicle; vesicles with AP-1-containing coats are normally found primarily in the trans-Golgi network. In at least humans, the AP-1 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (gamma1 and gamma2, mu1A and mu1B, and sigma1A, sigma1B and sigma1C).
A heterotetrameric AP-type membrane coat adaptor complex that consists of beta1, gamma, mu1 and sigma1 subunits and links clathrin to the membrane surface of a vesicle; vesicles with AP-1-containing coats are normally found primarily in the trans-Golgi network. In at least humans, the AP-1 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (gamma1 and gamma2, mu1A and mu1B, and sigma1A, sigma1B and sigma1C).
A heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits, and links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. Vesicles with AP-2-containing coats are normally found primarily near the plasma membrane, on endocytic vesicles. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC).
A heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits, and links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. Vesicles with AP-2-containing coats are normally found primarily near the plasma membrane, on endocytic vesicles. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC).
A cell junction that forms a connection between two or more cells in a multicellular organism; excludes direct cytoplasmic junctions such as ring canals.
A cell junction at which anchoring proteins (cadherins or integrins) extend through the plasma membrane and are attached to actin filaments.
An adherens junction which connects a cell to another cell.
A small cell-cell adherens junction assembled during the cellularization stage of insect embyrogenesis; spot adherens junctions later fuse to form the zonula adherens.
A small cell-cell adherens junction assembled during the cellularization stage of insect embyrogenesis; spot adherens junctions later fuse to form the zonula adherens.
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
A cell-cell adherens junction which forms a continuous belt near the apex of epithelial cells.
A cell-cell adherens junction that contains the transmembrane protein N-cadherin, which interacts with identical molecules from neighboring cells to form a tight mechanical intercellular link; forms a large portion of the intercalated disc, the structure at which myofibrils terminate in cardiomyocytes.
A specialized cell-cell junction found between nephrocytes of the insect kidney, which is adapted for filtration of hemolymph. The insect nephrocyte is anatomically and functionally similar to the glomerular podocyte of vertebrates.
A cell-cell junction that forms a continuous band around each cell in an epithelium; within the septate junction the membranes of adjacent cells maintain a constant distance of approximately 15 nm; found in arthropods.
A septate junction in which regular arrays of electron-dense septae span the intermembrane space.
A septate junction that lacks the regular arrays of electron-dense septae found in pleated septate junctions.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
An assembly of six molecules of connexin, made in the Golgi apparatus and subsequently transported to the plasma membrane, where docking of two connexons on apposed plasma membranes across the extracellular space forms a gap junction.
An assembly of six molecules of connexin, made in the Golgi apparatus and subsequently transported to the plasma membrane, where docking of two connexons on apposed plasma membranes across the extracellular space forms a gap junction.
An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes.
An adherens junction which connects a cell to the extracellular matrix.
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
A cell-substrate adherens junction, also known as a hemiadherens junction (HAJ) that forms one of a pair of junctions in opposing cells that are separated by only 30-40nm, with a thin line of extracellular electron-dense material in between; found where muscles attach to epidermal cells directly (in insects).
A cell-substrate junction found at the terminal anchorage site of skeletal muscle cells to tendons.
A cell-substrate adherens junction found in the apical region of a cell, such as those found in cuticle-secreting epithelia, which connect the apical membrane to the cuticle.
A cell-substrate adherens junction found in the apical region of a cell, such as those found in cuticle-secreting epithelia, which connect the apical membrane to the cuticle.
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
A protein complex found in the axoneme of eukaryotic cilia and flagella. It forms interconnections between the microtubule outer doublets that surround the inner central pair of microtubules.
A protein complex found in the axoneme of eukaryotic cilia and flagella. It forms interconnections between the microtubule outer doublets that surround the inner central pair of microtubules.
A protuberance from a cell of an organism that reproduces by budding, which will grow larger and become a separate daughter cell after nuclear division, cytokinesis, and cell wall formation (when appropriate). The daughter cell may completely separate from the mother cell, or the mother and daughter cells may remain associated.
The end of a cellular bud distal to the site of attachment to the mother cell.
The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
The projection formed by unicellular fungi in response to mating pheromone.
The projection formed by unicellular fungi in response to mating pheromone.
The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
A tight ring-shaped structure that forms in the division plane at the site of cytokinesis; composed of members of the conserved family of filament-forming proteins called septins as well as septin-associated proteins. This type of septin structure is observed at the bud neck of budding fungal cells, at the site of cell division in animal cells, at the junction between the mother cell and a pseudohyphal projection, and also within hyphae of filamentous fungi at sites where a septum will form.
A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too.
A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too.
A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too.
A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too.
A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too.
A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IA phosphoinositide 3-kinase (PI3K) subunit and an associated SH2 domain-containing regulatory subunit that is a member of a family of related proteins often called p85 proteins. Through the interaction with the SH2-containing adaptor subunits, Class IA PI3K catalytic subunits are linked to tyrosine kinase signaling pathways.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IA phosphoinositide 3-kinase (PI3K) subunit and an associated SH2 domain-containing regulatory subunit that is a member of a family of related proteins often called p85 proteins. Through the interaction with the SH2-containing adaptor subunits, Class IA PI3K catalytic subunits are linked to tyrosine kinase signaling pathways.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IA phosphoinositide 3-kinase (PI3K) subunit and an associated SH2 domain-containing regulatory subunit that is a member of a family of related proteins often called p85 proteins. Through the interaction with the SH2-containing adaptor subunits, Class IA PI3K catalytic subunits are linked to tyrosine kinase signaling pathways.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IA phosphoinositide 3-kinase (PI3K) subunit and an associated SH2 domain-containing regulatory subunit that is a member of a family of related proteins often called p85 proteins. Through the interaction with the SH2-containing adaptor subunits, Class IA PI3K catalytic subunits are linked to tyrosine kinase signaling pathways.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IA phosphoinositide 3-kinase (PI3K) subunit and an associated SH2 domain-containing regulatory subunit that is a member of a family of related proteins often called p85 proteins. Through the interaction with the SH2-containing adaptor subunits, Class IA PI3K catalytic subunits are linked to tyrosine kinase signaling pathways.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IB phosphoinositide 3-kinase (PI3K) subunit and an associated regulatory subunit that is larger than, and unrelated to, the p85 proteins present in class IA complexes. Class IB PI3Ks are stimulated by G-proteins and do not interact with the SH2-domain containing adaptors that bind to Class IA PI3Ks.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IB phosphoinositide 3-kinase (PI3K) subunit and an associated regulatory subunit that is larger than, and unrelated to, the p85 proteins present in class IA complexes. Class IB PI3Ks are stimulated by G-proteins and do not interact with the SH2-domain containing adaptors that bind to Class IA PI3Ks.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IB phosphoinositide 3-kinase (PI3K) subunit and an associated regulatory subunit that is larger than, and unrelated to, the p85 proteins present in class IA complexes. Class IB PI3Ks are stimulated by G-proteins and do not interact with the SH2-domain containing adaptors that bind to Class IA PI3Ks.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IB phosphoinositide 3-kinase (PI3K) subunit and an associated regulatory subunit that is larger than, and unrelated to, the p85 proteins present in class IA complexes. Class IB PI3Ks are stimulated by G-proteins and do not interact with the SH2-domain containing adaptors that bind to Class IA PI3Ks.
A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IB phosphoinositide 3-kinase (PI3K) subunit and an associated regulatory subunit that is larger than, and unrelated to, the p85 proteins present in class IA complexes. Class IB PI3Ks are stimulated by G-proteins and do not interact with the SH2-domain containing adaptors that bind to Class IA PI3Ks.
A protein complex that possesses 6-phosphofructokinase activity; homodimeric, homooctameric, and allosteric homotetrameric forms are known.
A protein complex that possesses alpha,alpha-trehalose-phosphate synthase (UDP-forming) and trehalose-phosphatase activities, and thus catalyzes two reactions in trehalose biosynthesis. In the complex identified in Saccharomyces, Tps1p has alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity, Tps2p has trehalose 6-phosphate phosphatase activity; Tps3p is a regulatory subunit, and an additional subunit, Tsl1p, may be present.
A protein complex that possesses alpha,alpha-trehalose-phosphate synthase (UDP-forming) and trehalose-phosphatase activities, and thus catalyzes two reactions in trehalose biosynthesis. In the complex identified in Saccharomyces, Tps1p has alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity, Tps2p has trehalose 6-phosphate phosphatase activity; Tps3p is a regulatory subunit, and an additional subunit, Tsl1p, may be present.
A protein complex that possesses alpha,alpha-trehalose-phosphate synthase (UDP-forming) and trehalose-phosphatase activities, and thus catalyzes two reactions in trehalose biosynthesis. In the complex identified in Saccharomyces, Tps1p has alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity, Tps2p has trehalose 6-phosphate phosphatase activity; Tps3p is a regulatory subunit, and an additional subunit, Tsl1p, may be present.
Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate.
A heterotetrameric enzyme complex made up of two components I and two components II. Catalyzes the formation of anthranilate, pyruvate and L-glutamate from chorismate and L-glutamine.
A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events.
A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events.
A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events.
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer.
A heterodimeric enzyme, composed of an alpha and a beta subunit. Participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane.
An enzyme complex which in eukaryotes is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Catalyzes the phosphorylation of proteins to O-phosphoproteins.
An enzyme complex which in eukaryotes is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Catalyzes the phosphorylation of proteins to O-phosphoproteins.
An enzyme complex which in eukaryotes is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Catalyzes the phosphorylation of proteins to O-phosphoproteins.
A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin.
A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin.
A protein complex that possesses protein serine/threonine kinase activity, and contains two catalytic alpha subunits and two regulatory beta subunits. Protein kinase CK2 complexes are found in nearly every subcellular compartment, and can phosphorylate many protein substrates in addition to casein.
A protein complex whose composition varies amongst species; in rice it probably exists in a homo-tetramer to homo-hexamer form and in Gram-negative bacteria as a dimer. Functions in the hydrolysis of alpha-(1,6)-D-glucosidic branch linkages.
A large protein complex which is involved in the repair of DNA double-strand breaks and, in mammals, V(D)J recombination events. It consists of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), the DNA end-binding heterodimer Ku, the nuclear phosphoprotein XRCC4 or a homolog thereof, and DNA ligase IV.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
Mitochondrial complex that possesses isocitrate dehydrogenase (NAD+) activity.
An enzyme complex that catalyzes the removal of serine- or threonine-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase.
An enzyme complex that catalyzes the phosphorylation of phosphorylase b to form phosphorylase a.
A protein complex that possesses protein farnesyltransferase activity.
An enzyme complex that catalyzes the hydrolysis of bonds in a cyclic nucleotide.
Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The This Eukaryotic form usually contains more subunits than its bacterial counterpart; for example, one known complex contains 30 E1 dimers, 60 E2 monomers, and 6 E3 dimers as well as a few copies of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase.
A heterodimeric enzyme complex, which in mammals is composed of an alpha and a beta subunit, and which associates with an accessory protein Rep (Rab escort protein). Catalyzes of the transfer of a geranyl-geranyl group from geranylgeranyl pyrophosphate to a Rab protein.
A heterodimeric enzyme complex, which in mammals is composed of an alpha and a beta subunit, and which associates with an accessory protein Rep (Rab escort protein). Catalyzes of the transfer of a geranyl-geranyl group from geranylgeranyl pyrophosphate to a Rab protein.
A heterodimeric enzyme complex, which in mammals is composed of an alpha and a beta subunit, and which associates with an accessory protein Rep (Rab escort protein). Catalyzes of the transfer of a geranyl-geranyl group from geranylgeranyl pyrophosphate to a Rab protein.
A heterodimeric enzyme complex, which in mammals is composed of an alpha and a beta subunit, and which associates with an accessory protein Rep (Rab escort protein). Catalyzes of the transfer of a geranyl-geranyl group from geranylgeranyl pyrophosphate to a Rab protein.
An enzyme complex that catalyzes the formation of hydroxypyruvate and alanine from serine and pyruvate.
An enzyme complex that catalyzes the formation of hydroxypyruvate and alanine from serine and pyruvate.
An enzyme complex that catalyzes the formation of hydroxypyruvate and alanine from serine and pyruvate.
An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor.
An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor.
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
The chemical reactions and pathways involving a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
The chemical reactions and pathways involving a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
The chemical reactions and pathways involving a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
The chemical reactions and pathways involving a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
The chemical reactions and pathways involving a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages.
The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glycogen.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glycogen.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glycogen.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glycogen.
The chemical reactions and pathways involving starch, the most important reserve polysaccharide in plants. It is a glucan consisting of two components, amylose and amylopectin, which are both glucose homopolymers. Starch is synthesized as a temporary storage form of carbon and can be catabolized to produce sucrose.
The chemical reactions and pathways resulting in the breakdown of starch, the most important reserve polysaccharide in plants.
The chemical reactions and pathways resulting in the breakdown of starch, the most important reserve polysaccharide in plants.
The chemical reactions and pathways resulting in the breakdown of starch, the most important reserve polysaccharide in plants.
The chemical reactions and pathways involving any disaccharide, sugars composed of two monosaccharide units.
The chemical reactions and pathways involving sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the formation of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the formation of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the formation of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the formation of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the breakdown of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the breakdown of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways resulting in the breakdown of sucrose, the disaccharide fructofuranosyl-glucopyranoside.
The chemical reactions and pathways involving lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the formation of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the formation of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the formation of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the formation of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the breakdown of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the breakdown of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways resulting in the breakdown of lactose, the disaccharide galactopyranosyl-glucose.
The chemical reactions and pathways involving trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways involving trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways involving trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways involving trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways involving trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
The chemical reactions and pathways involving melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways resulting in the breakdown of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways resulting in the breakdown of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways resulting in the breakdown of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways involving monosaccharides, the simplest carbohydrates. They are polyhydric alcohols containing either an aldehyde or a keto group and between three to ten or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides.
The chemical reactions and pathways involving xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the breakdown of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the breakdown of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the breakdown of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the formation of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the formation of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the formation of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways resulting in the formation of xylulose, the ketopentose threo-2-pentulose.
The chemical reactions and pathways involving fructose, the ketohexose arabino-2-hexulose. Fructose exists in a open chain form or as a ring compound. D-fructose is the sweetest of the sugars and is found free in a large number of fruits and honey.
The chemical reactions and pathways resulting in the breakdown of fructose, the ketohexose arabino-2-hexulose.
The chemical reactions and pathways resulting in the breakdown of fructose, the ketohexose arabino-2-hexulose.
The chemical reactions and pathways resulting in the breakdown of fructose, the ketohexose arabino-2-hexulose.
The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism.
The chemical reactions and pathways involving fructose 2,6-bisphosphate. The D enantiomer is an important regulator of the glycolytic and gluconeogenic pathways. It inhibits fructose 1,6-bisphosphatase and activates phosphofructokinase.
The chemical reactions and pathways involving fucose, or 6-deoxygalactose, which has two enantiomers, D-fucose and L-fucose.
The chemical reactions and pathways resulting in the formation of L-fucose (6-deoxy-L-galactose).
The chemical reactions and pathways resulting in the formation of L-fucose (6-deoxy-L-galactose).
The chemical reactions and pathways resulting in the formation of L-fucose (6-deoxy-L-galactose).
The chemical reactions and pathways resulting in the formation of L-fucose (6-deoxy-L-galactose).
The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
The chemical reactions and pathways resulting in the breakdown of glucose, the aldohexose gluco-hexose.
The chemical reactions and pathways resulting in the breakdown of glucose, the aldohexose gluco-hexose.
The chemical reactions and pathways resulting in the breakdown of glucose, the aldohexose gluco-hexose.
The process of introducing a phosphate group into glucose 1-phosphate to produce glucose bisphosphate.
The chemical reactions and pathways involving UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways involving galactose, the aldohexose galacto-hexose. D-galactose is widely distributed in combined form in plants, animals and microorganisms as a constituent of oligo- and polysaccharides; it also occurs in galactolipids and as its glucoside in lactose and melibiose.
The chemical reactions and pathways involving mannose, the aldohexose manno-hexose, the C-2 epimer of glucose. The D-(+)-form is widely distributed in mannans and hemicelluloses and is of major importance in the core oligosaccharide of N-linked oligosaccharides of glycoproteins.
The chemical reactions and pathways involving D-ribose (ribo-pentose). As beta-D-ribofuranose, D-ribose forms the glycose group of all ribonucleosides, ribonucleotides and ribonucleic acids, and also of ribose phosphates, various glycosides, some coenzymes and some forms of vitamin B12.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
The chemical reactions and pathways resulting in the formation of 2-deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of 2-deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of 2-deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of 2-deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyribose 1,5-bisphosphate, the diphosphorylated sugar 1,5-diphospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyribose 1,5-bisphosphate, the diphosphorylated sugar 1,5-diphospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyribose 1,5-bisphosphate, the diphosphorylated sugar 1,5-diphospho-2-deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyribose 1,5-bisphosphate, the diphosphorylated sugar 1,5-diphospho-2-deoxyribose.
The chemical reactions and pathways resulting in the breakdown of deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the breakdown of deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the breakdown of deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The chemical reactions and pathways resulting in the breakdown of deoxyribose 1-phosphate, the phosphorylated sugar 1-phospho-2-deoxyribose.
The process of introducing a phosphate group into deoxyribose 5-phosphate to produce deoxyribose bisphosphate.
The chemical reactions and pathways involving inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways involving inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways involving inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways involving inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways involving inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways resulting in the formation of inositol, 1,2,3,4,5,6-cyclohexanehexol, a growth factor for animals and microorganisms.
The chemical reactions and pathways involving aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the formation of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the formation of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the formation of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the formation of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the formation of glycosaminoglycans, any of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the formation of glycosaminoglycans, any of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the formation of glycosaminoglycans, any of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the formation of glycosaminoglycans, any of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the formation of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways resulting in the formation of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways resulting in the formation of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways resulting in the formation of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways resulting in the breakdown of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the breakdown of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the breakdown of aminoglycans, any polymer containing amino groups that consists of more than about 10 monosaccharide residues joined to each other by glycosidic linkages.
The chemical reactions and pathways resulting in the breakdown of glycosaminoglycans, any one of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the breakdown of glycosaminoglycans, any one of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the breakdown of glycosaminoglycans, any one of a group of polysaccharides that contain amino sugars.
The chemical reactions and pathways resulting in the breakdown of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways resulting in the breakdown of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways resulting in the breakdown of galactosaminoglycans, any of a group of polysaccharides that contain amino sugars derived from the galactose.
The chemical reactions and pathways involving chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways involving chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways involving chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the formation of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the formation of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the formation of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the formation of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the formation of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the formation of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the breakdown of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the breakdown of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the breakdown of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the breakdown of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The chemical reactions and pathways resulting in the breakdown of chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
A process in which chitin is transported to, or maintained in, a specific location.
A process in which chitin is transported to, or maintained in, a specific location.
The chemical reactions and pathways involving cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the formation of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the formation of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the formation of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the formation of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the breakdown of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the breakdown of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways resulting in the breakdown of cuticle chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in cuticles.
The chemical reactions and pathways involving cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the breakdown of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the breakdown of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways resulting in the breakdown of cell wall chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues, found in the walls of cells.
The chemical reactions and pathways involving any amino sugar, sugars containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways involving any amino sugar, sugars containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways involving any amino sugar, sugars containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways involving glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways involving glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways involving glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the formation of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the formation of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the formation of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the formation of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the formation of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the formation of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the breakdown of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the breakdown of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the breakdown of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the breakdown of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways resulting in the breakdown of glucosamine (2-amino-2-deoxyglucopyranose), an aminodeoxysugar that occurs in combined form in chitin.
The chemical reactions and pathways involving N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the formation of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the formation of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the formation of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the formation of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the breakdown of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the breakdown of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways resulting in the breakdown of N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
The chemical reactions and pathways involving UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways involving mannosomine, 2-amino-2-deoxymannose; the D-isomer is a constituent of neuraminic acids as well as mucolipids and mucoproteins.
The chemical reactions and pathways involving N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the formation of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the formation of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the formation of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the formation of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the breakdown of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the breakdown of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways resulting in the breakdown of N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.
The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.
The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.
The chemical reactions and pathways resulting in the formation of CMP-N-acetylneuraminate, a substance composed of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-N-acetylneuraminate, a substance composed of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-N-acetylneuraminate, a substance composed of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-N-acetylneuraminate, a substance composed of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways involving mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the formation of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the formation of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the formation of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the formation of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the breakdown of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the breakdown of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways resulting in the breakdown of mannoproteins, any protein that contains covalently bound mannose residues.
The chemical reactions and pathways involving hexitols, any alditol with a chain of six carbon atoms in the molecule.
The chemical reactions and pathways involving hexitols, any alditol with a chain of six carbon atoms in the molecule.
The chemical reactions and pathways involving hexitols, any alditol with a chain of six carbon atoms in the molecule.
The chemical reactions and pathways involving sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the formation of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the formation of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the formation of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the formation of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the breakdown of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the breakdown of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways resulting in the breakdown of sorbitol (D-glucitol), one of the ten stereoisomeric hexitols. It can be derived from glucose by reduction of the aldehyde group.
The chemical reactions and pathways involving uronic acid, any monocarboxylic acid formally derived by oxidizing to a carboxyl group the terminal hydroxymethylene group of either an aldose with four or more carbon atoms in the molecule, or of any glycoside derived from such an aldose.
The chemical reactions and pathways resulting in the breakdown of glucuronate, any salt or ester of glucuronic acid.
The chemical reactions and pathways resulting in the breakdown of glucuronate, any salt or ester of glucuronic acid.
The chemical reactions and pathways resulting in the breakdown of glucuronate, any salt or ester of glucuronic acid.
The chemical reactions and pathways resulting in the formation of UDP-glucuronate, a substance composed of glucuronic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-glucuronate, a substance composed of glucuronic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-glucuronate, a substance composed of glucuronic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-glucuronate, a substance composed of glucuronic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways involving alcohols, any of a class of compounds containing one or more hydroxyl groups attached to a saturated carbon atom.
The chemical reactions and pathways involving ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
The chemical reactions and pathways resulting in the breakdown of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
The chemical reactions and pathways resulting in the breakdown of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
The chemical reactions and pathways resulting in the breakdown of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
An ethanol metabolic process in which ethanol is converted to acetyl-CoA via acetaldehyde and acetate.
The chemical reactions and pathways involving octanol, the 8-carbon alcohol with the formula C8H17OH.
The chemical reactions and pathways involving glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
The chemical reactions and pathways involving glycerol-3-phosphate, a phosphoric monoester of glycerol.
The chemical reactions and pathways involving glucans, polysaccharides consisting only of glucose residues, occurring at the level of an individual cell.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->3)-beta-D-glucans.
The chemical reactions and pathways involving (1->6)-beta-D-glucans, compounds composed of glucose residues linked by (1->6)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->6)-beta-D-glucans, compounds composed of glucose residues linked by (1->6)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->6)-beta-D-glucans, compounds composed of glucose residues linked by (1->6)-beta-D-glucosidic bonds.
The chemical reactions and pathways involving (1->6)-beta-D-glucans, compounds composed of glucose residues linked by (1->6)-beta-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the formation of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways resulting in the breakdown of (1->6)-beta-D-glucans.
The chemical reactions and pathways involving a mannan backbone composed of D-mannose unites, substituted with D-glucose and/or D-galactose units.
The chemical reactions and pathways involving aldehydes, any organic compound with the formula R-CH=O, as carried out by individual cells.
The chemical reactions and pathways involving aldehydes, any organic compound with the formula R-CH=O, as carried out by individual cells.
The chemical reactions and pathways involving aldehydes, any organic compound with the formula R-CH=O, as carried out by individual cells.
The chemical reactions and pathways involving organic acids, any acidic compound containing carbon in covalent linkage.
The chemical reactions and pathways involving acetate, the anion of acetic acid.
The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
The chemical reactions and pathways resulting in the formation of acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated.
The chemical reactions and pathways resulting in the formation of acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated.
The chemical reactions and pathways resulting in the formation of acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated.
The chemical reactions and pathways resulting in the formation of acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated.
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
The chemical reactions and pathways involving lactate, the anion of lactic acid.
The chemical reactions and pathways involving lactate, the anion of lactic acid.
The chemical reactions and pathways involving lactate, the anion of lactic acid.
The chemical reactions and pathways involving lactate, the anion of lactic acid.
The chemical reactions and pathways involving lactate, the anion of lactic acid.
The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
A modification of the TCA cycle occurring in some plants and microorganisms, in which isocitrate is cleaved to glyoxylate and succinate. Glyoxylate can then react with acetyl-CoA to form malate.
The glucose-6-phosphate catabolic process in which, coupled to NADPH synthesis, glucose-6-P is oxidized with the formation of carbon dioxide (CO2) and ribulose 5-phosphate; ribulose 5-P then enters a series of reactions interconverting sugar phosphates. The pentose phosphate pathway is a major source of reducing equivalents for biosynthesis reactions and is also important for the conversion of hexoses to pentoses.
The glucose-6-phosphate catabolic process in which, coupled to NADPH synthesis, glucose-6-P is oxidized with the formation of carbon dioxide (CO2) and ribulose 5-phosphate; ribulose 5-P then enters a series of reactions interconverting sugar phosphates. The pentose phosphate pathway is a major source of reducing equivalents for biosynthesis reactions and is also important for the conversion of hexoses to pentoses.
The glucose-6-phosphate catabolic process in which, coupled to NADPH synthesis, glucose-6-P is oxidized with the formation of carbon dioxide (CO2) and ribulose 5-phosphate; ribulose 5-P then enters a series of reactions interconverting sugar phosphates. The pentose phosphate pathway is a major source of reducing equivalents for biosynthesis reactions and is also important for the conversion of hexoses to pentoses.
The glucose-6-phosphate catabolic process in which, coupled to NADPH synthesis, glucose-6-P is oxidized with the formation of carbon dioxide (CO2) and ribulose 5-phosphate; ribulose 5-P then enters a series of reactions interconverting sugar phosphates. The pentose phosphate pathway is a major source of reducing equivalents for biosynthesis reactions and is also important for the conversion of hexoses to pentoses.
A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
The chemical reactions and pathways involving citrate, 2-hydroxy-1,2,3-propanetricarboyxlate. Citrate is widely distributed in nature and is an important intermediate in the TCA cycle and the glyoxylate cycle.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
The chemical reactions and pathways involving succinyl-CoA, a compound composed of the monovalent acyl group 3-carboxypropanoyl, derived from succinic acid by loss of one OH group, linked to coenzyme A.
The chemical reactions and pathways involving succinate, also known as butanedioate or ethane dicarboxylate, the dianion of succinic acid. Succinate is an important intermediate in metabolism and a component of the TCA cycle.
The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.
The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.
The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle.
The chemical reactions and pathways involving isocitrate, the anion of isocitric acid, 1-hydroxy-1,2,3-propanetricarboxylic acid. Isocitrate is an important intermediate in the TCA cycle and the glycoxylate cycle.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving carbohydrates.
Any process that modulates the frequency, rate or extent of glycolysis.
Any process that modulates the frequency, rate or extent of glycolysis.
Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
The chemical reactions and pathways by which a cell derives energy from stored compounds such as fats or glycogen.
The anaerobic enzymatic conversion of organic compounds, especially carbohydrates, coupling the oxidation and reduction of NAD/H and the generation of adenosine triphosphate (ATP).
The chemical reactions and pathways resulting in the formation of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
The chemical reactions and pathways resulting in the formation of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
The chemical reactions and pathways resulting in the formation of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
The chemical reactions and pathways resulting in the formation of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
The chemical reactions and pathways resulting in the formation of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
The chemical reactions and pathways resulting in the formation of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
The chemical reactions and pathways resulting in the formation of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
The chemical reactions and pathways resulting in the formation of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
The chemical reactions and pathways involving acetaldehyde, a colorless, flammable liquid intermediate in the metabolism of alcohol.
The chemical reactions and pathways involving acetaldehyde, a colorless, flammable liquid intermediate in the metabolism of alcohol.
The chemical reactions and pathways involving acetaldehyde, a colorless, flammable liquid intermediate in the metabolism of alcohol.
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex I.
The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex I.
The transfer of electrons from succinate to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex II.
The transfer of electrons from succinate to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex II.
The transfer of electrons from succinate to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex II.
The transfer of electrons from ubiquinol to cytochrome c that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex III.
The transfer of electrons from cytochrome c to oxygen that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex IV.
The chemical reactions and pathways involving ferredoxin, any simple, nonenzymatic iron-sulfur protein that is characterized by having equal numbers of atoms of iron and labile sulfur. Iron and sulfur atoms are present in one or two clusters of two or four atoms of each.
Any process that maintains the redox environment of a cell or compartment within a cell.
Any process that maintains the redox environment of a cell or compartment within a cell.
Any process that maintains the redox environment of a cell or compartment within a cell.
Any process that maintains the redox environment of a cell or compartment within a cell.
Any process that maintains the redox environment of a cell or compartment within a cell.
A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
The process of transferring reducing equivalents from the cytosol into the mitochondria; NADH is used to synthesise glycerol 3-phosphate in the cytosol; this compound is then transported into the mitochondria where it is converted to dihydroxyacetone phosphate (DHAP) using FAD; DHAP then returns to the cytosol to complete the cycle.
The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.
The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
Catalysis of the reaction: 2 glutathione + protein-disulfide = oxidized glutathione + protein-dithiol.
The chemical reactions and pathways involving dihydrolipoamide, the reduced form of lipoamide, produced as an intermediate in the reactions in which lipoamide acts as a cofactor.
The chemical reactions and pathways involving dihydrolipoamide, the reduced form of lipoamide, produced as an intermediate in the reactions in which lipoamide acts as a cofactor.
The chemical reactions and pathways involving dihydrolipoamide, the reduced form of lipoamide, produced as an intermediate in the reactions in which lipoamide acts as a cofactor.
The chemical reactions and pathways involving dihydrolipoamide, the reduced form of lipoamide, produced as an intermediate in the reactions in which lipoamide acts as a cofactor.
Catalysis of the reaction: 5-methyltetrahydrofolate + oxidized ferredoxin = 5,10-methylenetetrahydrofolate + reduced ferredoxin.
Catalysis of the reaction: 5-methyltetrahydrofolate + oxidized ferredoxin = 5,10-methylenetetrahydrofolate + reduced ferredoxin.
Catalysis of the reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 H(+) + 2 NADPH.
Catalysis of the reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 H(+) + 2 NADPH.
Catalysis of the reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 H(+) + 2 NADPH.
Catalysis of the reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 H(+) + 2 NADPH.
Catalysis of the reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 H(+) + 2 NADPH.
The chemical reactions and pathways involving a dihydrobiopterin, a reduced pteridine derivative related to folic acid; it acts as an electron carrier in tyrosine biosynthesis and its quinoid form is produced by oxidation of tetrahydrobiopterin in several biological hydroxylation reactions.
The chemical reactions and pathways involving a dihydrobiopterin, a reduced pteridine derivative related to folic acid; it acts as an electron carrier in tyrosine biosynthesis and its quinoid form is produced by oxidation of tetrahydrobiopterin in several biological hydroxylation reactions.
The chemical reactions and pathways involving a dihydrobiopterin, a reduced pteridine derivative related to folic acid; it acts as an electron carrier in tyrosine biosynthesis and its quinoid form is produced by oxidation of tetrahydrobiopterin in several biological hydroxylation reactions.
The chemical reactions and pathways involving a dihydrobiopterin, a reduced pteridine derivative related to folic acid; it acts as an electron carrier in tyrosine biosynthesis and its quinoid form is produced by oxidation of tetrahydrobiopterin in several biological hydroxylation reactions.
The chemical reactions and pathways involving a dihydrobiopterin, a reduced pteridine derivative related to folic acid; it acts as an electron carrier in tyrosine biosynthesis and its quinoid form is produced by oxidation of tetrahydrobiopterin in several biological hydroxylation reactions.
The chemical reactions and pathways involving 6,7-dihydropteridine, a bicyclic compound with the formula C6H6N4.
The chemical reactions and pathways involving 6,7-dihydropteridine, a bicyclic compound with the formula C6H6N4.
The chemical reactions and pathways involving 6,7-dihydropteridine, a bicyclic compound with the formula C6H6N4.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving purines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving purines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving pyrimidine nucleobases.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving pyrimidine nucleobases.
The chemical reactions and pathways involving purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways involving purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways involving purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways involving purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways involving one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways involving one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways involving one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the breakdown of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways resulting in the breakdown of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways resulting in the breakdown of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways resulting in the breakdown of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.
The chemical reactions and pathways resulting in the breakdown of adenine, 6-aminopurine, one of the 5 main bases found in nucleic acids and a component of numerous important derivatives of its corresponding ribonucleoside, adenosine.
The chemical reactions and pathways resulting in the breakdown of adenine, 6-aminopurine, one of the 5 main bases found in nucleic acids and a component of numerous important derivatives of its corresponding ribonucleoside, adenosine.
The chemical reactions and pathways resulting in the breakdown of adenine, 6-aminopurine, one of the 5 main bases found in nucleic acids and a component of numerous important derivatives of its corresponding ribonucleoside, adenosine.
The chemical reactions and pathways resulting in the breakdown of guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important.
The chemical reactions and pathways resulting in the breakdown of guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important.
The chemical reactions and pathways resulting in the breakdown of guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important.
The chemical reactions and pathways resulting in the breakdown of inosine, hypoxanthine riboside, a nucleoside found free but not in combination in nucleic acids except in the anticodons of some tRNAs.
The chemical reactions and pathways resulting in the breakdown of inosine, hypoxanthine riboside, a nucleoside found free but not in combination in nucleic acids except in the anticodons of some tRNAs.
The chemical reactions and pathways resulting in the breakdown of inosine, hypoxanthine riboside, a nucleoside found free but not in combination in nucleic acids except in the anticodons of some tRNAs.
The chemical reactions and pathways resulting in the breakdown of deoxyinosine, hypoxanthine deoxyriboside.
The chemical reactions and pathways resulting in the breakdown of deoxyinosine, hypoxanthine deoxyriboside.
The chemical reactions and pathways resulting in the breakdown of deoxyinosine, hypoxanthine deoxyriboside.
The chemical reactions and pathways resulting in the breakdown of hypoxanthine to xanthine and thence to uric acid.
The oxidation of xanthine, 2,6-dihydroxypurine, a purine formed in the metabolic breakdown of guanine but not present in nucleic acids.
The chemical reactions and pathways resulting in the breakdown of purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the breakdown of purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the breakdown of purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
Catalysis of the reaction: a N-D-ribosylpurine + H2O = a purine + D-ribose.
The chemical reactions and pathways resulting in the breakdown of adenosine, adenine riboside, a ribonucleoside found widely distributed in cells of every type as the free nucleoside and in combination in nucleic acids and various nucleoside coenzymes.
The chemical reactions and pathways resulting in the breakdown of adenosine, adenine riboside, a ribonucleoside found widely distributed in cells of every type as the free nucleoside and in combination in nucleic acids and various nucleoside coenzymes.
The chemical reactions and pathways resulting in the breakdown of adenosine, adenine riboside, a ribonucleoside found widely distributed in cells of every type as the free nucleoside and in combination in nucleic acids and various nucleoside coenzymes.
The chemical reactions and pathways resulting in the breakdown of adenosine, adenine riboside, a ribonucleoside found widely distributed in cells of every type as the free nucleoside and in combination in nucleic acids and various nucleoside coenzymes.
The chemical reactions and pathways resulting in the breakdown of adenosine, adenine riboside, a ribonucleoside found widely distributed in cells of every type as the free nucleoside and in combination in nucleic acids and various nucleoside coenzymes.
The chemical reactions and pathways resulting in the breakdown of deoxyadenosine, 2-deoxyribosyladenine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxyadenosine, 2-deoxyribosyladenine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxyadenosine, 2-deoxyribosyladenine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxyadenosine, 2-deoxyribosyladenine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxyadenosine, 2-deoxyribosyladenine, one of the four major nucleosides of DNA.
Catalysis of the reaction: deoxyadenosine + H2O = deoxyinosine + NH3.
The chemical reactions and pathways resulting in the breakdown of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the breakdown of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the breakdown of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The process of introducing a phosphate group into a nucleoside diphosphate to produce a nucleoside triphosphate.
Any process which produces a purine nucleoside from derivatives of it, without de novo synthesis.
The chemical reactions and pathways resulting in the formation of AMP, adenosine monophosphate.
The chemical reactions and pathways resulting in the formation of AMP, adenosine monophosphate.
The chemical reactions and pathways resulting in the formation of AMP, adenosine monophosphate.
The chemical reactions and pathways resulting in the formation of AMP, adenosine monophosphate.
Any process that generates adenine, 6-aminopurine, from derivatives of it without de novo synthesis.
Any process that generates adenine, 6-aminopurine, from derivatives of it without de novo synthesis.
Any process that generates adenosine, adenine riboside, from derivatives of it without de novo synthesis.
The chemical reactions and pathways resulting in the formation of dAMP, deoxyadenosine monophosphate (2'-deoxyadenosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dAMP, deoxyadenosine monophosphate (2'-deoxyadenosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dAMP, deoxyadenosine monophosphate (2'-deoxyadenosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dAMP, deoxyadenosine monophosphate (2'-deoxyadenosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the formation of ADP, adenosine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of ADP, adenosine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of ADP, adenosine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of ADP, adenosine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of dADP, deoxyadenosine diphosphate (2'-deoxyadenosine 5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dADP, deoxyadenosine diphosphate (2'-deoxyadenosine 5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dADP, deoxyadenosine diphosphate (2'-deoxyadenosine 5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dADP, deoxyadenosine diphosphate (2'-deoxyadenosine 5'-diphosphate).
The process of introducing a phosphate group into dADP, deoxyadenosine diphosphate, to produce dATP.
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate).
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate).
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate).
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate).
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate) from other compounds, including ADP, adenosine diphosphate.
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate) from other compounds, including ADP, adenosine diphosphate.
The chemical reactions and pathways resulting in the formation of dATP, deoxyadenosine triphosphate (2'-deoxyadenosine 5'-triphosphate) from other compounds, including ADP, adenosine diphosphate.
The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
Any process that generates guanine, 2-amino-6-hydroxypurine, from derivatives of it without de novo synthesis.
Any process that generates guanosine, guanine riboside, from derivatives of it without de novo synthesis.
Any process that generates deoxyguanosine from derivatives of it, without de novo synthesis.
The chemical reactions and pathways resulting in the formation of dGMP, deoxyguanosine monophosphate (2'-deoxyguanosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dGMP, deoxyguanosine monophosphate (2'-deoxyguanosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dGMP, deoxyguanosine monophosphate (2'-deoxyguanosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dGMP, deoxyguanosine monophosphate (2'-deoxyguanosine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of cyclic GMP, guanosine 3',5'-phosphate.
The chemical reactions and pathways resulting in the formation of cyclic GMP, guanosine 3',5'-phosphate.
The chemical reactions and pathways resulting in the formation of cyclic GMP, guanosine 3',5'-phosphate.
The chemical reactions and pathways resulting in the formation of cyclic GMP, guanosine 3',5'-phosphate.
The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the formation of GTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the formation of dGDP, deoxyguanosine diphosphate, (2'-deoxyguanosine 5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dGDP, deoxyguanosine diphosphate, (2'-deoxyguanosine 5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dGDP, deoxyguanosine diphosphate, (2'-deoxyguanosine 5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dGDP, deoxyguanosine diphosphate, (2'-deoxyguanosine 5'-diphosphate).
The process of introducing a phosphate group into dGDP, deoxyguanosine diphosphate, to produce dGTP.
The chemical reactions and pathways resulting in the formation of dGTP, deoxyguanosine triphosphate (2'-deoxyguanosine 5'-triphosphate) from other compounds, including gGDP, deoxyguanosine diphosphate.
The chemical reactions and pathways resulting in the formation of dGTP, deoxyguanosine triphosphate (2'-deoxyguanosine 5'-triphosphate) from other compounds, including gGDP, deoxyguanosine diphosphate.
The chemical reactions and pathways resulting in the formation of dGTP, deoxyguanosine triphosphate (2'-deoxyguanosine 5'-triphosphate) from other compounds, including gGDP, deoxyguanosine diphosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
Any process that generates inosine, hypoxanthine riboside, from derivatives of it without de novo synthesis.
Any process that generates inosine, hypoxanthine riboside, from derivatives of it without de novo synthesis.
Any process that generates deoxyinosine from derivatives of it, without de novo synthesis.
The process of introducing a phosphate group into IDP, inosine (5'-)diphosphate, to produce ITP.
The chemical reactions and pathways resulting in the breakdown of ITP, inosine (5'-)triphosphate.
The chemical reactions and pathways resulting in the breakdown of ITP, inosine (5'-)triphosphate.
The chemical reactions and pathways resulting in the breakdown of ITP, inosine (5'-)triphosphate.
The chemical reactions and pathways resulting in the breakdown of ITP, inosine (5'-)triphosphate.
The process of introducing a phosphate group into dIDP, deoxyinosine diphosphate, to produce dITP.
The chemical reactions and pathways resulting in the breakdown of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the breakdown of AMP, adenosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of AMP, adenosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of AMP, adenosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways resulting in the breakdown of the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
Catalysis of the reaction: dADP + thioredoxin disulfide + H2O = ADP + thioredoxin.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction.
The chemical reactions and pathways resulting in the breakdown of guanosine monophosphate into other compounds, including inosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of guanosine monophosphate into other compounds, including inosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of guanosine monophosphate into other compounds, including guanine.
The chemical reactions and pathways resulting in the breakdown of guanosine monophosphate into other compounds, including guanine.
The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate.
The chemical reactions and pathways resulting in the breakdown of IMP, inosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of IMP, inosine monophosphate.
The chemical reactions and pathways resulting in the breakdown of IMP, inosine monophosphate.
The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways involving any pyrimidine nucleoside, one of a family of organic molecules consisting of a pyrimidine base covalently bonded to ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways involving any pyrimidine nucleoside, one of a family of organic molecules consisting of a pyrimidine base covalently bonded to ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways involving any pyrimidine nucleoside, one of a family of organic molecules consisting of a pyrimidine base covalently bonded to ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways involving a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways involving a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways involving a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
The chemical reactions and pathways resulting in the breakdown of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the breakdown of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the breakdown of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the breakdown of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the breakdown of cytosine, 4-amino-2-hydroxypyrimidine, a pyrimidine derivative that is one of the five main bases found in nucleic acids; it occurs widely in cytidine derivatives.
The chemical reactions and pathways resulting in the breakdown of cytosine, 4-amino-2-hydroxypyrimidine, a pyrimidine derivative that is one of the five main bases found in nucleic acids; it occurs widely in cytidine derivatives.
The chemical reactions and pathways resulting in the breakdown of cytosine, 4-amino-2-hydroxypyrimidine, a pyrimidine derivative that is one of the five main bases found in nucleic acids; it occurs widely in cytidine derivatives.
The chemical reactions and pathways resulting in the breakdown of thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base.
The chemical reactions and pathways resulting in the breakdown of thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base.
The chemical reactions and pathways resulting in the breakdown of thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base.
The chemical reactions and pathways resulting in the breakdown of 5-methylcytosine, a methylated base of DNA.
The chemical reactions and pathways resulting in the breakdown of 5-methylcytosine, a methylated base of DNA.
The chemical reactions and pathways resulting in the breakdown of 5-methylcytosine, a methylated base of DNA.
The chemical reactions and pathways resulting in the breakdown of uracil, 2,4-dioxopyrimidine, one of the pyrimidine bases occurring in RNA, but not in DNA.
The chemical reactions and pathways resulting in the breakdown of uracil, 2,4-dioxopyrimidine, one of the pyrimidine bases occurring in RNA, but not in DNA.
The chemical reactions and pathways resulting in the breakdown of uracil, 2,4-dioxopyrimidine, one of the pyrimidine bases occurring in RNA, but not in DNA.
The chemical reactions and pathways resulting in the breakdown of thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.
The chemical reactions and pathways resulting in the breakdown of thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.
The chemical reactions and pathways resulting in the breakdown of thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.
The chemical reactions and pathways resulting in the breakdown of thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.
The chemical reactions and pathways resulting in the breakdown of thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.
The chemical reactions and pathways resulting in the breakdown of thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.
The chemical reactions and pathways resulting in the breakdown of cytidine, cytosine riboside, a widely distributed nucleoside.
The chemical reactions and pathways resulting in the breakdown of cytidine, cytosine riboside, a widely distributed nucleoside.
The chemical reactions and pathways resulting in the breakdown of cytidine, cytosine riboside, a widely distributed nucleoside.
The chemical reactions and pathways resulting in the breakdown of deoxycytidine, 2-deoxyribosylcytosine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxycytidine, 2-deoxyribosylcytosine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxycytidine, 2-deoxyribosylcytosine, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of uridine, uracil riboside, a ribonucleoside very widely distributed but occurring almost entirely as phosphoric esters in ribonucleotides and ribonucleic acids.
The chemical reactions and pathways resulting in the breakdown of uridine, uracil riboside, a ribonucleoside very widely distributed but occurring almost entirely as phosphoric esters in ribonucleotides and ribonucleic acids.
The chemical reactions and pathways resulting in the breakdown of uridine, uracil riboside, a ribonucleoside very widely distributed but occurring almost entirely as phosphoric esters in ribonucleotides and ribonucleic acids.
The chemical reactions and pathways resulting in the breakdown of deoxyuridine, 2-deoxyribosyluracil, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxyuridine, 2-deoxyribosyluracil, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the breakdown of deoxyuridine, 2-deoxyribosyluracil, one of the four major nucleosides of DNA.
The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate.
The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate.
The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate.
The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate.
Any process that generates uracil, 2,4-dioxopyrimidine, from derivatives of it without de novo synthesis.
The chemical reactions and pathways resulting in the formation of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the formation of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the formation of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the formation of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the formation of dUMP, deoxyuridine monophosphate (2'-deoxyuridine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dUMP, deoxyuridine monophosphate (2'-deoxyuridine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dUMP, deoxyuridine monophosphate (2'-deoxyuridine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dUMP, deoxyuridine monophosphate (2'-deoxyuridine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dUDP, deoxyuridine diphosphate (2'-deoxy-5'-uridylyl phosphate).
The chemical reactions and pathways resulting in the formation of dUDP, deoxyuridine diphosphate (2'-deoxy-5'-uridylyl phosphate).
The chemical reactions and pathways resulting in the formation of dUDP, deoxyuridine diphosphate (2'-deoxy-5'-uridylyl phosphate).
The chemical reactions and pathways resulting in the formation of dUDP, deoxyuridine diphosphate (2'-deoxy-5'-uridylyl phosphate).
The chemical reactions and pathways resulting in the formation of UTP, uridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of UTP, uridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of UTP, uridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of UTP, uridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of dUTP, deoxyuridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of dUTP, deoxyuridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of dUTP, deoxyuridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of dUTP, deoxyuridine (5'-)triphosphate.
The chemical reactions and pathways resulting in the formation of TMP, ribosylthymine monophosphate.
The chemical reactions and pathways resulting in the formation of TMP, ribosylthymine monophosphate.
The chemical reactions and pathways resulting in the formation of TMP, ribosylthymine monophosphate.
The chemical reactions and pathways resulting in the formation of TMP, ribosylthymine monophosphate.
The chemical reactions and pathways resulting in the formation of dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate).
The chemical reactions and pathways resulting in the formation of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the formation of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the formation of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the formation of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the formation of dTDP, deoxyribosylthymine diphosphate (2'-deoxyribosylthymine5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dTDP, deoxyribosylthymine diphosphate (2'-deoxyribosylthymine5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dTDP, deoxyribosylthymine diphosphate (2'-deoxyribosylthymine5'-diphosphate).
The chemical reactions and pathways resulting in the formation of dTDP, deoxyribosylthymine diphosphate (2'-deoxyribosylthymine5'-diphosphate).
The chemical reactions and pathways resulting in the formation of TTP, ribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of TTP, ribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of TTP, ribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of TTP, ribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of dTTP, deoxyribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of dTTP, deoxyribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of dTTP, deoxyribosylthymine triphosphate.
The chemical reactions and pathways resulting in the formation of dTTP, deoxyribosylthymine triphosphate.
Any process that generates cytidine, cytosine riboside, from derivatives of it without de novo synthesis.
Any process that generates deoxycytidine, 2-deoxyribosylcytosine, from derivatives of it, without de novo synthesis.
Any process that generates CMP, cytidine monophosphate, from derivatives of it without de novo synthesis.
Any process that generates dCMP, deoxycytidine monophosphate from derivatives of it, without de novo synthesis.
The chemical reactions and pathways resulting in the formation of dCDP, deoxycytidine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of dCDP, deoxycytidine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of dCDP, deoxycytidine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of dCDP, deoxycytidine 5'-diphosphate.
The chemical reactions and pathways resulting in the formation of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the formation of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the formation of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the formation of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the formation of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the formation of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the formation of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the formation of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the breakdown of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the breakdown of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the breakdown of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
The chemical reactions and pathways resulting in the breakdown of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the breakdown of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the breakdown of TDP, ribosylthymine diphosphate.
The chemical reactions and pathways resulting in the breakdown of dTDP, deoxyribosylthymine diphosphate.
The chemical reactions and pathways resulting in the breakdown of dTDP, deoxyribosylthymine diphosphate.
The chemical reactions and pathways resulting in the breakdown of dTDP, deoxyribosylthymine diphosphate.
Catalysis of the reaction: dTTP + thioredoxin disulfide + H2O = TTP + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin.
The chemical reactions and pathways resulting in the breakdown of CMP, cytidine monophosphate.
The chemical reactions and pathways resulting in the breakdown of CMP, cytidine monophosphate.
The chemical reactions and pathways resulting in the breakdown of CMP, cytidine monophosphate.
The chemical reactions and pathways resulting in the breakdown of dCMP, deoxycytidine monophosphate.
The chemical reactions and pathways resulting in the breakdown of dCMP, deoxycytidine monophosphate.
The chemical reactions and pathways resulting in the breakdown of dCMP, deoxycytidine monophosphate.
Catalysis of the reaction: dCDP + thioredoxin disulfide + H2O = CDP + thioredoxin.
The chemical reactions and pathways resulting in the breakdown of dCDP, deoxycytidine 5'-diphosphate.
The chemical reactions and pathways resulting in the breakdown of dCDP, deoxycytidine 5'-diphosphate.
The chemical reactions and pathways resulting in the breakdown of dCDP, deoxycytidine 5'-diphosphate.
Catalysis of the reaction: dCTP + thioredoxin disulfide + H2O = CTP + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin.
The chemical reactions and pathways resulting in the breakdown of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the breakdown of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the breakdown of dCTP, deoxycytidine triphosphate.
The chemical reactions and pathways resulting in the breakdown of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the breakdown of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the breakdown of CTP, cytidine 5'-triphosphate.
The chemical reactions and pathways resulting in the breakdown of CTP, cytidine 5'-triphosphate.
Catalysis of the reaction: dUDP + thioredoxin disulfide + H2O = UDP + thioredoxin.
The chemical reactions and pathways resulting in the breakdown of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP, uridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the breakdown of dUDP, deoxyuridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the breakdown of dUDP, deoxyuridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the breakdown of dUDP, deoxyuridine (5'-)diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the breakdown of UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate.
Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides.
A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
The process in which new strands of DNA are synthesized in the mitochondrion.
The process in which new strands of DNA are synthesized in the mitochondrion.
The process in which new strands of DNA are synthesized in the mitochondrion.
The process in which new strands of DNA are synthesized in the mitochondrion.
The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number.
The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase.
The aggregation, arrangement and bonding together of a set of components to form the nuclear pre-replicative complex, a protein-DNA complex that forms at the eukaryotic DNA replication origin and is required for replication initiation.
The aggregation, arrangement and bonding together of a set of components to form the nuclear pre-replicative complex, a protein-DNA complex that forms at the eukaryotic DNA replication origin and is required for replication initiation.
The aggregation, arrangement and bonding together of a set of components to form the nuclear pre-replicative complex, a protein-DNA complex that forms at the eukaryotic DNA replication origin and is required for replication initiation.
The aggregation, arrangement and bonding together of a set of components to form the nuclear pre-replicative complex, a protein-DNA complex that forms at the eukaryotic DNA replication origin and is required for replication initiation.
The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication.
The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication.
The synthesis of a short RNA polymer, usually 4-15 nucleotides long, using one strand of unwound DNA as a template; the RNA then serves as a primer from which DNA polymerases extend synthesis.
The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
The process in which a DNA strand is synthesized from template DNA during replication by the action of polymerases, which add nucleotides to the 3' end of the nascent DNA strand.
The process in which a DNA strand is synthesized from template DNA during replication by the action of polymerases, which add nucleotides to the 3' end of the nascent DNA strand.
The synthesis of DNA from a template strand in the 5' to 3' direction; leading strand elongation is continuous as it proceeds in the same direction as the replication fork.
The synthesis of DNA from a template strand in a net 3' to 5' direction. Lagging strand DNA elongation proceeds by discontinuous synthesis of short stretches of DNA, known as Okazaki fragments, from RNA primers; these fragments are then joined by DNA ligase. Although each segment of nascent DNA is synthesized in the 5' to 3' direction, the overall direction of lagging strand synthesis is 3' to 5', mirroring the progress of the replication fork.
The process in which DNA replication at a replication fork ceases; occurs when the replication fork reaches a specific termination site or when two replication forks meet.
Any process that modulates the frequency, rate or extent of DNA replication.
The maintenance of the integrity of extrachromosomal plasmid DNA; includes processes that ensure plasmids are retained in the daughter cells after cell division.
The process in which the number of copies of a gene is increased in certain cells as extra copies of DNA are made in response to certain signals of cell development or of stress from the environment.
A DNA biosynthetic process that uses RNA as a template for RNA-dependent DNA polymerases (e.g. reverse transcriptase) that synthesize the new strand.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The replication of DNA that precedes meiotic cell division.
The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
Any process that modulates the frequency, rate or extent of DNA repair.
The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
The formation of an AP site, a deoxyribose sugar with a missing base, by DNA glycosylase which recognizes an altered base in DNA and catalyzes its hydrolytic removal. This sugar phosphate is the substrate recognized by the AP endonuclease, which cuts the DNA phosphodiester backbone at the 5' side of the altered site to leave a gap which is subsequently repaired.
Excision of the sugar phosphate residue at an AP site, i.e. a deoxyribose sugar with a missing base, by a phosphodiesterase enzyme.
Repair of the damaged strand by the combined action of an apurinic endouclease that degrades a few bases on the damaged strand and a polymerase that synthesizes a 'patch' in the 5' to 3' direction, using the undamaged strand as a template.
The ligation by DNA ligase of DNA strands. Ligation occurs after polymerase action to fill the gap left by the action of endonucleases during base-excision repair.
A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
The repair of UV-induced T-T, C-T and C-C dimers.
The stabilization of the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage as well as the unwound DNA. The stabilization of the protein-DNA complex ensures proper positioning of the preincision complex before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage.
The aggregation, arrangement and bonding together of proteins on DNA to form the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage. This assembly occurs before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage.
The endonucleolytic cleavage of the damaged strand of DNA 3' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision precedes the incision formed 5' to the site of damage.
The endonucleolytic cleavage of the damaged strand of DNA 5' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision follows the incision formed 3' to the site of damage.
Repair of the gap in the DNA helix by DNA polymerase and DNA ligase after the portion of the strand containing the lesion has been removed by pyrimidine-dimer repair enzymes.
A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication.
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
The covalent alteration of one or more nucleotide sites in DNA, resulting in a change in its properties.
The addition of alkyl groups to many positions on all four bases of DNA. Alkylating agents can also modify the bases of incoming nucleotides in the course of DNA synthesis.
The covalent transfer of a methyl group to either N-6 of adenine or C-5 or N-4 of cytosine.
The repair of alkylation damage, e.g. the removal of the alkyl group at the O6-position of guanine by O6-alkylguanine-DNA alkyltransferase (AGT).
The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one.
The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one.
The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments.
Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
The cell cycle process in which genetic information is transferred from one helix to another. It often occurs in association with general genetic recombination events, and is believed to be a straightforward consequence of the mechanisms of general recombination and DNA repair. For example, meiosis might yield three copies of the maternal version of an allele and only one copy of the paternal allele, indicating that one of the two copies of the paternal allele has been changed to a copy of the maternal allele.
The exchange, reciprocal or nonreciprocal, of genetic material between one DNA molecule and a homologous region of DNA that occurs during mitotic cell cycles.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Any process involved in a type of transpositional recombination which occurs via a DNA intermediate.
Lateral transfer of an intron to a homologous allele that lacks the intron, mediated by a site-specific endonuclease encoded within the mobile intron.
Lateral transfer of a group II intron to a homologous allele that lacks the intron, mediated by a site-specific endonuclease encoded within the mobile intron; group II introns are self-splicing introns with a conserved secondary structure.
Lateral transfer of a group I intron to a homologous allele that lacks the intron, mediated by a site-specific endonuclease encoded within the mobile intron; group I introns are self-splicing introns that use guanosine as a cofactor in the splicing reaction.
Any process in which DNA and associated proteins are formed into a compact, orderly structure.
Any process in which DNA and associated proteins are formed into a compact, orderly structure.
Any process in which DNA and associated proteins are formed into a compact, orderly structure.
The covalent alteration of one or more amino acid residues within a histone protein.
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin.
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin.
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin.
Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin.
The formation of nucleosomes on newly replicated DNA, coupled to strand elongation.
The formation of nucleosomes outside the context of DNA replication.
The controlled breakdown of nucleosomes, the beadlike structural units of eukaryotic chromatin composed of histones and DNA.
Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation.
Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation.
Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation.
Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin.
Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin.
Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin.
Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin.
Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin.
Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin.
Maintenance of transcription by remodelling of chromatin into an 'open configuration'. Once established, this regulation is mitotically stable and is maintained over many cell divisions. It is also heritable.
Interacting selectively and non-covalently and stoichiometrically with a chromatin insulator sequence, a DNA sequence that prevents enhancer-mediated activation or repression of transcription.
The initial formation of a transcriptionally silent chromatin structure such as heterochromatin.
The maintenance of chromatin in a transcriptionally silent state such as heterochromatin.
Repression of transcription by methylation of DNA, leading to the formation of heterochromatin.
Repression of transcription of telomeric DNA by altering the structure of chromatin.
Repression of transcription of telomeric DNA by altering the structure of chromatin.
Repression of transcription of telomeric DNA by altering the structure of chromatin.
Repression of transcription of telomeric DNA by altering the structure of chromatin.
Heritable alterations in the activity of a gene that depend on whether it passed through the paternal or the maternal germline, but that are not encoded by DNA itself.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
The cellular synthesis of RNA on a template of DNA.
Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase preinitiation complex (PIC) at the core promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. The initiation phase ends just before and does not include promoter clearance, or release, which is the transition between the initiation and elongation phases of transcription.
The extension of an RNA molecule after transcription initiation and promoter clearance at a DNA-dependent RNA polymerase promoter by the addition of ribonucleotides catalyzed by an RNA polymerase.
The extension of an RNA molecule after transcription initiation and promoter clearance at a DNA-dependent RNA polymerase promoter by the addition of ribonucleotides catalyzed by an RNA polymerase.
The extension of an RNA molecule after transcription initiation and promoter clearance at a DNA-dependent RNA polymerase promoter by the addition of ribonucleotides catalyzed by an RNA polymerase.
The extension of an RNA molecule after transcription initiation and promoter clearance at a DNA-dependent RNA polymerase promoter by the addition of ribonucleotides catalyzed by an RNA polymerase.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase I.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase I.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA ploymerase III.
Any process that modulates the frequency, rate or extent of transcription mediated by RNA ploymerase III.
Any process involved in the assembly of the RNA polymerase I preinitiation complex (PIC) at an RNA polymerase I promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase I preinitiation complex (PIC) at an RNA polymerase I promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase I preinitiation complex (PIC) at an RNA polymerase I promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase I specific promoter by the addition of ribonucleotides catalyzed by RNA polymerase I.
The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase I specific promoter by the addition of ribonucleotides catalyzed by RNA polymerase I.
Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules.
Any process involved in the assembly of the RNA polymerase II preinitiation complex (PIC) at an RNA polymerase II promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase II promoter by the addition of ribonucleotides catalyzed by RNA polymerase II.
The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase II promoter by the addition of ribonucleotides catalyzed by RNA polymerase II.
Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.
Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.
Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.
Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.
Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.
Selection of a splice site by components of the assembling spliceosome.
Selection of a splice site by components of the assembling spliceosome.
Selection of a splice site by components of the assembling spliceosome.
Selection of a splice site by components of the assembling spliceosome.
The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
Any process in which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner.
Interacting selectively and non-covalently with a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.
Interacting selectively and non-covalently with a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.
Interacting selectively and non-covalently with a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.
Interacting selectively and non-covalently with a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.
The conversion of an adenosine residue to inosine in an RNA molecule by deamination.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
Any process involved in the assembly of the RNA polymerase III preinitiation complex (PIC) at an RNA polymerase III promoter region of a DNA template, resulting in the subsequent synthesis of RNA from that promoter. The initiation phase includes PIC assembly and the formation of the first few bonds in the RNA chain, including abortive initiation, which occurs when the first few nucleotides are repeatedly synthesized and then released. Promoter clearance, or release, is the transition between the initiation and elongation phases of transcription.
The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase III promoter by the addition of ribonucleotides catalyzed by RNA polymerase III.
The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase III promoter by the addition of ribonucleotides catalyzed by RNA polymerase III.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Hypermethylation of the 7-(mono)methylguanosine (m(7)G) cap structure at the 2' position of the guanosine residue to convert a mono-methylated cap to a 2,2,7-trimethylguanosine cap structure. This type of cap modification occurs on small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs) and is dependent on prior guanine-N7 methylation.
Splicing of tRNA substrates via recognition of the folded RNA structure that brings the 5' and 3' splice sites into proximity and cleavage of the RNA at both the 3' and 5' splice sites by an endonucleolytic mechanism, followed by ligation of the exons.
The synthesis of RNA from a mitochondrial DNA template, usually by a specific mitochondrial RNA polymerase.
A transcription initiation process that takes place at a promoter on the mitochondrial chromosome, and results in RNA synthesis by a mitochondrial RNA polymerase.
The extension of an RNA molecule after transcription initiation and promoter clearance at mitochondrial promoter by the addition of ribonucleotides catalyzed by a mitchondrial RNA polymerase.
The process in which the synthesis of an RNA molecule using a mitochondrial DNA template is completed.
The process in which the synthesis of an RNA molecule using a mitochondrial DNA template is completed.
Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules.
Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
Any mRNA 3'-end processing that involves the binding to and cleavage of a stem-loop structure. For example, histone mRNAs contain a highly conserved stem-loop sequence at the 3' end of the mRNA with a 6 base pairs (bp) stem and a 4-nt loop. The mRNA is cleaved between these two elements, after the fourth or fifth nucleotide, which is typically an adenosine.
The chemical reactions and pathways involving tRNA, transfer RNA, a class of relatively small RNA molecules responsible for mediating the insertion of amino acids into the sequence of nascent polypeptide chains during protein synthesis. Transfer RNA is characterized by the presence of many unusual minor bases, the function of which has not been completely established.
The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.
The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.
The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.
The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.
The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.
The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes.
A process in which RNA is transported to, or maintained in, a specific location.
A process in which RNA is transported to, or maintained in, a specific location.
The import of RNA from the cytoplasm to the nucleus.
The import of RNA from the cytoplasm to the nucleus.
The import of RNA from the cytoplasm to the nucleus.
The directed movement of RNA from the nucleus to the cytoplasm.
The directed movement of RNA from the nucleus to the cytoplasm.
The directed movement of RNA from the nucleus to the cytoplasm.
The directed movement of RNA from the nucleus to the cytoplasm.
The directed movement of mRNA from the nucleus to the cytoplasm.
The directed movement of mRNA from the nucleus to the cytoplasm.
The directed movement of mRNA from the nucleus to the cytoplasm.
The directed movement of mRNA from the nucleus to the cytoplasm.
The directed movement of rRNA from the nucleus to the cytoplasm; the rRNA is usually in the form of ribonucleoproteins.
The directed movement of rRNA from the nucleus to the cytoplasm; the rRNA is usually in the form of ribonucleoproteins.
The directed movement of rRNA from the nucleus to the cytoplasm; the rRNA is usually in the form of ribonucleoproteins.
The directed movement of rRNA from the nucleus to the cytoplasm; the rRNA is usually in the form of ribonucleoproteins.
The directed movement of snRNA from the nucleus to the cytoplasm.
The directed movement of snRNA from the nucleus to the cytoplasm.
The directed movement of snRNA from the nucleus to the cytoplasm.
The directed movement of snRNA from the nucleus to the cytoplasm.
The directed movement of tRNA from the nucleus to the cytoplasm.
The directed movement of tRNA from the nucleus to the cytoplasm.
The directed movement of tRNA from the nucleus to the cytoplasm.
The directed movement of tRNA from the nucleus to the cytoplasm.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.
The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid  group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.
The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a  class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA.
The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA.  The  2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling asparagine to asparaginyl-tRNA, catalyzed by asparaginyl-tRNA synthetase. The asparaginyl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an asparagine-accetping tRNA.
The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid  accetping tRNA.
The process of coupling cysteine to cysteinyl-tRNA, catalyzed by cysteinyl-tRNA synthetase. A cysteinyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a cysteine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling glutamate to glutamyl-tRNA, catalyzed by glutamyl-tRNA synthetase. The glutamyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamic acid-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling glutamine to glutaminyl-tRNA, catalyzed by glutaminyl-tRNA synthetase. The glutaminyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling glycine to glycyl-tRNA, catalyzed by glycyl-tRNA synthetase. The glycyll-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a glycine-accepting tRNA.
The process of coupling histidine to histidyl-tRNA, catalyzed by histidyl-tRNA synthetase. The histidyl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3''-OH group of a histidine-accetping tRNA.
The process of coupling isoleucine to isoleucyl-tRNA, catalyzed by isoleucyl-tRNA synthetase. The isoleucyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a isoleucine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA.
The process of coupling methionine to methionyl-tRNA, catalyzed by methionyl-tRNA synthetase. The methionyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a methionine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a  class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-accetping tRNA.
The process of coupling serine to seryl-tRNA, catalyzed by seryl-tRNA synthetase. The seryl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a serine-accetping tRNA.
The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a  class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-accetping tRNA.
The process of coupling tryptophan to tryptophanyl-tRNA, catalyzed by tryptophanyl-tRNA synthetase. The tryptophanyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tryptophan-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase.The tyrosyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.T
The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a  class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
Any process that modulates the frequency, rate or extent of translational initiation.
Any process that modulates the frequency, rate or extent of the translation of certain mRNAs involved in iron metabolism; regulated by the concentration of iron.
Any process that modulates the frequency, rate, extent or accuracy of translational elongation.
Any process that modulates the frequency, rate or extent of translational termination.
Any process that modulates the ability of the translational apparatus to interpret the genetic code.
Any process that modulates the ability of the translational apparatus to interpret the genetic code.
The continuation of translation beyond a stop codon by the use of a special tRNA that recognizes the UAG and UGA codons as modified amino acids, rather than as termination codons.
A mechanism whereby different proteins may result from a single mRNA molecule, due to a change in the parsing of three nucleotides per codon relative to an initiating AUG codon.
The process of assisting in the folding of a nascent peptide chain into its correct tertiary structure.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
The aggregation, arrangement and bonding together of a set of components to form a steroid hormone receptor complex, an intracellular receptor that binds steroid hormones. The complex is often a dimer, and forms after the steroid has bound the receptor.
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
The process of introducing a phosphate group on to a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.
The process of removing one or more phosphoric residues from a protein.
The transfer, from NAD, of ADP-ribose to protein amino acids.
The addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
The acetylation of the N-terminal amino acid of proteins.
The addition of an acetyl group to a non-terminal amino acid in a protein.
The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
The addition of a sulfate group as an ester to a protein amino acid.
The addition of a sulfate group as an ester to a protein amino acid.
The sulfation of peptidyl-tyrosine residues to form peptidyl-O4'-sulfo-L-tyrosine.
The addition of a methyl group to a protein amino acid. A methyl group is derived from methane by the removal of a hydrogen atom.
The methylation of the N-terminal amino acid of a protein.
The methylation of the C-terminal amino acid of a protein.
The removal of a methyl group, from a protein amino acid. A methyl group is derived from methane by the removal of a hydrogen atom.
The hydroxylation of peptidyl-aspartic acid to form peptidyl-hydroxyaspartic acid.
The hydroxylation of peptidyl-asparagine to form peptidyl-hydroxyasparagine.
A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
The chemical reactions and pathways resulting in the formation of dolichyl diphosphate, a diphosphorylated dolichol derivative.
The chemical reactions and pathways resulting in the formation of dolichyl diphosphate, a diphosphorylated dolichol derivative.
The chemical reactions and pathways resulting in the formation of dolichyl diphosphate, a diphosphorylated dolichol derivative.
The chemical reactions and pathways resulting in the formation of dolichyl diphosphate, a diphosphorylated dolichol derivative.
The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation.
The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation.
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
Addition of a carbohydrate or carbohydrate derivative unit via a nitrogen (N) atom of the N-terminal amino acid of a protein.
The covalent attachment of lipid groups to an amino acid in a protein.
The covalent attachment of lipid groups to an amino acid in a protein.
The covalent attachment of lipid groups to an amino acid in a protein.
The covalent attachment of a lipid group to the amino terminus of a protein.
The covalent attachment of a myristoyl group to the N-terminal amino acid residue of a protein.
The covalent attachment of a palmitoyl group to the N-terminal amino acid residue of a protein.
The covalent attachment of a lipid group to the carboxy terminus of a protein.
The covalent attachment of a prenyl group to a protein; geranyl, farnesyl, or geranylgeranyl groups may be added.
The covalent attachment of a prenyl group to a protein; geranyl, farnesyl, or geranylgeranyl groups may be added.
The covalent attachment of a prenyl group to a protein; geranyl, farnesyl, or geranylgeranyl groups may be added.
The covalent attachment of a farnesyl group to a protein.
The covalent attachment of a farnesyl group to a protein.
The covalent attachment of a farnesyl group to a protein.
The covalent attachment of a geranylgeranyl group to a protein.
The covalent attachment of a geranylgeranyl group to a protein.
The covalent attachment of a geranylgeranyl group to a protein.
The chemical reactions and pathways involving glycosylphosphatidylinositol anchors, molecular mechanisms for attaching membrane proteins to the lipid bilayer of cell membranes. Structurally they consist of a molecule of phosphatidylinositol to which is linked, via the C-6 hydroxyl of the inositol, a carbohydrate chain. This chain is in turn linked to the protein through an ethanolamine phosphate group, the amino group of which is in amide linkage with the C-terminal carboxyl of the protein chain, the phosphate group being esterified to the C-6 hydroxyl of the terminal mannose of the core carbohydrate chain.
The chemical reactions and pathways involving glycosylphosphatidylinositol anchors, molecular mechanisms for attaching membrane proteins to the lipid bilayer of cell membranes. Structurally they consist of a molecule of phosphatidylinositol to which is linked, via the C-6 hydroxyl of the inositol, a carbohydrate chain. This chain is in turn linked to the protein through an ethanolamine phosphate group, the amino group of which is in amide linkage with the C-terminal carboxyl of the protein chain, the phosphate group being esterified to the C-6 hydroxyl of the terminal mannose of the core carbohydrate chain.
The chemical reactions and pathways involving glycosylphosphatidylinositol anchors, molecular mechanisms for attaching membrane proteins to the lipid bilayer of cell membranes. Structurally they consist of a molecule of phosphatidylinositol to which is linked, via the C-6 hydroxyl of the inositol, a carbohydrate chain. This chain is in turn linked to the protein through an ethanolamine phosphate group, the amino group of which is in amide linkage with the C-terminal carboxyl of the protein chain, the phosphate group being esterified to the C-6 hydroxyl of the terminal mannose of the core carbohydrate chain.
The chemical reactions and pathways involving glycosylphosphatidylinositol anchors, molecular mechanisms for attaching membrane proteins to the lipid bilayer of cell membranes. Structurally they consist of a molecule of phosphatidylinositol to which is linked, via the C-6 hydroxyl of the inositol, a carbohydrate chain. This chain is in turn linked to the protein through an ethanolamine phosphate group, the amino group of which is in amide linkage with the C-terminal carboxyl of the protein chain, the phosphate group being esterified to the C-6 hydroxyl of the terminal mannose of the core carbohydrate chain.
The chemical reactions and pathways involving glycosylphosphatidylinositol anchors, molecular mechanisms for attaching membrane proteins to the lipid bilayer of cell membranes. Structurally they consist of a molecule of phosphatidylinositol to which is linked, via the C-6 hydroxyl of the inositol, a carbohydrate chain. This chain is in turn linked to the protein through an ethanolamine phosphate group, the amino group of which is in amide linkage with the C-terminal carboxyl of the protein chain, the phosphate group being esterified to the C-6 hydroxyl of the terminal mannose of the core carbohydrate chain.
The chemical reactions and pathways involving glycosylphosphatidylinositol anchors, molecular mechanisms for attaching membrane proteins to the lipid bilayer of cell membranes. Structurally they consist of a molecule of phosphatidylinositol to which is linked, via the C-6 hydroxyl of the inositol, a carbohydrate chain. This chain is in turn linked to the protein through an ethanolamine phosphate group, the amino group of which is in amide linkage with the C-terminal carboxyl of the protein chain, the phosphate group being esterified to the C-6 hydroxyl of the terminal mannose of the core carbohydrate chain.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.
The GPI anchor metabolic process that results in enzymatic cleavage of the anchor, releasing an anchored protein from the membrane.
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
Addition of a single ubiquitin group to a protein.
Addition of a single ubiquitin group to a protein.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
The removal of sugar residues from a glycosylated protein.
The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving amino acids.
The chemical reactions and pathways involving alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of alanine, 2-aminopropanoic acid.
The chemical reactions and pathways involving arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the breakdown of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the breakdown of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways resulting in the breakdown of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways involving asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of asparagine, 2-amino-3-carbamoylpropanoic acid.
The chemical reactions and pathways involving aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the formation of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the formation of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the formation of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the formation of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the breakdown of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the breakdown of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways resulting in the breakdown of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
The chemical reactions and pathways involving cysteine, 2-amino-3-mercaptopropanoic acid.
The chemical reactions and pathways resulting in the formation of cysteine from other compounds, including serine.
The chemical reactions and pathways resulting in the formation of cysteine from other compounds, including serine.
The chemical reactions and pathways resulting in the formation of cysteine from other compounds, including serine.
The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, the anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxoglutarate.
The chemical reactions and pathways resulting in the formation of succinate from glutamate. Also known as GABA (gamma-aminobutyrate) shunt since it channels glutamate into the TCA cycle bypassing two steps of that cycle. There are three enzymes involved in the GABA shunt: glutamate decarboxylase (GAD), GABA aminotransferase (GABA-TA), and succinate semialdehyde dehydrogenase (SSADH). These three enzymes acting in concert to convert glutamate into succinate. The GABA shunt is predominantly associated with neurotransmission in the mammalian brain. It is also present in nonneuronal cells, in plants, in unicellular eukaryotes, and in prokaryotes.
The chemical reactions and pathways resulting in the formation of succinate from glutamate. Also known as GABA (gamma-aminobutyrate) shunt since it channels glutamate into the TCA cycle bypassing two steps of that cycle. There are three enzymes involved in the GABA shunt: glutamate decarboxylase (GAD), GABA aminotransferase (GABA-TA), and succinate semialdehyde dehydrogenase (SSADH). These three enzymes acting in concert to convert glutamate into succinate. The GABA shunt is predominantly associated with neurotransmission in the mammalian brain. It is also present in nonneuronal cells, in plants, in unicellular eukaryotes, and in prokaryotes.
The chemical reactions and pathways resulting in the formation of succinate from glutamate. Also known as GABA (gamma-aminobutyrate) shunt since it channels glutamate into the TCA cycle bypassing two steps of that cycle. There are three enzymes involved in the GABA shunt: glutamate decarboxylase (GAD), GABA aminotransferase (GABA-TA), and succinate semialdehyde dehydrogenase (SSADH). These three enzymes acting in concert to convert glutamate into succinate. The GABA shunt is predominantly associated with neurotransmission in the mammalian brain. It is also present in nonneuronal cells, in plants, in unicellular eukaryotes, and in prokaryotes.
The chemical reactions and pathways resulting in the formation of succinate from glutamate. Also known as GABA (gamma-aminobutyrate) shunt since it channels glutamate into the TCA cycle bypassing two steps of that cycle. There are three enzymes involved in the GABA shunt: glutamate decarboxylase (GAD), GABA aminotransferase (GABA-TA), and succinate semialdehyde dehydrogenase (SSADH). These three enzymes acting in concert to convert glutamate into succinate. The GABA shunt is predominantly associated with neurotransmission in the mammalian brain. It is also present in nonneuronal cells, in plants, in unicellular eukaryotes, and in prokaryotes.
The chemical reactions and pathways resulting in the formation of succinate from glutamate. Also known as GABA (gamma-aminobutyrate) shunt since it channels glutamate into the TCA cycle bypassing two steps of that cycle. There are three enzymes involved in the GABA shunt: glutamate decarboxylase (GAD), GABA aminotransferase (GABA-TA), and succinate semialdehyde dehydrogenase (SSADH). These three enzymes acting in concert to convert glutamate into succinate. The GABA shunt is predominantly associated with neurotransmission in the mammalian brain. It is also present in nonneuronal cells, in plants, in unicellular eukaryotes, and in prokaryotes.
The chemical reactions and pathways resulting in the formation of succinate from glutamate. Also known as GABA (gamma-aminobutyrate) shunt since it channels glutamate into the TCA cycle bypassing two steps of that cycle. There are three enzymes involved in the GABA shunt: glutamate decarboxylase (GAD), GABA aminotransferase (GABA-TA), and succinate semialdehyde dehydrogenase (SSADH). These three enzymes acting in concert to convert glutamate into succinate. The GABA shunt is predominantly associated with neurotransmission in the mammalian brain. It is also present in nonneuronal cells, in plants, in unicellular eukaryotes, and in prokaryotes.
The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the formation of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the breakdown of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the breakdown of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways resulting in the breakdown of glutamine, 2-amino-4-carbamoylbutanoic acid.
The chemical reactions and pathways involving glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the formation of glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the formation of glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the formation of glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the formation of glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the breakdown of glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the breakdown of glycine, aminoethanoic acid.
The chemical reactions and pathways resulting in the breakdown of glycine, aminoethanoic acid.
The chemical reactions and pathways involving histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
The chemical reactions and pathways involving isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
The chemical reactions and pathways resulting in the breakdown of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
The chemical reactions and pathways resulting in the breakdown of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
The chemical reactions and pathways resulting in the breakdown of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
The chemical reactions and pathways involving leucine, 2-amino-4-methylpentanoic acid.
The chemical reactions and pathways resulting in the breakdown of leucine, 2-amino-4-methylpentanoic acid.
The chemical reactions and pathways resulting in the breakdown of leucine, 2-amino-4-methylpentanoic acid.
The chemical reactions and pathways resulting in the breakdown of leucine, 2-amino-4-methylpentanoic acid.
The chemical reactions and pathways involving lysine, 2,6-diaminohexanoic acid.
The chemical reactions and pathways resulting in the breakdown of lysine, 2,6-diaminohexanoic acid.
The chemical reactions and pathways resulting in the breakdown of lysine, 2,6-diaminohexanoic acid.
The chemical reactions and pathways resulting in the breakdown of lysine, 2,6-diaminohexanoic acid.
The chemical reactions and pathways involving methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways involving methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways involving methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism.
The chemical reactions and pathways resulting in the formation of S-adenosylmethioninamine, (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt.
The chemical reactions and pathways resulting in the formation of S-adenosylmethioninamine, (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt.
The chemical reactions and pathways resulting in the formation of S-adenosylmethioninamine, (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt.
The chemical reactions and pathways resulting in the formation of S-adenosylmethioninamine, (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt.
The chemical reactions and pathways resulting in the formation of S-adenosylmethioninamine, (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt.
The chemical reactions and pathways involving L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways involving L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways involving L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
The chemical reactions and pathways involving proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the breakdown of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the breakdown of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the breakdown of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
The chemical reactions and pathways involving L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the breakdown of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the breakdown of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the breakdown of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways involving threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways involving threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways involving threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the breakdown of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the breakdown of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways resulting in the breakdown of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
The chemical reactions and pathways involving tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
The chemical reactions and pathways involving tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the formation of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the formation of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the formation of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the formation of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways resulting in the breakdown of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
The chemical reactions and pathways involving valine, 2-amino-3-methylbutanoic acid.
The chemical reactions and pathways resulting in the breakdown of valine, 2-amino-3-methylbutanoic acid.
The chemical reactions and pathways resulting in the breakdown of valine, 2-amino-3-methylbutanoic acid.
The chemical reactions and pathways resulting in the breakdown of valine, 2-amino-3-methylbutanoic acid.
The chemical reactions and pathways involving compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways involving compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways involving compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways involving compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways involving compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways involving compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways occurring at the level of individual cells involving any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways involving any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways involving any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the formation of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the formation of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the formation of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the formation of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the formation of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the breakdown of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the breakdown of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the breakdown of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways resulting in the breakdown of any betaine, the N-trimethyl derivative of an amino acid.
The chemical reactions and pathways involving ethanolamine (2-aminoethanol), an important water-soluble base of phospholipid (phosphatidylethanolamine).
The chemical reactions and pathways involving ethanolamine (2-aminoethanol), an important water-soluble base of phospholipid (phosphatidylethanolamine).
The chemical reactions and pathways resulting in the breakdown of acetylcholine, the acetic acid ester of the organic base choline.
The chemical reactions and pathways resulting in the breakdown of acetylcholine, the acetic acid ester of the organic base choline.
The chemical reactions and pathways resulting in the breakdown of acetylcholine, the acetic acid ester of the organic base choline.
The chemical reactions and pathways involving melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom.
The chemical reactions and pathways resulting in the formation of melanin from other compounds, including tyrosine.
The chemical reactions and pathways resulting in the formation of melanin from other compounds, including tyrosine.
The chemical reactions and pathways resulting in the formation of melanin from other compounds, including tyrosine.
The chemical reactions and pathways involving any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the formation of dopamine (3,4-dihydroxyphenylethylamine) from L-tyrosine, via the metabolic precursor 3,4-dihydroxy-L-phenylalanine (L-dopa). Dopamine is a catecholamine neurotransmitter and a metabolic precursor of norepinephrine and epinephrine.
The chemical reactions and pathways resulting in the formation of dopamine (3,4-dihydroxyphenylethylamine) from L-tyrosine, via the metabolic precursor 3,4-dihydroxy-L-phenylalanine (L-dopa). Dopamine is a catecholamine neurotransmitter and a metabolic precursor of norepinephrine and epinephrine.
The chemical reactions and pathways resulting in the formation of dopamine (3,4-dihydroxyphenylethylamine) from L-tyrosine, via the metabolic precursor 3,4-dihydroxy-L-phenylalanine (L-dopa). Dopamine is a catecholamine neurotransmitter and a metabolic precursor of norepinephrine and epinephrine.
The chemical reactions and pathways involving indolalkylamines, indole or indole derivatives containing a primary, secondary, or tertiary amine group.
The chemical reactions and pathways involving indolalkylamines, indole or indole derivatives containing a primary, secondary, or tertiary amine group.
The chemical reactions and pathways involving indolalkylamines, indole or indole derivatives containing a primary, secondary, or tertiary amine group.
The chemical reactions and pathways resulting in the formation from tryptophan of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the formation from tryptophan of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the formation from tryptophan of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The process in which the tryptophan 5-monooxygenase enzyme is changed so that it can carry out its enzymatic activity.
The chemical reactions and pathways resulting in the formation of octopamine, 1-(p-hydroxyphenyl)-2-aminoethanol. The D enantiomer is about one-tenth as active as norepinephrine and is found in the salivary glands of Octopus and Eledone species.
The chemical reactions and pathways resulting in the formation of octopamine, 1-(p-hydroxyphenyl)-2-aminoethanol. The D enantiomer is about one-tenth as active as norepinephrine and is found in the salivary glands of Octopus and Eledone species.
The chemical reactions and pathways resulting in the formation of octopamine, 1-(p-hydroxyphenyl)-2-aminoethanol. The D enantiomer is about one-tenth as active as norepinephrine and is found in the salivary glands of Octopus and Eledone species.
The chemical reactions and pathways resulting in the formation of octopamine, 1-(p-hydroxyphenyl)-2-aminoethanol. The D enantiomer is about one-tenth as active as norepinephrine and is found in the salivary glands of Octopus and Eledone species.
The formation of either of the compounds secreted by the thyroid gland, mainly thyroxine and triiodothyronine. This is achieved by the iodination and joining of tyrosine molecules to form the precursor thyroglobin, proteolysis of this precursor gives rise to the thyroid hormones.
The chemical reactions and pathways involving ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the formation of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the formation of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the formation of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the formation of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the breakdown of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the breakdown of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways resulting in the breakdown of ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
The chemical reactions and pathways involving polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the formation of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the formation of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the formation of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the formation of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the formation of spermine, a polybasic amine found in human sperm, in ribosomes and in some viruses and involved in nucleic acid packaging.
The chemical reactions and pathways resulting in the formation of spermine, a polybasic amine found in human sperm, in ribosomes and in some viruses and involved in nucleic acid packaging.
The chemical reactions and pathways resulting in the formation of spermine, a polybasic amine found in human sperm, in ribosomes and in some viruses and involved in nucleic acid packaging.
The chemical reactions and pathways resulting in the formation of spermine, a polybasic amine found in human sperm, in ribosomes and in some viruses and involved in nucleic acid packaging.
The chemical reactions and pathways resulting in the breakdown of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the breakdown of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways resulting in the breakdown of polyamines, any organic compound containing two or more amino groups.
The chemical reactions and pathways involving phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways involving creatine (N-(aminoiminomethyl)-N-methylglycine), a compound synthesized from the amino acids arginine, glycine, and methionine that occurs in muscle.
The chemical reactions and pathways resulting in the formation of creatine, N-[amino(imino)methyl]-N-methylglycine. Creatine is formed by a process beginning with amidino group transfer from L-arginine to glycine to form guanidinoacetate, followed by methyl group transfer from S-adenosyl-L-methionine to guanidinoacetate; it is then is phosphorylated to form a pool that stores high energy phosphate for the replenishment of ATP during periods of high, or fluctuating energy demand. In animals, most creatine is transported to and used in muscle.
The chemical reactions and pathways resulting in the formation of creatine, N-[amino(imino)methyl]-N-methylglycine. Creatine is formed by a process beginning with amidino group transfer from L-arginine to glycine to form guanidinoacetate, followed by methyl group transfer from S-adenosyl-L-methionine to guanidinoacetate; it is then is phosphorylated to form a pool that stores high energy phosphate for the replenishment of ATP during periods of high, or fluctuating energy demand. In animals, most creatine is transported to and used in muscle.
The chemical reactions and pathways resulting in the formation of creatine, N-[amino(imino)methyl]-N-methylglycine. Creatine is formed by a process beginning with amidino group transfer from L-arginine to glycine to form guanidinoacetate, followed by methyl group transfer from S-adenosyl-L-methionine to guanidinoacetate; it is then is phosphorylated to form a pool that stores high energy phosphate for the replenishment of ATP during periods of high, or fluctuating energy demand. In animals, most creatine is transported to and used in muscle.
The chemical reactions and pathways resulting in the formation of creatine, N-[amino(imino)methyl]-N-methylglycine. Creatine is formed by a process beginning with amidino group transfer from L-arginine to glycine to form guanidinoacetate, followed by methyl group transfer from S-adenosyl-L-methionine to guanidinoacetate; it is then is phosphorylated to form a pool that stores high energy phosphate for the replenishment of ATP during periods of high, or fluctuating energy demand. In animals, most creatine is transported to and used in muscle.
The chemical reactions and pathways resulting in the breakdown of creatinine, 2-amino-1,5-dihydro-1-methyl-4H-imidazol-4-one, an end product of creatine metabolism and a normal constituent of urine.
The chemical reactions and pathways resulting in the breakdown of creatinine, 2-amino-1,5-dihydro-1-methyl-4H-imidazol-4-one, an end product of creatine metabolism and a normal constituent of urine.
The chemical reactions and pathways resulting in the breakdown of creatinine, 2-amino-1,5-dihydro-1-methyl-4H-imidazol-4-one, an end product of creatine metabolism and a normal constituent of urine.
The chemical reactions and pathways involving phosphocreatine, a phosphagen of creatine present in high concentration in striated muscle which is synthesized and broken down by creatine phosphokinase to buffer ATP concentration. It acts as an immediate energy reserve for muscle.
The chemical reactions and pathways involving phosphoarginine, a phosphagen of L-arginine with phosphoric acid containing the phosphoamide bond. It is a source of energy in the contraction of muscle in invertebrates, corresponding to phosphocreatine in the muscles of vertebrates.
The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.
The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.
The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.
The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.
The directed movement of a ribosomal protein from the cytoplasm into the nucleus, across the nuclear membrane. At least some ribosomal proteins, including rpl12, uses the importin 11 pathway as a major route into the nucleus.
The directed movement of a ribosomal protein from the cytoplasm into the nucleus, across the nuclear membrane. At least some ribosomal proteins, including rpl12, uses the importin 11 pathway as a major route into the nucleus.
The directed movement of a ribosomal protein from the cytoplasm into the nucleus, across the nuclear membrane. At least some ribosomal proteins, including rpl12, uses the importin 11 pathway as a major route into the nucleus.
The directed movement of a protein from the nucleus into the cytoplasm.
The directed movement of a protein from the nucleus into the cytoplasm.
The directed movement of a protein from the nucleus into the cytoplasm.
The directed movement of a protein from the nucleus into the cytoplasm.
The directed movement of a protein from the nucleus into the cytoplasm.
The directed movement of a protein from the nucleus into the cytoplasm.
The process of directing proteins towards a membrane, usually using signals contained within the protein.
The process of directing proteins towards a membrane, usually using signals contained within the protein.
The targeting of proteins to a membrane that occurs during translation. The transport of most secretory proteins, particularly those with more than 100 amino acids, into the endoplasmic reticulum lumen occurs in this manner, as does the import of some proteins into mitochondria.
The targeting of proteins to a membrane that occurs during translation. The transport of most secretory proteins, particularly those with more than 100 amino acids, into the endoplasmic reticulum lumen occurs in this manner, as does the import of some proteins into mitochondria.
The targeting of proteins to a membrane that occurs during translation. The transport of most secretory proteins, particularly those with more than 100 amino acids, into the endoplasmic reticulum lumen occurs in this manner, as does the import of some proteins into mitochondria.
The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
The process in which an SRP-bound ribosome forms a complex with the SRP receptor in the ER membrane, allowing the ribosome to bind to the membrane, during cotranslational membrane targeting.
The process in which an SRP-bound ribosome forms a complex with the SRP receptor in the ER membrane, allowing the ribosome to bind to the membrane, during cotranslational membrane targeting.
The process in which an SRP-bound ribosome forms a complex with the SRP receptor in the ER membrane, allowing the ribosome to bind to the membrane, during cotranslational membrane targeting.
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
The process in which SRP binds to the signal peptide in a nascent protein, causing protein elongation to pause, during cotranslational membrane targeting.
The process in which SRP binds to the signal peptide in a nascent protein, causing protein elongation to pause, during cotranslational membrane targeting.
The process in which SRP binds to the signal peptide in a nascent protein, causing protein elongation to pause, during cotranslational membrane targeting.
The removal of the signal peptide from a nascent protein during cotranslational membrane targeting.
The removal of the signal peptide from a nascent protein during cotranslational membrane targeting.
The removal of the signal peptide from a nascent protein during cotranslational membrane targeting.
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
The process of directing proteins towards the lysosome using signals contained within the protein.
The process of directing proteins towards the vacuole, usually using signals contained within the protein.
The process of directing proteins towards the vacuole, usually using signals contained within the protein.
The process of directing proteins towards the vacuole, usually using signals contained within the protein.
The process of directing proteins towards the vacuole, usually using signals contained within the protein.
Protein processing that takes place in the vacuole. Most protein processing in the vacuole represents proteolytic cleavage of precursors to form active enzymes.
Protein processing that takes place in the vacuole. Most protein processing in the vacuole represents proteolytic cleavage of precursors to form active enzymes.
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
The cleavage of peptide bonds in proteins, usually near the N terminus, contributing to the process of import into the mitochondrion. Several different peptidases mediate cleavage of proteins destined for different mitochondrial compartments.
The cleavage of peptide bonds in proteins, usually near the N terminus, contributing to the process of import into the mitochondrion. Several different peptidases mediate cleavage of proteins destined for different mitochondrial compartments.
The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
Interacting selectively and non-covalently with a lipid.
The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
The chemical reactions and pathways resulting in the formation of hexadecanal, the C16 straight chain aldehyde.
The chemical reactions and pathways resulting in the formation of hexadecanal, the C16 straight chain aldehyde.
The chemical reactions and pathways resulting in the formation of hexadecanal, the C16 straight chain aldehyde.
The chemical reactions and pathways resulting in the formation of hexadecanal, the C16 straight chain aldehyde.
The chemical reactions and pathways resulting in the formation of hexadecanal, the C16 straight chain aldehyde.
The chemical reactions and pathways resulting in the formation of hexadecanal, the C16 straight chain aldehyde.
A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group.
The chemical reactions and pathways involving neutral lipids, lipids only soluble in solvents of very low polarity.
The chemical reactions and pathways involving acylglycerol, any mono-, di- or triester of glycerol with (one or more) fatty acids.
The chemical reactions and pathways involving acylglycerol, any mono-, di- or triester of glycerol with (one or more) fatty acids.
The chemical reactions and pathways involving acylglycerol, any mono-, di- or triester of glycerol with (one or more) fatty acids.
The chemical reactions and pathways resulting in the formation of monoacylglycerol, any ester of glycerol in which any one of its hydroxyl groups has been acylated with a fatty acid, the other being non-esterified.
The chemical reactions and pathways resulting in the formation of monoacylglycerol, any ester of glycerol in which any one of its hydroxyl groups has been acylated with a fatty acid, the other being non-esterified.
The chemical reactions and pathways resulting in the formation of monoacylglycerol, any ester of glycerol in which any one of its hydroxyl groups has been acylated with a fatty acid, the other being non-esterified.
The chemical reactions and pathways resulting in the formation of monoacylglycerol, any ester of glycerol in which any one of its hydroxyl groups has been acylated with a fatty acid, the other being non-esterified.
The chemical reactions and pathways resulting in the formation of monoacylglycerol, any ester of glycerol in which any one of its hydroxyl groups has been acylated with a fatty acid, the other being non-esterified.
The chemical reactions and pathways resulting in the formation of monoacylglycerol, any ester of glycerol in which any one of its hydroxyl groups has been acylated with a fatty acid, the other being non-esterified.
The chemical reactions and pathways involving triglyceride, any triester of glycerol. The three fatty acid residues may all be the same or differ in any permutation. Triglycerides are important components of plant oils, animal fats and animal plasma lipoproteins.
The chemical reactions and pathways involving triglyceride, any triester of glycerol. The three fatty acid residues may all be the same or differ in any permutation. Triglycerides are important components of plant oils, animal fats and animal plasma lipoproteins.
The chemical reactions and pathways involving triglyceride, any triester of glycerol. The three fatty acid residues may all be the same or differ in any permutation. Triglycerides are important components of plant oils, animal fats and animal plasma lipoproteins.
The release of triglycerides, any triester of glycerol, from storage within cells or tissues, making them available for metabolism.
The chemical reactions and pathways involving membrane lipids, any lipid found in or associated with a biological membrane.
The chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester.
The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine.
The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine.
The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine.
The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine.
The chemical reactions and pathways involving phosphatidyl-N-monomethylethanolamine (PMME), a derivative of phosphatidylethanolamine with a methylated amine group.
The chemical reactions and pathways involving phosphatidyl-N-monomethylethanolamine (PMME), a derivative of phosphatidylethanolamine with a methylated amine group.
The chemical reactions and pathways involving phosphatidyl-N-monomethylethanolamine (PMME), a derivative of phosphatidylethanolamine with a methylated amine group.
The chemical reactions and pathways involving phosphatidyl-N-monomethylethanolamine (PMME), a derivative of phosphatidylethanolamine with a methylated amine group.
The chemical reactions and pathways involving phosphatidyl-N-monomethylethanolamine (PMME), a derivative of phosphatidylethanolamine with a methylated amine group.
The chemical reactions and pathways involving phosphatidyl-N-monomethylethanolamine (PMME), a derivative of phosphatidylethanolamine with a methylated amine group.
A phosphatidylethanolamine biosynthetic process that proceeds via the enzymatic action of dihydrosphingosine phosphate lyase.
The transfer of a phospholipid from its site of synthesis to the plasma membrane.
The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue.
The chemical reactions and pathways resulting in the formation of diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
The chemical reactions and pathways resulting in the formation of diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
The chemical reactions and pathways resulting in the formation of diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
The chemical reactions and pathways resulting in the formation of diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
The chemical reactions and pathways resulting in the formation of diacylglycerol, a glyceride in which any two of the R groups (positions not specified) are acyl groups while the remaining R group can be either H or an alkyl group.
The chemical reactions and pathways involving any 1,2-diacyl-sn-glycero-3-phosphocholine, the compounds most commonly designated lecithin.
The chemical reactions and pathways involving any 1,2-diacyl-sn-glycero-3-phosphocholine, the compounds most commonly designated lecithin.
The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.
The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.
The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.
The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids.
The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
The phosphatidylcholine biosynthetic process that begins with the phosphorylation of choline and ends with the combination of CDP-choline with diacylglycerol to form phosphatidylcholine.
The phosphatidylcholine biosynthetic process that begins with the phosphorylation of choline and ends with the combination of CDP-choline with diacylglycerol to form phosphatidylcholine.
The chemical reactions and pathways involving phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. They are important constituents of cell membranes.
The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the breakdown of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the breakdown of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the breakdown of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways involving glycerol ethers, any anhydride formed between two organic hydroxy compounds, one of which is glycerol.
The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli.
The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli.
The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli.
The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli.
The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli.
The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli.
The chemical reactions and pathways involving glycolipids, a class of 1,2-di-O-acylglycerols joined at oxygen 3 by a glycosidic linkage to a carbohydrate part (usually a mono-, di- or tri-saccharide). Some substances classified as bacterial glycolipids have the sugar group acylated by one or more fatty acids and the glycerol group may be absent.
The chemical reactions and pathways involving sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways involving 3-keto-sphinganine, a derivative of sphinganine with a ketone group at C3. It is an intermediate in the synthesis of sphingosine.
The chemical reactions and pathways involving 3-keto-sphinganine, a derivative of sphinganine with a ketone group at C3. It is an intermediate in the synthesis of sphingosine.
The chemical reactions and pathways involving 3-keto-sphinganine, a derivative of sphinganine with a ketone group at C3. It is an intermediate in the synthesis of sphingosine.
The chemical reactions and pathways involving sphinganine, D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways involving sphinganine, D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways involving sphinganine, D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways involving sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways involving sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways involving sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways resulting in the formation of sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways resulting in the formation of sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways resulting in the formation of sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways resulting in the formation of sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways resulting in the formation of sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways resulting in the formation of sphinganine-1-phosphate, the phosphorylated derivative of D-erythro-2-amino-1,3-octadecanediol.
The chemical reactions and pathways involving sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues.
The chemical reactions and pathways involving sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues.
The chemical reactions and pathways involving sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues.
The chemical reactions and pathways involving sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues.
The chemical reactions and pathways involving sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues.
The chemical reactions and pathways involving phytosphingosine, (2S,3S,4R)-2-aminooctadecane-1,3,4-triol, a constituent of many plant sphingolipids.
The chemical reactions and pathways involving ceramides, any N-acylated sphingoid.
The chemical reactions and pathways involving inositol phosphoceramides, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group.
The chemical reactions and pathways involving inositol phosphoceramides, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group.
The chemical reactions and pathways involving inositol phosphoceramides, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group.
The chemical reactions and pathways involving inositol phosphoceramides, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl-inositol phosphorylceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains a phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl diphosphorylinositol ceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains two phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl diphosphorylinositol ceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains two phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving mannosyl diphosphorylinositol ceramide, any lipid with a phosphodiester bridge between an inositol residue and the ceramide group which contains two phosphoryl (-P(O)=) groups and a mannose derivative.
The chemical reactions and pathways involving glycosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of a monosaccharide (or derivative) by a ceramide group.
The chemical reactions and pathways involving glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group. They are neutral glycolipids containing equimolar amounts of fatty acid, glucose, and sphingosine or a sphingosine derivative.
The chemical reactions and pathways resulting in the formation of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways resulting in the formation of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways resulting in the formation of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways resulting in the formation of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways resulting in the breakdown of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways resulting in the breakdown of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways resulting in the breakdown of glucosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of glucose by a ceramide group.
The chemical reactions and pathways involving galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the formation of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the formation of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the formation of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the formation of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the breakdown of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the breakdown of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways resulting in the breakdown of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
The chemical reactions and pathways involving sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine, any of a class of phospholipids in which the amino group of sphingosine is in amide linkage with one of several fatty acids, while the terminal hydroxyl group of sphingosine is esterified to phosphorylcholine.
The chemical reactions and pathways resulting in the breakdown of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways resulting in the breakdown of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways resulting in the breakdown of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine.
The chemical reactions and pathways involving glycosphingolipids, any compound with residues of sphingoid and at least one monosaccharide.
The chemical reactions and pathways resulting in the formation of glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide.
The chemical reactions and pathways resulting in the formation of glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide.
The chemical reactions and pathways resulting in the formation of glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide.
The chemical reactions and pathways resulting in the formation of glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide.
The chemical reactions and pathways resulting in the breakdown of ganglioside, a ceramide oligosaccharide carrying, in addition to other sugar residues, one or more sialic residues.
The chemical reactions and pathways resulting in the breakdown of ganglioside, a ceramide oligosaccharide carrying, in addition to other sugar residues, one or more sialic residues.
The chemical reactions and pathways resulting in the breakdown of ganglioside, a ceramide oligosaccharide carrying, in addition to other sugar residues, one or more sialic residues.
The chemical reactions and pathways involving icosanoids, any of a group of C20 polyunsaturated fatty acids.
The chemical reactions and pathways involving icosanoids, any of a group of C20 polyunsaturated fatty acids.
The chemical reactions and pathways involving icosanoids, any of a group of C20 polyunsaturated fatty acids.
The chemical reactions and pathways involving leukotriene, a pharmacologically active substance derived from a polyunsaturated fatty acid, such as arachidonic acid.
The chemical reactions and pathways involving prostanoids, any compound based on or derived from the prostanoate structure.
The chemical reactions and pathways involving prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring due to the formation of a bond between two carbons of a fatty acid. They have a wide range of biological activities.
The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.
The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.
The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.
The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.
The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
The chemical reactions and pathways resulting in the formation of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the formation of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the formation of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the formation of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the formation of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the formation of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the formation of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the formation of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the formation of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the formation of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the formation of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the formation of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the formation of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the formation of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the formation of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the formation of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the formation of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the formation of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the formation of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the formation of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the formation of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the formation of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the formation of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the formation of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the formation of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the formation of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the formation of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the formation of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the breakdown of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
The chemical reactions and pathways resulting in the breakdown of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
The chemical reactions and pathways resulting in the breakdown of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
The chemical reactions and pathways resulting in the breakdown of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the breakdown of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the breakdown of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
The chemical reactions and pathways resulting in the breakdown of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the breakdown of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the breakdown of ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects.
The chemical reactions and pathways resulting in the breakdown of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the breakdown of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the breakdown of androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways resulting in the breakdown of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the breakdown of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the breakdown of mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the breakdown of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the breakdown of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways resulting in the breakdown of glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol.
The chemical reactions and pathways involving sesquiterpenoid compounds, terpenoids with three isoprene units.
The chemical reactions and pathways resulting in the formation of the sesquiterpenoid alcohol farnesol, 3,7,11-trimethyl-2,6,10,dodecatrien-1-ol.
The chemical reactions and pathways resulting in the formation of the sesquiterpenoid alcohol farnesol, 3,7,11-trimethyl-2,6,10,dodecatrien-1-ol.
The chemical reactions and pathways resulting in the formation of the sesquiterpenoid alcohol farnesol, 3,7,11-trimethyl-2,6,10,dodecatrien-1-ol.
The chemical reactions and pathways resulting in the formation of the sesquiterpenoid alcohol farnesol, 3,7,11-trimethyl-2,6,10,dodecatrien-1-ol.
The chemical reactions and pathways involving juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the formation of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the formation of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the formation of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the formation of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the breakdown of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the breakdown of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways resulting in the breakdown of juvenile hormones, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis.
The chemical reactions and pathways involving isoprenoid compounds, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways involving isoprenoid compounds, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways involving isoprenoid compounds, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways involving isoprenoid compounds, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways involving isoprenoid compounds, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways involving isoprenoid compounds, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways involving terpenoids, any member of a class of compounds characterized by an isoprenoid chemical structure and including derivatives with various functional groups.
The chemical reactions and pathways involving triterpenoid compounds, terpenoids with six isoprene units.
The chemical reactions and pathways involving triterpenoid compounds, terpenoids with six isoprene units.
The chemical reactions and pathways involving triterpenoid compounds, terpenoids with six isoprene units.
The chemical reactions and pathways resulting in the formation of hydrocarbons that make up the cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of hydrocarbons that make up the cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of hydrocarbons that make up the cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of hydrocarbons that make up the cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells.
The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells.
The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells.
The chemical reactions and pathways resulting in the formation of eye pigments, any general or particular coloring matter in living organisms, found or utilized in the eye.
The chemical reactions and pathways resulting in the formation of eye pigments, any general or particular coloring matter in living organisms, found or utilized in the eye.
The chemical reactions and pathways resulting in the formation of eye pigments, any general or particular coloring matter in living organisms, found or utilized in the eye.
The chemical reactions and pathways resulting in the formation of eye pigments, any general or particular coloring matter in living organisms, found or utilized in the eye.
The chemical reactions and pathways resulting in the formation of ommochromes, any of a large group of natural polycyclic pigments commonly found in the Arthropoda, particularly in the ommatidia of the compound eye.
The chemical reactions and pathways resulting in the formation of ommochromes, any of a large group of natural polycyclic pigments commonly found in the Arthropoda, particularly in the ommatidia of the compound eye.
The chemical reactions and pathways resulting in the formation of ommochromes, any of a large group of natural polycyclic pigments commonly found in the Arthropoda, particularly in the ommatidia of the compound eye.
The chemical reactions and pathways resulting in the formation of ommochromes, any of a large group of natural polycyclic pigments commonly found in the Arthropoda, particularly in the ommatidia of the compound eye.
The chemical reactions and pathways resulting in the formation of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the formation of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the formation of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the formation of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the formation of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the formation of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
The chemical reactions and pathways involving coenzymes, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
The chemical reactions and pathways involving coenzymes, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
The chemical reactions and pathways involving coenzymes, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
The chemical reactions and pathways involving coenzymes, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
The chemical reactions and pathways involving coenzymes, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
The chemical reactions and pathways involving coenzymes, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
The chemical reactions and pathways involving a prosthetic group, the non-amino acid portion of certain protein molecules. Prosthetic groups may be inorganic or organic and are usually required for the biological activity of the protein.
The chemical reactions and pathways involving a prosthetic group, the non-amino acid portion of certain protein molecules. Prosthetic groups may be inorganic or organic and are usually required for the biological activity of the protein.
The chemical reactions and pathways involving a prosthetic group, the non-amino acid portion of certain protein molecules. Prosthetic groups may be inorganic or organic and are usually required for the biological activity of the protein.
The chemical reactions and pathways involving coenzymes that are required, in addition to an enzyme and a substrate, for an oxidoreductase reaction to proceed.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
A metabolic process that generates a pool of NADH by the reduction of NAD+.
A metabolic process that generates a pool of NADH by the reduction of NAD+.
A metabolic process that generates a pool of NADH by the reduction of NAD+.
The chemical reactions and pathways resulting in the breakdown of nicotinamide riboside, the product of the formation of a glycosidic bond between ribose and nicotinamide.
The chemical reactions and pathways resulting in the breakdown of nicotinamide riboside, the product of the formation of a glycosidic bond between ribose and nicotinamide.
The chemical reactions and pathways resulting in the breakdown of nicotinamide riboside, the product of the formation of a glycosidic bond between ribose and nicotinamide.
The chemical reactions and pathways resulting in the breakdown of nicotinamide riboside, the product of the formation of a glycosidic bond between ribose and nicotinamide.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; metabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
A metabolic process that generates a pool of NADPH by the reduction of NADP+.
A metabolic process that generates a pool of NADPH by the reduction of NADP+.
A metabolic process that generates a pool of NADPH by the reduction of NADP+.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH.
The chemical reactions and pathways involving ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways involving ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways involving ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways involving the reduced form of flavin adenine dinucleotide.
The chemical reactions and pathways involving the reduced form of flavin adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways resulting in the formation of FAD, the oxidized form of flavin-adenine dinucleotide.
The chemical reactions and pathways involving lipoamide, the functional form of lipoic acid in which the carboxyl group is attached to protein by an amide linkage to a lysine amino group.
The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways resulting in the breakdown of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways resulting in the breakdown of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways resulting in the breakdown of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
The chemical reactions and pathways involving any phosphorylated nucleoside.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
The process of introducing a phosphate group into AMP, adenosine monophosphate, to produce ADP. Addition of two phosphate groups produces ATP.
The process of introducing a phosphate group into ADP, adenosine diphosphate, to produce ATP.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways involving a folic acid-containing compound, i.e. any of a group of heterocyclic compounds based on the pteroic acid skeleton conjugated with one or more L-glutamic acid or L-glutamate units.
The chemical reactions and pathways resulting in the formation of dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways resulting in the formation of dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways resulting in the formation of dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways resulting in the formation of dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways resulting in the formation of dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways resulting in the formation of dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways involving dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways involving dihydrofolate, the dihydroxylated derivative of folate.
The chemical reactions and pathways involving vitamins. Vitamin is a general term for a number of unrelated organic substances that occur in many foods in small amounts and that are necessary in trace amounts for the normal metabolic functioning of the body. Vitamins may be water-soluble or fat-soluble and usually serve as components of coenzyme systems.
The chemical reactions and pathways involving any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways involving biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid; the (+) enantiomer is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions.
The chemical reactions and pathways involving biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid; the (+) enantiomer is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions.
The chemical reactions and pathways involving biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid; the (+) enantiomer is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions.
The chemical reactions and pathways involving biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid; the (+) enantiomer is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions.
The chemical reactions and pathways involving biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid; the (+) enantiomer is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions.
The chemical reactions and pathways involving nicotinamide, pyridine-3-carboxamide, the amide of nicotinic acid. It is a member of the B complex of vitamins and occurs widely in living organisms.
The chemical reactions and pathways involving nicotinamide, pyridine-3-carboxamide, the amide of nicotinic acid. It is a member of the B complex of vitamins and occurs widely in living organisms.
The chemical reactions and pathways involving nicotinamide, pyridine-3-carboxamide, the amide of nicotinic acid. It is a member of the B complex of vitamins and occurs widely in living organisms.
The chemical reactions and pathways involving nicotinamide, pyridine-3-carboxamide, the amide of nicotinic acid. It is a member of the B complex of vitamins and occurs widely in living organisms.
The chemical reactions and pathways involving nicotinamide, pyridine-3-carboxamide, the amide of nicotinic acid. It is a member of the B complex of vitamins and occurs widely in living organisms.
The chemical reactions and pathways involving riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
The chemical reactions and pathways involving riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
The chemical reactions and pathways involving riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
The chemical reactions and pathways involving riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
The chemical reactions and pathways involving riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
The chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
Catalysis of the reaction: 2 cob(I)alamin + H(+) + NAD(+) = 2 cob(II)alamin + NADH.
The chemical reactions and pathways involving of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways involving any of the vitamin A compounds, retinol, retinal (retinaldehyde) and retinoic acid, all of which are derivatives of beta-carotene.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways involving any member of a large group of derivatives or analogs of porphyrin. Porphyrins consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways involving any member of a large group of derivatives or analogs of porphyrin. Porphyrins consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the formation of uroporphyrinogen III.
The chemical reactions and pathways resulting in the formation of uroporphyrinogen III.
The chemical reactions and pathways resulting in the formation of uroporphyrinogen III.
The chemical reactions and pathways resulting in the formation of uroporphyrinogen III.
The chemical reactions that utilize succinyl-CoA in the synthesis of protoporphyrin IX.
The chemical reactions that utilize succinyl-CoA in the synthesis of protoporphyrin IX.
The chemical reactions that utilize succinyl-CoA in the synthesis of protoporphyrin IX.
The chemical reactions that utilize succinyl-CoA in the synthesis of protoporphyrin IX.
The chemical reactions that utilize succinyl-CoA in the synthesis of protoporphyrin IX.
The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
The chemical reactions and pathways resulting in the formation of heme a, a derivative of heme found in cytochrome aa3.
The chemical reactions and pathways resulting in the formation of heme a, a derivative of heme found in cytochrome aa3.
The chemical reactions and pathways resulting in the formation of heme a, a derivative of heme found in cytochrome aa3.
The chemical reactions and pathways resulting in the formation of heme a, a derivative of heme found in cytochrome aa3.
The chemical reactions and pathways resulting in the formation of heme a, a derivative of heme found in cytochrome aa3.
The chemical reactions and pathways resulting in the formation of heme a, a derivative of heme found in cytochrome aa3.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme b, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
The chemical reactions and pathways resulting in the formation of heme c, a derivative of heme found in cytochromes c, b4, and f.
The chemical reactions and pathways resulting in the formation of heme c, a derivative of heme found in cytochromes c, b4, and f.
The chemical reactions and pathways resulting in the formation of heme c, a derivative of heme found in cytochromes c, b4, and f.
The chemical reactions and pathways resulting in the formation of heme c, a derivative of heme found in cytochromes c, b4, and f.
The chemical reactions and pathways resulting in the formation of heme c, a derivative of heme found in cytochromes c, b4, and f.
The chemical reactions and pathways resulting in the formation of heme c, a derivative of heme found in cytochromes c, b4, and f.
The chemical reactions and pathways resulting in the breakdown of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the breakdown of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the breakdown of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the breakdown of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
The chemical reactions and pathways resulting in the loss of electrons from one or more atoms in heme.
The chemical reactions and pathways resulting in the formation of bilirubin monoglucuronide or bilirubin diglucuronide, water-soluble derivatives of bilirubin.
A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary sulfur sources and then activates genes to scavenge the last traces of the primary sulfur source and to transport and metabolize alternate sulfur sources. The utilization process begins when the cell or organism detects sulfur levels, includes the activation of genes whose products detect, transport or metabolize sulfur-containing compounds, and ends when the sulfur is incorporated into the cell or organism's metabolism.
Any process that modulates the frequency, rate or extent of sulfur utilization.
The chemical reactions and pathways involving the nonmetallic element phosphorus or compounds that contain phosphorus, usually in the form of a phosphate group (PO4).
A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary phosphorus source and then activates genes to scavenge the last traces of the primary phosphorus source and to transport and metabolize alternative phosphorus sources. The utilization process begins when the cell or organism detects phosphorus levels, includes the phosphorus-containing substances, and ends when phosphorus is incorporated into the cell or organism's metabolism.
Any process that modulates the frequency, rate or extent of phosphorus utilization.
The chemical reactions and pathways involving the phosphate group, the anion or salt of any phosphoric acid.
The chemical reactions and pathways involving the phosphate group, the anion or salt of any phosphoric acid.
The chemical reactions and pathways involving a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the breakdown of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the breakdown of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the breakdown of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the formation of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the formation of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the formation of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways resulting in the formation of a polyphosphate, the anion or salt of polyphosphoric acid.
The chemical reactions and pathways involving diatomic oxygen (O2).
The chemical reactions and pathways involving diatomic oxygen (O2).
The chemical reactions and pathways involving a reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. They contribute to the microbicidal activity of phagocytes, regulation of signal transduction and gene expression, and the oxidative damage to biopolymers.
The chemical reactions and pathways involving a reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. They contribute to the microbicidal activity of phagocytes, regulation of signal transduction and gene expression, and the oxidative damage to biopolymers.
The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to living organisms. Used of chemical compounds, e.g. a xenobiotic chemical, such as a pesticide.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insecticide stimulus. Insecticides are chemicals used to kill insects.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insecticide stimulus. Insecticides are chemicals used to kill insects.
The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
Any process that modulates the frequency, rate or extent of nitrogen utilization.
The chemical reactions and pathways resulting in the formation of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.
The chemical reactions and pathways resulting in the formation of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.
The chemical reactions and pathways resulting in the formation of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.
The chemical reactions and pathways resulting in the formation of nitric oxide, nitrogen monoxide (NO), a colorless gas only slightly soluble in water.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein.
The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein.
The directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of cations, atoms or small molecules with a net positive charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of cations, atoms or small molecules with a net positive charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of cations, atoms or small molecules with a net positive charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of calcium (Ca) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of calcium (Ca) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of calcium (Ca) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of anions, atoms or small molecules with a net negative charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of chloride into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of metal ions, any metal ion with an electric charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of cobalt (Co) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of copper (Cu) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of iron (Fe) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of iron (Fe) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of manganese (Mn) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of zinc (Zn II) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of zinc (Zn II) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of water (H2O) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of dicarboxylic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of dicarboxylic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of a neurotransmitter into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Neurotransmitters are any chemical substance that is capable of transmitting (or inhibiting the transmission of) a nerve impulse from a neuron to another cell.
The directed movement of serotonin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Serotonin (5-hydroxytryptamine) is a monoamine neurotransmitter occurring in the peripheral and central nervous systems.
The directed movement of allantoate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of allantoin, (2,5-dioxo-4-imidazolidinyl)urea, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of allantoin, (2,5-dioxo-4-imidazolidinyl)urea, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Transport of substances into, out of or within a mitochondrion.
Transport of substances into, out of or within a mitochondrion.
Transport of substances into, out of or within a mitochondrion.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: oxoglutarate(out) + malate(in) = oxoglutarate(in) + malate(out).
The directed movement of alpha-ketoglutarate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of alpha-ketoglutarate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of malate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of tricarboxylic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of citrate, 2-hydroxy-1,2,3-propanetricarboyxlate, into or out of a mitochondrial matrix.
The directed movement of citrate, 2-hydroxy-1,2,3-propanetricarboyxlate, into or out of a mitochondrial matrix.
The directed movement of acyl carnitine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Acyl carnitine is the condensation product of a carboxylic acid and carnitine and is the transport form for a fatty acid crossing the mitochondrial membrane.
The process in which aspartate is transported across a lipid bilayer, from one side of a membrane to the other.
The process in which aspartate is transported across a lipid bilayer, from one side of a membrane to the other.
The directed movement of L-glutamate across a membrane.
The directed movement of L-glutamate across a membrane.
The directed movement of L-glutamate across a membrane.
The directed movement of acetate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of acetate across a plasma membrane.
The directed movement of pyruvate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of pyruvate, 2-oxopropanoate, across a plasma membrane.
The process in which pyruvate is transported across a mitochondrial membrane, into or out of the mitochondrion.
The process in which pyruvate is transported across a mitochondrial membrane, into or out of the mitochondrion.
The process in which pyruvate is transported across a mitochondrial membrane, into or out of the mitochondrion.
The process in which pyruvate is transported across a mitochondrial membrane, into or out of the mitochondrion.
The process in which pyruvate is transported across a mitochondrial membrane, into or out of the mitochondrion.
The process in which pyruvate is transported across a mitochondrial membrane, into or out of the mitochondrion.
The process in which a calcium ion (Ca2+) is transported across a mitochondrial membrane, into or out of the mitochondrion.
The transfer of acyl groups to and from acyl-CoA molecules to form O-acylcarnitine, which can exchange across the mitochondrial inner membrane with unacylated carnitine.
The process in which a drug is transported across a membrane.
The process in which a drug is transported across a membrane.
The directed movement of eye pigment precursors, the inactive forms of visual pigments, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of oligopeptides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
The transport of substances that occurs outside cells.
The directed extracellular movement of carbohydrates.
The directed extracellular movement of amino acids.
The directed movement of a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate, into, out of or within a cell.
The directed movement of purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of purine bases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of a pyrimidine nucleotide, any compound consisting of a pyrimidine nucleoside esterified with (ortho)phosphate, into, out of or within a cell.
The directed movement of amino acids, organic acids containing one or more amino substituents, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of asparagine, alpha-aminosuccinamic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of glutamine, 2-amino-4-carbamoylbutanoic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of glutamine, 2-amino-4-carbamoylbutanoic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
Any process involved in the maintenance of an internal steady state of ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of calcium ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of metal ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of cadmium ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of cobalt ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of copper ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining iron ions in an extracellular area such that they are separated from other components of a biological system.
Any process involved in the maintenance of an internal steady state of zinc ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of sodium ions at the level of a cell.
Any process involved in maintaining the steady state of a cell's volume. The cell's volume refers to the three-dimensional space occupied by a cell.
Any process involved in the maintenance of an internal equilibrium of hydrogen ions, thereby modulating the internal pH, within an organism or cell.
The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
The directed movement of substances within the Golgi, mediated by small transport vesicles. These either fuse with the cis-Golgi or with each other to form the membrane stacks known as the cis-Golgi reticulum (network).
The directed movement of substances from the Golgi to other parts of the cell, including organelles and the plasma membrane, mediated by small transport vesicles.
The directed movement of substances from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane, where they fuse and release their contents by exocytosis.
The directed movement of proteins from the Golgi to a secretory granule. The secretory granule is a membrane-bounded particle, usually protein, formed in the granular endoplasmic reticulum and the Golgi complex.
The directed movement of proteins from the Golgi to a transport vesicle. Continuously secreted proteins are sorted into transport vesicles that fuse with the plasma membrane, releasing their contents by exocytosis.
The directed movement of substances from the Golgi to early sorting endosomes. Clathrin vesicles transport substances from the trans-Golgi to endosomes.
The directed movement of substances from the Golgi to early sorting endosomes. Clathrin vesicles transport substances from the trans-Golgi to endosomes.
The directed movement of substances from the Golgi to early sorting endosomes. Clathrin vesicles transport substances from the trans-Golgi to endosomes.
The directed movement of substances from the Golgi to early sorting endosomes. Clathrin vesicles transport substances from the trans-Golgi to endosomes.
The directed movement of substances from the Golgi to the vacuole.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
The evagination of a membrane, resulting in formation of a vesicle.
A protein coat is added to the vesicle to form the proper shape of the vesicle and to target the vesicle for transport to its destination.
The initial attachment of a vesicle membrane to a target membrane, mediated by proteins protruding from the membrane of the vesicle and the target membrane, that contributes to exocytosis.
An endocytosis process that results in the uptake of liquid material by cells from their external environment; literally 'cell drinking'. Liquid is enclosed in vesicles, called pinosomes, formed by invagination of the plasma membrane.
An endocytosis process that results in the uptake of liquid material by cells from their external environment; literally 'cell drinking'. Liquid is enclosed in vesicles, called pinosomes, formed by invagination of the plasma membrane.
An endocytosis process that results in the uptake of liquid material by cells from their external environment; literally 'cell drinking'. Liquid is enclosed in vesicles, called pinosomes, formed by invagination of the plasma membrane.
An endocytosis process that results in the uptake of liquid material by cells from their external environment; literally 'cell drinking'. Liquid is enclosed in vesicles, called pinosomes, formed by invagination of the plasma membrane.
An endocytosis process that results in the uptake of liquid material by cells from their external environment; literally 'cell drinking'. Liquid is enclosed in vesicles, called pinosomes, formed by invagination of the plasma membrane.
An endocytosis process that results in the engulfment of external particulate material by phagocytes. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles.
The initial step in phagocytosis involving adhesion to bacteria, immune complexes and other particulate matter, or an apoptotic cell and based on recognition of factors such as bacterial cell wall components, opsonins like complement and antibody or protein receptors and lipids like phosphatidyl serine, and leading to intracellular signaling in the phagocytosing cell.
The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis.
The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis.
The directed movement of molecules between the nucleus and the cytoplasm.
The directed movement of molecules between the nucleus and the cytoplasm.
The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
The breakdown of structures such as organelles, proteins, or other macromolecular structures during apoptosis.
The breakdown of structures such as organelles, proteins, or other macromolecular structures during apoptosis.
The breakdown of structures such as organelles, proteins, or other macromolecular structures during apoptosis.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the execution phase of apoptosis.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the execution phase of apoptosis.
A T cell apoptotic process that occurs towards the end of the expansion phase following the initial activation of mature T cells by antigen and is triggered by T cell receptor stimulation and signals transmitted via various surface-expressed members of the TNF receptor family such as Fas ligand, Fas, and TNF and the p55 and p75 TNF receptors.
A T cell apoptotic process that occurs towards the end of the expansion phase following the initial activation of mature T cells by antigen and is triggered by T cell receptor stimulation and signals transmitted via various surface-expressed members of the TNF receptor family such as Fas ligand, Fas, and TNF and the p55 and p75 TNF receptors.
A T cell apoptotic process that occurs towards the end of the expansion phase following the initial activation of mature T cells by antigen and is triggered by T cell receptor stimulation and signals transmitted via various surface-expressed members of the TNF receptor family such as Fas ligand, Fas, and TNF and the p55 and p75 TNF receptors.
A T cell apoptotic process that occurs towards the end of the expansion phase following the initial activation of mature T cells by antigen and is triggered by T cell receptor stimulation and signals transmitted via various surface-expressed members of the TNF receptor family such as Fas ligand, Fas, and TNF and the p55 and p75 TNF receptors.
A T cell apoptotic process that occurs towards the end of the expansion phase following the initial activation of mature T cells by antigen and is triggered by T cell receptor stimulation and signals transmitted via various surface-expressed members of the TNF receptor family such as Fas ligand, Fas, and TNF and the p55 and p75 TNF receptors.
A T cell apoptotic process that occurs towards the end of the expansion phase following the initial activation of mature T cells by antigen and is triggered by T cell receptor stimulation and signals transmitted via various surface-expressed members of the TNF receptor family such as Fas ligand, Fas, and TNF and the p55 and p75 TNF receptors.
Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage.
Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage.
Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage.
Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage.
Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage.
Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage.
The directed, self-propelled movement of a cell or subcellular component without the involvement of an external agent such as a transporter or a pore.
The directed, self-propelled movement of a cell or subcellular component without the involvement of an external agent such as a transporter or a pore.
The directed, self-propelled movement of a cell or subcellular component without the involvement of an external agent such as a transporter or a pore.
The orderly movement of a cell from one site to another along a substrate such as the extracellular matrix; the migrating cell forms a protrusion that attaches to the substrate.
The formation of a cell surface protrusion, such as a lamellipodium or filopodium, at the leading edge of a migrating cell.
The formation of adhesions that stabilize protrusions at the leading edge of a migrating cell; involves integrin activation, clustering, and the recruitment of structural and signaling components to nascent adhesions.
The translocation of the cell body forward during cell migration, mediated by tractional force on its substrate and tension in the cortical cytoskeleton. Adhesions transmit propulsive forces and serve as traction points over which the cell moves.
The disassembly of adhesions at the front and rear of a migrating cell. At the leading edge, adhesion disassembly accompanies the formation of new protrusions; at the cell rear, it promotes tail retraction.
The directed movement of accumulated adhesion components such as integrins from the rear of a migrating cell toward the cell front, where they are available to form new protrusions and adhesions.
The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
Any process that modulates the frequency, rate or extent of muscle contraction.
A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length.
Any process that modulates the frequency, rate or extent of smooth muscle contraction.
A process in which force is generated within striated muscle tissue, resulting in the shortening of the muscle. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Striated muscle is a type of muscle in which the repeating units (sarcomeres) of the contractile myofibrils are arranged in registry throughout the cell, resulting in transverse or oblique striations observable at the level of the light microscope.
Any process that modulates the frequency, rate or extent of striated muscle contraction.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a mechanical stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a mechanical stimulus.
The series of events required for an organism to receive a sensory mechanical stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events required for an organism to receive a sensory mechanical stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events required for an organism to receive a sensory mechanical stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.
The process of syncytia-forming cell-cell fusion, caused by a virus.
The process of syncytia-forming cell-cell fusion, caused by a virus.
The process of syncytia-forming cell-cell fusion, caused by a virus.
The process of syncytia-forming cell-cell fusion, caused by a virus.
The formation of a syncytium, a mass of cytoplasm containing several nuclei enclosed within a single plasma membrane. Syncytia are normally derived from single cells that fuse or fail to complete cell division.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat.
Any process involved in the activation of any of the steps of the alternative pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes.
Any process involved in the activation of any of the steps of the classical pathway of the complement cascade which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes.
An immune response mediated through a body fluid.
An immune response against bacteria, specific to males and mediated through a body fluid.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-negative bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of biosynthesis of antibacterial peptides active against Gram-positive bacteria.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
Any process that activates or increases the frequency, rate, or extent of antifungal peptide biosynthesis.
A defense response that is mediated by cells.
A defense response that is mediated by cells.
A defense response that is mediated by cells.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hypotonic environment, i.e. an environment with a lower concentration of solutes than the organism or cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
The accumulation of glycerol within a cell, for example by increased glycerol biosynthesis combined with decreased permeability of the cell membrane to glycerol, in response to the detection of a hyperosmotic environment.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
The widespread phosphorylation of various molecules, triggering many downstream processes, that occurs in response to the detection of DNA damage.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage and resulting in the stopping or reduction in rate of the cell cycle.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, resulting in the induction of the transcription of p21 (also known as WAF1, CIP1 and SDI1) or any equivalent protein, in response to the detection of DNA damage.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipid hydroperoxide stimulus. Lipid hydroperoxide is the highly reactive primary oxygenated products of polyunsaturated fatty acids.
The series of molecular signals generated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB.
The series of molecular signals generated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB.
The series of molecular signals generated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB.
Any series of molecular signals that conveys information from the endoplasmic reticulum to the nucleus, usually resulting in a change in transcriptional regulation.
Any series of molecular signals that conveys information from the endoplasmic reticulum to the nucleus, usually resulting in a change in transcriptional regulation.
Any series of molecular signals that conveys information from the endoplasmic reticulum to the nucleus, usually resulting in a change in transcriptional regulation.
Any series of molecular signals that conveys information from the endoplasmic reticulum to the nucleus, usually resulting in a change in transcriptional regulation.
Any series of molecular signals that conveys information from the endoplasmic reticulum to the nucleus, usually resulting in a change in transcriptional regulation.
Any series of molecular signals that conveys information from the endoplasmic reticulum to the nucleus, usually resulting in a change in transcriptional regulation.
The conversion of inactive NF-kappaB to the active form, thereby allowing it to activate transcription of target genes, as a result of signaling from the endoplasmic reticulum.
The conversion of inactive NF-kappaB to the active form, thereby allowing it to activate transcription of target genes, as a result of signaling from the endoplasmic reticulum.
The conversion of inactive NF-kappaB to the active form, thereby allowing it to activate transcription of target genes, as a result of signaling from the endoplasmic reticulum.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
Catalysis of the formation of a phosphodiester bond between a hydroxyl group at the end of one RNA chain and the 5'-phosphate group at the end of another.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
The activation of genes whose promoters contain a specific sequence elements such as the unfolded protein response element (UPRE; consensus CAGCGTG) or the ER stress-response element (ERSE; CCAAN(N)9CCACG), as a result of signaling via the unfolded protein response.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating deprivation of sterols. Sterols are a group of steroids characterized by the presence of one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nitrogen.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an organelle within a cell. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an organelle within a cell. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an organelle within a cell. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an organelle within a cell. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an organelle within a cell. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear envelope.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear envelope.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear pore.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear pore.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear pore.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleolus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleolus.
Interacting selectively and non-covalently with a centromere, a region of chromosome where the spindle fibers attach during mitosis and meiosis.
Interacting selectively and non-covalently with a telomere, a specific structure at the end of a linear chromosome required for the integrity and maintenance of the end.
Interacting selectively and non-covalently with a telomere, a specific structure at the end of a linear chromosome required for the integrity and maintenance of the end.
The maintenance of proper telomeric length by the addition of telomeric repeats by telomerase.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrial membrane, either of the lipid bilayer surrounding a mitochondrion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrial membrane, either of the lipid bilayer surrounding a mitochondrion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial inner membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial inner membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial inner membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial outer membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial outer membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the plasma membrane.
The modification of actin by addition of ubiquitin groups.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
A cytoskeleton organization process that directly or indirectly links cytoskeletal filaments to the plasma membrane.
A microtubule-based process that results in the movement of organelles, other microtubules, or other cellular components.  Examples include motor-driven movement along microtubules and movement driven by polymerization or depolymerization of microtubules.
The removal of tubulin heterodimers from one or both ends of a microtubule.
The removal of tubulin heterodimers from one or both ends of a microtubule.
The removal of tubulin heterodimers from one or both ends of a microtubule.
The removal of tubulin heterodimers from one or both ends of a microtubule.
The process in which tubulin alpha-beta heterodimers begin aggregation to form an oligomeric tubulin structure (a microtubule seed). Microtubule nucleation is the initiating step in the formation of a microtubule in the absence of any existing microtubules ('de novo' microtubule formation).
The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer.
The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer.
The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer.
Completion of folding of alpha- and beta-tubulin; takes place subsequent to chaperonin-mediated partial folding; mediated by a complex of folding cofactors.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
Any process that stops, prevents, or reduces the frequency, rate or extent of the depolymerization of the specialized microtubules of the axoneme.
Any process that stops, prevents, or reduces the frequency, rate or extent of the depolymerization of the specialized microtubules of the axoneme.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cytoplasm. The cytoplasm is all of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cytoplasm. The cytoplasm is all of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the Golgi apparatus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the Golgi apparatus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes.
The directed movement of substances into, out of or within a vacuole.
Any process that reduces the pH of the vacuole, measured by the concentration of the hydrogen ion.
Any process involved in the maintenance of an internal steady state of calcium ions in the vacuole or between a vacuole and its surroundings.
The directed movement of proteins imported into a cell by endocytosis to the vacuole.
The chemical reactions and pathways resulting in the breakdown of a protein in the vacuole, usually by the action of vacuolar proteases.
The chemical reactions and pathways resulting in the breakdown of a protein in the vacuole, usually by the action of vacuolar proteases.
The chemical reactions and pathways resulting in the breakdown of a protein in the vacuole, usually by the action of vacuolar proteases.
The chemical reactions and pathways resulting in the breakdown of a protein in the vacuole, usually by the action of vacuolar proteases.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosome. A lysosome is a cytoplasmic, membrane-bounded organelle that is found in most animal cells and that contains a variety of hydrolases.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosome. A lysosome is a cytoplasmic, membrane-bounded organelle that is found in most animal cells and that contains a variety of hydrolases.
The directed movement of substances into, out of or within a lysosome.
Any process that reduces the pH of the lysosomal lumen, measured by the concentration of the hydrogen ion.
The aggregation, arrangement and bonding together of a set of components to form a junction between cells.
The aggregation, arrangement and bonding together of a set of components to form a junction between a cell and its substrate.
The aggregation, arrangement, and bonding together of a set of components to form a cell-substrate adherens junction.
The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M).
A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M).
A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle, the array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during DNA segregation and serves to move the duplicated chromosomes apart.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle, the array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during DNA segregation and serves to move the duplicated chromosomes apart.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle, the array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during DNA segregation and serves to move the duplicated chromosomes apart.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle, the array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during DNA segregation and serves to move the duplicated chromosomes apart.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
The aggregation, arrangement and bonding together of a set of components to form the spindle during a meiotic cell cycle in males. An example of this is found in Drosophila melanogaster.
The formation of the spindle during meiosis I of a meiotic cell cycle in males. An example of this is found in Drosophila melanogaster.
The formation of the spindle during meiosis II of a meiotic cell cycle in males. An example of this is found in Drosophila melanogaster.
The aggregation, arrangement and bonding together of a set of components to form the spindle during a meiotic cell cycle in females. An example of this is found in Drosophila melanogaster.
The aggregation, arrangement and bonding together of a set of components to form the spindle during meiosis I of a meiotic cell cycle in females. An example of this is found in Drosophila melanogaster.
The aggregation, arrangement and bonding together of a set of components to form the spindle during meiosis II of a meiotic cell cycle in females. An example of this is found in Drosophila melanogaster.
The cell cycle process in which genetic material, in the form of chromosomes, is organized and then physically separated and apportioned to two or more sets during the meiotic cell cycle in a male.
The cell cycle process in which the sister chromatids of a replicated chromosome become tethered to each other.
The cell cycle process in which the sister chromatids of a replicated chromosome become tethered to each other.
Any process that modulates the frequency, rate or extent of sister chromatid cohesion.
The cell cycle process in which the sister chromatids of a replicated chromosome are joined along the entire length of the chromosome, from their formation in S phase through metaphase during a mitotic cell cycle. This cohesion cycle is critical for high fidelity chromosome transmission.
The joining of the sister chromatids of a replicated chromosome along the entire length of the chromosome that occurs during meiosis in a male.
The joining of the sister chromatids of a replicated chromosome along the entire length of the chromosome that occurs during meiosis in a female.
Any process that increases the frequency, rate or extent of transcription as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase I promoter as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase I promoter as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase III promoter as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase III promoter as the cell leaves M phase. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
The cell cycle process in which chromatin structure is compacted prior to and during mitosis in eukaryotic cells.
The cell cycle process in which the controlled breakdown of the nuclear envelope during mitotic cell division occurs.
The cell cycle process in which the controlled breakdown of the nuclear envelope during mitotic cell division occurs.
The cell cycle process in which the controlled breakdown of the nuclear envelope during mitotic cell division occurs.
The cell cycle process in which lamin is depolymerized.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis.
The cell cycle process in which chromosomes are aligned at the metaphase plate, a plane halfway between the poles of the mitotic spindle, during mitosis.
The cell cycle process in which chromosome structure is altered from the condensed form taken on during mitosis to the relaxed disperse form held in resting cells.
The cell cycle process that results in reformation of the nuclear envelope during mitotic cell division.
The cell cycle process in which nuclear pore complexes reform during mitotic cell division.
Any process that modulates the frequency, rate or extent of mitosis.
A cell cycle process by which a cell commits to entering S phase via a positive feedback mechanism between the regulation of transcription and G1 CDK activity.
The cell cycle process by which a cell commits to entering the next mitotic cell cycle phase.
The cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin.
The cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin.
A cell cycle checkpoint that ensures accurate chromosome replication and segregation by preventing progression through a mitotic cell cycle until conditions are suitable for the cell to proceed to the next stage.
A cell cycle checkpoint that ensures accurate chromosome replication and segregation by preventing progression through a mitotic cell cycle until conditions are suitable for the cell to proceed to the next stage.
A cell cycle checkpoint that ensures accurate chromosome replication and segregation by preventing progression through a mitotic cell cycle until conditions are suitable for the cell to proceed to the next stage.
A cell cycle checkpoint that delays the metaphase/anaphase transition of a mitotic nuclear division until the spindle is correctly assembled and chromosomes are attached to the spindle.
A cell cycle checkpoint that delays the metaphase/anaphase transition of a mitotic nuclear division until the spindle is correctly assembled and chromosomes are attached to the spindle.
A mitotic cell cycle checkpoint that detects and negatively regulates progression through the G2/M transition of the cell cycle in response to DNA damage.
Any process involved in the progression from anaphase/telophase to G1 that is associated with a conversion from high to low mitotic CDK activity.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The directed movement of the nucleus to a specific location within a cell.
The cell cycle process in which centrosome duplication and separation takes place. The centrosome cycle can operate with a considerable degree of independence from other processes of the cell cycle.
The cell cycle process in which centrosome duplication and separation takes place. The centrosome cycle can operate with a considerable degree of independence from other processes of the cell cycle.
The cell cycle process in which centrosome duplication and separation takes place. The centrosome cycle can operate with a considerable degree of independence from other processes of the cell cycle.
The cell cycle process in which centrosome duplication and separation takes place. The centrosome cycle can operate with a considerable degree of independence from other processes of the cell cycle.
The cell cycle process in which a daughter centriole is formed perpendicular to an existing centriole. An immature centriole contains a ninefold radially symmetric array of single microtubules; mature centrioles consist of a radial array of nine microtubule triplets, doublets, or singlets depending upon the species and cell type. Duplicated centrioles also become the ciliary basal body in cells that form cilia during G0.
The cell cycle process in which a daughter centriole is formed perpendicular to an existing centriole. An immature centriole contains a ninefold radially symmetric array of single microtubules; mature centrioles consist of a radial array of nine microtubule triplets, doublets, or singlets depending upon the species and cell type. Duplicated centrioles also become the ciliary basal body in cells that form cilia during G0.
The cell cycle process in which a daughter centriole is formed perpendicular to an existing centriole. An immature centriole contains a ninefold radially symmetric array of single microtubules; mature centrioles consist of a radial array of nine microtubule triplets, doublets, or singlets depending upon the species and cell type. Duplicated centrioles also become the ciliary basal body in cells that form cilia during G0.
The cell cycle process in which a daughter centriole is formed perpendicular to an existing centriole. An immature centriole contains a ninefold radially symmetric array of single microtubules; mature centrioles consist of a radial array of nine microtubule triplets, doublets, or singlets depending upon the species and cell type. Duplicated centrioles also become the ciliary basal body in cells that form cilia during G0.
Separation of duplicated centrosome components at the beginning of mitosis. The centriole pair within each centrosome becomes part of a separate microtubule organizing center that nucleates a radial array of microtubules called an aster. The two asters move to opposite sides of the nucleus to form the two poles of the mitotic spindle.
The process of marking the place where cytokinesis will occur.
The process of marking the place where cytokinesis will occur.
The process of marking the place where cytokinesis will occur.
Any process involved in the net addition of membrane at the site of cytokinesis; includes vesicle recruitment and fusion, local lipid synthesis and insertion.
A cell cycle process that results in the division of the cytoplasm of a cell after meiosis I, resulting in the separation of the original cell into two daughter cells.
A cell cycle process that results in the division of the cytoplasm of a cell after meiosis II, resulting in the separation of the original cell into two daughter cells.
A cell cycle process that occurs as part of the male meiotic cell cycle and results in the division of the cytoplasm of a cell to produce two daughter cells.
A cell cycle process that occurs as part of the male meiotic cell cycle and results in the division of the cytoplasm of a cell to produce two daughter cells.
A mitotic cell cycle in which chromosomes are replicated and sister chromatids separate, but spindle formation, nuclear membrane breakdown and nuclear division do not occur, resulting in an increased number of chromosomes in the cell.
A form of asexual reproduction, occurring in certain bacteria and fungi (e.g. yeasts) and some primitive animals in which an individual arises from a daughter cell formed by pinching off a part of the parent cell. The budlike outgrowths so formed may sometimes remain attached to the parent cell.
The specification and formation of anisotropic intracellular organization or cell growth patterns.
The specification and formation of anisotropic intracellular organization or cell growth patterns.
The specification and formation of anisotropic intracellular organization or cell growth patterns.
The specification and formation of anisotropic intracellular organization or cell growth patterns.
Any process that modulates the frequency, rate or extent of the formation and growth of cell buds.
The process in which the bud portion of a cell that reproduces by budding irreversibly increases in size over time by accretion and biosynthetic production of matter similar to that already present.
Growth at the tip of a bud, in a cell that reproduces by budding.
Unlocalized bud growth such that the entire surface of the bud expands evenly, in a cell that reproduces by budding.
The process of defining the next site of bud emergence adjacent to the last site of bud emergence on a budding cell.
The process of defining the next site of bud emergence adjacent to the last site of bud emergence on a budding cell.
The process of defining subsequent sites of bud emergence such that budding takes place at alternating poles of a budding cell.
The process of defining subsequent sites of bud emergence such that budding takes place at alternating poles of a budding cell.
The process of defining subsequent sites of bud emergence such that budding takes place at alternating poles of a budding cell.
A pattern of cell growth that occurs in conditions of nitrogen limitation and abundant fermentable carbon source. Cells become elongated, switch to a unipolar budding pattern, remain physically attached to each other, and invade the growth substrate.
The first meiotic nuclear division in which homologous chromosomes are paired and segregated from each other, producing two haploid daughter nuclei.
The cell cycle phase which is the first stage of meiosis I and during which chromosomes condense and the two daughter centrioles and their asters migrate toward the poles of the cell.
The meiotic cell cycle process where side by side pairing and physical juxtaposition of homologous chromosomes is created during meiotic prophase. Synapsis begins when the chromosome arms begin to pair from the clustered telomeres and ends when synaptonemal complex or linear element assembly is complete.
The meiotic cell cycle process where side by side pairing and physical juxtaposition of homologous chromosomes is created during meiotic prophase. Synapsis begins when the chromosome arms begin to pair from the clustered telomeres and ends when synaptonemal complex or linear element assembly is complete.
The meiotic cell cycle process where side by side pairing and physical juxtaposition of homologous chromosomes is created during meiotic prophase. Synapsis begins when the chromosome arms begin to pair from the clustered telomeres and ends when synaptonemal complex or linear element assembly is complete.
The cell cycle process in which the synaptonemal complex is formed. This is a structure that holds paired chromosomes together during prophase I of meiosis and that promotes genetic recombination.
The cell cycle process in which double strand breaks are formed and repaired through a double Holliday junction intermediate. This results in the equal exchange of genetic material between non-sister chromatids in a pair of homologous chromosomes. These reciprocal recombinant products ensure the proper segregation of homologous chromosomes during meiosis I and create genetic diversity.
The cell cycle process in which double strand breaks are formed and repaired through a double Holliday junction intermediate. This results in the equal exchange of genetic material between non-sister chromatids in a pair of homologous chromosomes. These reciprocal recombinant products ensure the proper segregation of homologous chromosomes during meiosis I and create genetic diversity.
The cell cycle process in which double strand breaks are formed and repaired through a double Holliday junction intermediate. This results in the equal exchange of genetic material between non-sister chromatids in a pair of homologous chromosomes. These reciprocal recombinant products ensure the proper segregation of homologous chromosomes during meiosis I and create genetic diversity.
The cell cycle process in which double strand breaks are formed and repaired through a double Holliday junction intermediate. This results in the equal exchange of genetic material between non-sister chromatids in a pair of homologous chromosomes. These reciprocal recombinant products ensure the proper segregation of homologous chromosomes during meiosis I and create genetic diversity.
The cell cycle phase, following prophase I, during which chromosomes become aligned on the equatorial plate of the cell as part of meiosis I.
The cell cycle phase during which chromosomes separate and migrate towards the poles of the spindle the as part of meiosis I.
The cell cycle phase which follows anaphase I of meiosis and during which the chromosomes arrive at the poles of the cell and the division of the cytoplasm starts.
The second nuclear division of meiosis, in which the two chromatids in each chromosome are separated, resulting in four daughter nuclei from the two nuclei produced in meiosis II.
The cell cycle phase which is the first stage of meiosis II and during which chromosomes condense and the two daughter centrioles and their asters migrate toward the poles of the cell.
The cell cycle phase, following prophase II, during which chromosomes become aligned on the equatorial plate of the cell as part of meiosis II.
The cell cycle phase during which chromosomes separate and migrate towards the poles of the spindle the as part of meiosis II.
The cell cycle phase which follows anaphase II of meiosis and during which the chromosomes arrive at the poles of the cell and the division of the cytoplasm starts.
A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the male germline.
A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the male germline.
A cell cycle process comprising the steps by which a cell progresses through male meiosis I, the first meiotic division in the male germline.
A cell cycle process comprising the steps by which a cell progresses through male meiosis II, the second meiotic division in the male germline.
A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the female germline.
A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the female germline.
The cell cycle process in which the first meiotic division occurs in the female germline.
During meiosis, the aggregation, arrangement and bonding together of strand exchange proteins (recombinases) to form small, electron dense structures in association with meiotic chromosomes.
The cell cycle process in which the second meiotic division occurs in the female germline.
The increase in size or mass of an entire organism, a part of an organism or a cell.
The increase in size or mass of an entire organism, a part of an organism or a cell.
The increase in size or mass of an entire organism, a part of an organism or a cell.
Any process that mediates interactions between a cell and its surroundings. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The attachment of a plasma membrane adhesion molecule in one cell to an identical molecule in an adjacent cell.
The attachment of a neuron to another cell via adhesion molecules.
The attachment of a neuron to another cell via adhesion molecules.
The attachment of a leukocyte to another cell via adhesion molecules.
The attachment of a leukocyte to another cell via adhesion molecules.
The binding of a cell to the extracellular matrix via adhesion molecules.
The binding of a cell to the extracellular matrix via adhesion molecules that do not require the presence of calcium for the interaction.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion.
Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
Coordinated organization of groups of cells in a tissue, such that they all orient to similar coordinates.
A series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a receptor on the surface of the target cell, where the receptor possesses catalytic activity or is closely associated with an enzyme such as a protein kinase, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to a receptor on the surface of the target cell where the receptor possesses guanylyl cyclase activity, and ending with regulation of a downstream cellular process, e.g. transcription.
Interacting selectively and non-covalently with a receptor that possesses protein tyrosine kinase activity.
Any process that initiates the activity of the inactive transmembrane receptor protein tyrosine kinase activity.
Any process that initiates the activity of the inactive transmembrane receptor protein tyrosine kinase activity.
The aggregation, arrangement and bonding together of a set of components to form a complex capable of relaying a signal within a cell.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
The chemical reactions and pathways resulting in the breakdown of epidermal growth factor (EGF), following internalization of the receptor-bound ligand into the signal-receiving cell. Full breakdown of epidermal growth factor results in a ligand that is unable to bind and activate its receptor.
Any process that modulates the frequency, rate or extent of EGF-activated receptor activity.
Any process that modulates the frequency, rate or extent of EGF-activated receptor activity.
Any process that modulates the frequency, rate or extent of EGF-activated receptor activity.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Interacting selectively and non-covalently with TGF-beta, transforming growth factor beta, a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types.
Interacting selectively and non-covalently with TGF-beta, transforming growth factor beta, a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types.
Interacting selectively and non-covalently with TGF-beta, transforming growth factor beta, a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types.
Interacting selectively and non-covalently with TGF-beta, transforming growth factor beta, a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types.
The aggregation, arrangement and bonding together of a ligand-bound type II transforming growth factor beta (TGF-beta) receptor dimer with a type I TGF-beta receptor dimer, following ligand binding, to form a heterotetrameric TGF-beta receptor complex.
The aggregation, arrangement and bonding together of a ligand-bound type II transforming growth factor beta (TGF-beta) receptor dimer with a type I TGF-beta receptor dimer, following ligand binding, to form a heterotetrameric TGF-beta receptor complex.
The aggregation, arrangement and bonding together of a ligand-bound type II transforming growth factor beta (TGF-beta) receptor dimer with a type I TGF-beta receptor dimer, following ligand binding, to form a heterotetrameric TGF-beta receptor complex.
The process of introducing a phosphate group on to a common-partner SMAD protein. A common partner SMAD protein binds to pathway-restricted SMAD proteins forming a complex that translocates to the nucleus.
The process of introducing a phosphate group on to a common-partner SMAD protein. A common partner SMAD protein binds to pathway-restricted SMAD proteins forming a complex that translocates to the nucleus.
The process of introducing a phosphate group on to a common-partner SMAD protein. A common partner SMAD protein binds to pathway-restricted SMAD proteins forming a complex that translocates to the nucleus.
The process of introducing a phosphate group on to a common-partner SMAD protein. A common partner SMAD protein binds to pathway-restricted SMAD proteins forming a complex that translocates to the nucleus.
The aggregation, arrangement and bonding together of a set of components to form a protein complex that contains SMAD proteins.
A series of molecular signals initiated by the binding of an extracellular ligand to a receptor on the surface of the target cell where the receptor possesses protein tyrosine phosphatase activity, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.  The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation or inhibition of a nucleotide cyclase activity and a subsequent change in the concentration of a cyclic nucleotide.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation or inhibition of a nucleotide cyclase activity and a subsequent change in the concentration of a cyclic nucleotide.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation or inhibition of a nucleotide cyclase activity and a subsequent change in the concentration of a cyclic nucleotide.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation or inhibition of a nucleotide cyclase activity and a subsequent change in the concentration of a cyclic nucleotide.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation or inhibition of a nucleotide cyclase activity and a subsequent change in the concentration of a cyclic nucleotide.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation or inhibition of a nucleotide cyclase activity and a subsequent change in the concentration of a cyclic nucleotide.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of adenylyl cyclase activity and a subsequent change in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation of adenylyl cyclase activity and a subsequent increase in the concentration of cyclic AMP (cAMP).
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through inhibition of adenylyl cyclase activity and a subsequent decrease in the concentration of cyclic AMP (cAMP).
Any process that stops, prevents, or reduces the frequency, rate or extent of adenylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of adenylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of adenylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of adenylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of adenylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of adenylate cyclase activity.
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a dopamine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, followed by activation of guanylyl cyclase (GC) activity and a subsequent increase in the concentration of cyclic GMP (cGMP).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The initiation of the activity of the inactive enzyme phospolipase C as the result of a series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand.
Any process that increases the concentration of calcium ions in the cytosol.
Any process that increases the concentration of calcium ions in the cytosol.
Any process that increases the concentration of calcium ions in the cytosol.
Any process that increases the concentration of calcium ions in the cytosol.
Any process that increases the concentration of calcium ions in the cytosol.
Any process that increases the concentration of calcium ions in the cytosol.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of protein kinase C (PKC). PKC is activated by second messengers including diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of protein kinase C (PKC). PKC is activated by second messengers including diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of protein kinase C (PKC). PKC is activated by second messengers including diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled glutamate receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a G protein-coupled acetylcholine receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a serotonin receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a tachykinin receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a tachykinin receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a tachykinin receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a serotonin receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of octopamine or tyramine binding to a cell surface receptor. Octopamine and tyramine are decarboxylation products of tyrosine, and are the invertebrate counterparts of the vertebrate adrenergic transmitters.
The series of molecular signals generated as a consequence of octopamine or tyramine binding to a cell surface receptor. Octopamine and tyramine are decarboxylation products of tyrosine, and are the invertebrate counterparts of the vertebrate adrenergic transmitters.
The series of molecular signals generated as a consequence of a dopamine receptor binding to one of its physiological ligands.
Any series of molecular signals initiated by an acetylcholine receptor on the surface of the target cell binding to one of its physiological ligands, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction and ends with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by an acetylcholine receptor on the surface of the target cell binding to one of its physiological ligands, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction and ends with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by an acetylcholine receptor on the surface of the target cell binding to one of its physiological ligands, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
The series of molecular signals generated by the binding of gamma-aminobutyric acid (GABA, 4-aminobutyrate), an amino acid which acts as a neurotransmitter in some organisms, to a cell surface receptor.
A series of molecular signals initiated by the binding of glutamate to a glutamate receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of glutamate to a glutamate receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by glutamate binding to a glutamate receptor on the surface of the target cell, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. Ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by glutamate binding to a glutamate receptor on the surface of the target cell, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. Ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by glutamate binding to a glutamate receptor on the surface of the target cell, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. Ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of a tachykinin, i.e. a short peptide with the terminal sequence (Phe-X-Gly-Leu-Met-NH2), binding to a cell surface receptor.
The series of molecular signals generated as a consequence of a peptide neurotransmitter binding to a cell surface receptor.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The series of successive proteolytic cleavages of the Notch protein, which result in an active form of the receptor.
The activation of transcription of specific genes as a result of Notch signaling, mediated by the Notch intracellular domain.
The activation of transcription of specific genes as a result of Notch signaling, mediated by the Notch intracellular domain.
A series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.
A series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.
A series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.
A series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.
A series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.
A series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.
The posttranslational modification of members of the Hedgehog family of signaling proteins in order for Hedgehog to exert its biological activity. These modifications include cleavage of its signal sequence, autocatalytic protein cleavage and the attachment of sterol groups.
The posttranslational modification of members of the Hedgehog family of signaling proteins in order for Hedgehog to exert its biological activity. These modifications include cleavage of its signal sequence, autocatalytic protein cleavage and the attachment of sterol groups.
The posttranslational modification of members of the Hedgehog family of signaling proteins in order for Hedgehog to exert its biological activity. These modifications include cleavage of its signal sequence, autocatalytic protein cleavage and the attachment of sterol groups.
The series of molecular signals that are initiated by the transmembrane protein Smoothened. In the presence of a Hedgehog signaling molecule, the Patched protein no longer inhibits the activity of Smoothened, and Smoothened signals via the Hedgehog signaling complex to activate downstream components of the Hedgehog signaling pathway.
Any process that increases the activity of a transcription factor that activates transcription of Hedgehog-target genes in response to Smoothened signaling. In Drosophila, Cubitus interruptus (Ci) is the only identified transcription factor so far in the Hedgehog signaling pathway. In vertebrates, members of the Gli protein family are activated in this way. Activation of the Gli/Ci transcription factor is distinct from its stabilization, when proteolytic cleavage is inhibited.
Any process that increases the activity of a transcription factor that activates transcription of Hedgehog-target genes in response to Smoothened signaling. In Drosophila, Cubitus interruptus (Ci) is the only identified transcription factor so far in the Hedgehog signaling pathway. In vertebrates, members of the Gli protein family are activated in this way. Activation of the Gli/Ci transcription factor is distinct from its stabilization, when proteolytic cleavage is inhibited.
A series of molecular signals initiated by the binding of extracellular ligand to an integrin on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions.
The series of molecular signals initiated in response to osmotic change.
The series of molecular signals initiated in response to osmotic change.
The series of molecular signals initiated in response to osmotic change.
The series of molecular signals initiated in response to osmotic change.
The series of molecular signals initiated in response to osmotic change.
The series of molecular signals initiated in response to osmotic change.
A series of molecular signals generated in response to osmotic change, as mediated through a Sho1 osmosensor system.
A series of molecular signals generated in response to osmotic change, as mediated through a Sho1 osmosensor system.
A series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system.
A series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system.
A series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system.
A series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system.
A series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system.
A series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system.
The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The stimulation of the activity of NF-kappaB-inducing kinase through phosphorylation at specific residues.
The stimulation of the activity of NF-kappaB-inducing kinase through phosphorylation at specific residues.
The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
The initiation of the activity of the inactive enzyme JUN kinase kinase (JNKK) activity. JNKKs are involved in a signaling pathway that is primarily activated by cytokines and exposure to environmental stress.
The initiation of the activity of the inactive enzyme JUN kinase kinase (JNKK) activity. JNKKs are involved in a signaling pathway that is primarily activated by cytokines and exposure to environmental stress.
The initiation of the activity of the inactive enzyme JUN kinase (JNK).
The process of introducing a phosphate group into a JUN protein.
Any process in which STAT proteins (Signal Transducers and Activators of Transcription) and JAK (Janus Activated Kinase) proteins convey a signal to trigger a change in the activity or state of a cell. The JAK-STAT cascade begins with activation of STAT proteins by members of the JAK family of tyrosine kinases, proceeds through dimerization and subsequent nuclear translocation of STAT proteins, and ends with regulation of target gene expression by STAT proteins.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
Any intracellular signal transduction in which the signal is passed on within the cell via nitric oxide (NO). Includes synthesis of nitric oxide, receptors/sensors for nitric oxide (such as soluble guanylyl cyclase/sGC) and downstream effectors that further transmit the signal within the cell. Nitric oxide transmits its downstream effects through either cyclic GMP (cGMP)-dependent or independent mechanisms.
Any intracellular signal transduction in which the signal is passed on within the cell via nitric oxide (NO). Includes synthesis of nitric oxide, receptors/sensors for nitric oxide (such as soluble guanylyl cyclase/sGC) and downstream effectors that further transmit the signal within the cell. Nitric oxide transmits its downstream effects through either cyclic GMP (cGMP)-dependent or independent mechanisms.
Any intracellular signal transduction in which the signal is passed on within the cell via nitric oxide (NO). Includes synthesis of nitric oxide, receptors/sensors for nitric oxide (such as soluble guanylyl cyclase/sGC) and downstream effectors that further transmit the signal within the cell. Nitric oxide transmits its downstream effects through either cyclic GMP (cGMP)-dependent or independent mechanisms.
Any intracellular signal transduction in which the signal is passed on within the cell via nitric oxide (NO). Includes synthesis of nitric oxide, receptors/sensors for nitric oxide (such as soluble guanylyl cyclase/sGC) and downstream effectors that further transmit the signal within the cell. Nitric oxide transmits its downstream effects through either cyclic GMP (cGMP)-dependent or independent mechanisms.
Any series of molecular signals in which a small monomeric GTPase relays one or more of the signals.
A series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state.
A series of molecular signals within the cell that are mediated by a member of the Rho family of proteins switching to a GTP-bound active state.
The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
The process of synaptic transmission from a neuron to another neuron across a synapse.
The vesicular release of acetylcholine from a presynapse, across a chemical synapse, the subsequent activation of dopamine receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
The process in which glial cells envelop neuronal cell bodies and/or axons to form an insulating layer. This can take the form of myelinating or non-myelinating ensheathment.
The process of synaptic transmission from a neuron to a muscle, across a synapse.
The biological process whose specific outcome is the progression of a multicellular organism over time from an initial condition (e.g. a zygote or a young adult) to a later condition (e.g. a multicellular animal or an aged adult).
The generation and maintenance of gametes in a multicellular organism. A gamete is a haploid reproductive cell.
The generation and maintenance of gametes in a multicellular organism. A gamete is a haploid reproductive cell.
The process whose specific outcome is the progression of the pole cell over time, from its formation to the mature structure.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a pole cell regardless of its environment; upon determination, the cell fate cannot be reversed.
Formation of a small group of cells (pole cells) at the posterior pole of the insect blastula. They are the first cells to cellularize after the arrival of nuclei at the end of the syncytial blastula stage and are the precursors to the insect germ cells.
The directed movement of a pole cell (germline progenitors in insects) from its site of production at the posterior pole of the embryo through to the site where the gonads will form.
The process whose specific outcome is the progression of an immature germ cell over time, from its formation to the mature structure (gamete). A germ cell is any reproductive cell in a multicellular organism.
The process whose specific outcome is the progression of an immature germ cell over time, from its formation to the mature structure (gamete). A germ cell is any reproductive cell in a multicellular organism.
Any of the rounds of incomplete mitosis undergone by a cystoblast to form a cyst of interconnected cells.
The process of formation of spermatozoa, including spermatocytogenesis and spermiogenesis.
The mitotic divisions of the primary spermatogonial cell (a primordial male germ cell) to form secondary spermatogonia (primary spermatocytes).
The phase of growth and gene expression that male germ cells undergo as they enter the spermatocyte stage. The cells grow in volume and transcribe most of the gene products needed for the morphological events that follow meiosis.
The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure.
The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure.
Fusion of mitochondria during insect spermatid differentiation to form two masses, which wrap around each other to form a densely packed sphere called the Nebenkern.
Fusion of mitochondria during insect spermatid differentiation to form two masses, which wrap around each other to form a densely packed sphere called the Nebenkern.
The assembly and organization of the sperm flagellar axoneme, the bundle of microtubules and associated proteins that forms the core of the eukaryotic sperm flagellum, and is responsible for movement.
The specialization of the spermatid nucleus during the development of a spermatid into a mature male gamete competent for fertilization.
The change in shape of the spermatid nucleus from a spherical structure to an elongated organelle, during the latter part of spermatid differentiation.
The resolution of the male germline syncytium or cyst into individual gametes by packaging each spermatid into its own plasma membrane.
Generation of the female gamete; specialised haploid cells produced by meiosis and along with a male gamete takes part in sexual reproduction.
Construction of a stage-1 egg chamber in the anterior part of the germarium, from the progeny of germ-line and somatic stem cells. An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a germarium-derived cell becomes capable of differentiating autonomously into an oocyte cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a germarium-derived cell becomes capable of differentiating autonomously into an oocyte cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a germarium-derived cell becomes capable of differentiating autonomously into an oocyte cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this is found in Drosophila melanogaster.
Growth of the egg chamber between the time it leaves the germarium and the onset of vitellogenesis. During this time both nurse cells and the oocyte undergo developmental changes including nuclear organization and cytoplasmic growth. An example of this is found in Drosophila melanogaster.
The production of yolk. Yolk is a mixture of materials used for embryonic nutrition.
The production of yolk. Yolk is a mixture of materials used for embryonic nutrition.
The directed movement of an ovarian follicle cell that takes place during oogenesis. During egg chamber formation, follicle cells migrate to envelop the germ-line cysts and move in between cysts. At stage 10B, follicle cells migrate centripetally between the nurse cells and the oocyte, enclosing the anterior of the egg. An example of this is found in Drosophila melanogaster.
The directed movement of a border cell through the nurse cells to reach the oocyte. An example of this is found in Drosophila melanogaster.
The attachment of a somatic follicle cell to another somatic follicle cell or to its substratum, the germline cells. An example of this is found in Drosophila melanogaster.
The attachment of a somatic follicle cell to another somatic follicle cell or to its substratum, the germline cells. An example of this is found in Drosophila melanogaster.
Transfer of constituents synthesized in the ovarian nurse cells to the oocyte, through the ring canals, as the egg chamber is growing. An example of this is found in Drosophila melanogaster.
Assembly of the intercellular bridges that connect the germ-line cells of a female cyst.
Assembly of the intercellular bridges that connect the germ-line cells of a female cyst.
Attachment of the nurse cell nucleus to the plasma membrane.
The directed movement of cytoplasmic constituents synthesized in the nurse cells to the oocyte.
The construction of a chorion-containing eggshell. An example of this is found in Drosophila melanogaster.
Construction of the vitelline membrane portion of a chorion-containing eggshell. An example of this is found in Drosophila melanogaster.
Construction of the chorion portion of the eggshell, which comprises the channels for gas exchange in an insect eggshell.
Construction of the chorion portion of the eggshell, which comprises the channels for gas exchange in an insect eggshell.
Amplification by up to 60-fold of the loci containing the chorion gene clusters. Amplification is necessary for the rapid synthesis of chorion proteins by the follicle cells, and occurs by repeated firing of one or more origins located within each gene cluster.
The synthesis, deposition, and organization of the materials in a cell of an ovary; where the cell can then undergo meiosis and form an ovum. An example of this is found in Drosophila melanogaster.
The synthesis, deposition, and organization of the materials in a cell of an ovary; where the cell can then undergo meiosis and form an ovum. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of an axis in the oocyte. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of an axis in the oocyte. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by cells of the germ line. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by cells of the germ line. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by cells of the germ line. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by cells of the germ line. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
The directed movement of the oocyte nucleus within the cell as part of the establishment and maintenance of the dorsal/ventral axis of the oocyte. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by somatic cells. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by somatic cells. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by somatic cells. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by somatic cells. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along its anterior-posterior axis. An example of this is found in Drosophila melanogaster.
Polarization of the oocyte along its anterior-posterior axis. An example of this is found in Drosophila melanogaster.
Establishment of the specialized cytoplasm found at the poles of the egg. An example of this is found in Drosophila melanogaster.
Any process in which RNA is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process in which RNA is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process in which RNA is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process in which RNA is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process that modulates the frequency, rate or extent of the process in which oskar mRNA is transported to, or maintained in, the oocyte pole plasm.
Any process that modulates the frequency, rate or extent of the process in which oskar mRNA is transported to, or maintained in, the oocyte pole plasm.
Any process in which a protein is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process in which a protein is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process in which a protein is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process in which a protein is transported to, or maintained in, the oocyte pole plasm. An example of this is found in Drosophila melanogaster.
Any process that stops, prevents or reduces the rate that oskar mRNAs are effectively translated into protein.
Any process that stops, prevents or reduces the rate that oskar mRNAs are effectively translated into protein.
Any process that stops, prevents or reduces the rate that oskar mRNAs are effectively translated into protein.
Any process that stops, prevents or reduces the rate that oskar mRNAs are effectively translated into protein.
The introduction of semen or sperm into the genital tract of a female.
The physical displacement of sperm stored from previous mating encounters.
The generation of a mature, active peptide pheromone via processes unique to its processing and modification. An example of this process is found in Saccharomyces cerevisiae.
The generation of a mature, active peptide pheromone via processes unique to its processing and modification. An example of this process is found in Saccharomyces cerevisiae.
The generation of a mature, active peptide pheromone via processes unique to its processing and modification. An example of this process is found in Saccharomyces cerevisiae.
The generation of a mature, active peptide pheromone via processes unique to its processing and modification. An example of this process is found in Saccharomyces cerevisiae.
Any process involving pheromones that activates or increases the rate of transcription from an RNA polymerase II promoter.
Any process involving pheromones that activates or increases the rate of transcription from an RNA polymerase II promoter.
Any process involving pheromones that activates or increases the rate of transcription from an RNA polymerase II promoter.
Any process involving pheromones that activates or increases the rate of transcription from an RNA polymerase II promoter.
Any process involving pheromones that activates or increases the rate of transcription from an RNA polymerase II promoter.
Any process involving pheromones that activates or increases the rate of transcription from an RNA polymerase II promoter.
The union of male and female gametes to form a zygote.
The union of male and female gametes to form a zygote.
The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place.
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida.
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
The binding and fusion of a sperm, with the plasma membrane of the oocyte as part of the process of single fertilization. In sperm with flagella, binding occurs at the posterior (post-acrosomal) region of the sperm head.
The process in which the egg becomes metabolically active, initiates protein and DNA synthesis and undergoes structural changes to its cortex and/or cytoplasm.
The merging of two pronuclei in a fertilized egg to fuse and produce a single zygotic genome.
The process in which anatomical structures are generated and organized. Morphogenesis pertains to the creation of form.
The process in which anatomical structures are generated and organized. Morphogenesis pertains to the creation of form.
The process in which anatomical structures are generated and organized. Morphogenesis pertains to the creation of form.
The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant.
The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant.
The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant.
The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant.
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
Any process that modulates the rate or extent of progress through the mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the preblastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the preblastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the preblastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the preblastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the preblastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the preblastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
A cell cycle process that modulates the rate or extent of the progression through the syncytial blastoderm mitotic cell cycle.
The separation of a multi-nucleate cell or syncytium into individual cells. An example of this is found in Drosophila melanogaster embryo development.
The hierarchical steps resulting in the progressive subdivision of the anterior/posterior axis of the embryo.
Subdivision of the embryo along the anterior/posterior axis into anterior, posterior and terminal regions.
The specification of the dorsal/ventral axis of the embryo, through the products of genes expressed in the zygote.
The specification of the dorsal/ventral axis of the embryo, through the products of genes expressed in the zygote.
The specification of the dorsal/ventral axis of the embryo, through the products of genes expressed in the zygote.
The process that results in the patterns of cell differentiation that will arise in an embryo.
The process that results in the patterns of cell differentiation that will arise in an embryo.
The process that results in the patterns of cell differentiation that will arise in an embryo.
The specification of the anterior/posterior axis of the embryo by products of genes expressed in the zygote; exemplified in insects by the gap genes, pair rule genes and segment polarity gene cascade.
Specification of the anterior (head and thoracic segments) of the embryo by the gap genes; exemplified in insects by the actions of hunchback gene product.
Specification of the central (trunk) regions of the embryo by the gap genes; exemplified in insects by the actions of the Kruppel gene product.
The activation of genes encoding transcription factors in the central region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila Kruppel gene by the hunchback and bicoid gene products.
The activation of genes encoding transcription factors in the central region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila Kruppel gene by the hunchback and bicoid gene products.
The activation of genes encoding transcription factors in the central region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila Kruppel gene by the hunchback and bicoid gene products.
The activation of genes encoding transcription factors in the central region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila Kruppel gene by the hunchback and bicoid gene products.
The activation of genes encoding transcription factors in the central region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila Kruppel gene by the hunchback and bicoid gene products.
The activation of genes encoding transcription factors in the central region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila Kruppel gene by the hunchback and bicoid gene products.
Specification of the borders of central gap gene expression mediated largely by the effects of other gap genes; in insects this is exemplified by knirps repression of Kruppel.
The regionalization process in which the posterior (abdominal) regions of the embryo are specified by the gap genes.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
The activation of genes encoding transcription factors in the posterior region of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila knirps gene.
Specification of the borders of posterior gap gene expression mediated largely by the effects of other gap genes; in insects this is exemplified by hunchback and tailless repression of knirps.
Specification of the terminal regions (the two non-segmented ends) of the embryo by the gap genes; exemplified in insects by the actions of huckebein and tailless gene products.
The activation of genes encoding transcription factors at the anterior and posterior ends of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila tailless and huckebein genes.
The activation of genes encoding transcription factors at the anterior and posterior ends of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila tailless and huckebein genes.
The activation of genes encoding transcription factors at the anterior and posterior ends of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila tailless and huckebein genes.
The activation of genes encoding transcription factors at the anterior and posterior ends of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila tailless and huckebein genes.
The activation of genes encoding transcription factors at the anterior and posterior ends of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila tailless and huckebein genes.
The activation of genes encoding transcription factors at the anterior and posterior ends of an insect embryo by a combination of maternal regulatory signals and interactions among themselves; exemplified by the activation of expression of the Drosophila tailless and huckebein genes.
Specification of the borders of terminal gap gene expression mediated largely by the effects of other gap genes.
The regionalization process that divides the spatial regions of an embryo into serially repeated regions.
Allocation of cells to parasegments in the embryo, through the action of overlapping series of pair rule gene activities.
Division of the 14 parasegments of the embryo into anterior and posterior compartments; exemplified by the actions of the segment polarity gene products.
The establishment of an organism's body plan or part of an organism with respect to the left and right halves. The pattern can either be symmetric, such that the halves are mirror images, or asymmetric where the pattern deviates from this symmetry.
A complex and coordinated series of cellular movements that occurs at the end of cleavage during embryonic development of most animals. The details of gastrulation vary from species to species, but usually result in the formation of the three primary germ layers, ectoderm, mesoderm and endoderm.
Formation of a ventral indentation (furrow) from the blastoderm epithelium, which is internalized to form a tube in the interior of the embryo, marking the start of gastrulation.
The regionalization process in which the area where the ventral midline will form is specified.
The regionalization process in which the area where the ventral midline will form is specified.
The regionalization process in which the area where the ventral midline will form is specified.
The regionalization process in which the area where the ventral midline will form is specified.
Formation of a cup-shaped invagination at the posterior end of the embryo, bringing the posterior midgut and hindgut primordia into the interior.
Internalization of the anterior midgut into the interior of the embryo.
Formation of a partial necklace of inturning tissue on the lateral sides of the embryo, along the dorsal-ventral axis. This furrow demarcates head from thorax in the developing protostome.
Elongation of the germ band on the ventral side of the embryo, accompanied by a halving in width. The elongation process pushes the posterior midgut invagination closed and compresses the amnioserosa further.
Formation of the amnioserosa, an epithelium that occupies a hole in the embryonic dorsal epidermis. This occurs by the transformation of a narrow strip of cells at the dorsal midline of the blastoderm from columnar to squamous cells, accompanied by a lateral shift.
The process in which segments assume individual identities; exemplified in insects by the actions of the products of the homeotic genes.
The specification of the characteristic structures of the head segments following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The specification of the characteristic structures of the labial segment following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The specification of the characteristic structures of the maxillary segment following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The specification of the characteristic structures of the antennal segment following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The specification of the characteristic structures of the thoracic segments following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The specification of the characteristic structures of the abdominal segments following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The regionalization process in which embryonic segments are divided into compartments that will result in differences in cell differentiation.
The process giving rise to specification of cell identity in the anterior compartments of the segmented embryo.
The process involved in the specification of cell identity in the posterior compartments of the segmented embryo.
Any developmental process that results in the creation of defined areas or spaces within an organism to which cells respond and eventually are instructed to differentiate.
Any developmental process that results in the creation of defined areas or spaces within an organism to which cells respond and eventually are instructed to differentiate.
The spreading of the amnioserosa from its compressed state to cover the whole of the dorsal surface. Initiating in the thorax and spreading posteriorly, it is accompanied by the transition from a parasegmental to segmental division of the embryo.
The process during Drosophila embryogenesis whereby the ectodermal cells of the lateral epithelium stretch in a coordinated fashion to internalize the amnioserosa cells and close the embryo dorsally.
Events that occur at the start of dorsal closure.
The cell fate determination process in which a cell within the dorsal ectoderm becomes capable of differentiating autonomously into a leading edge cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The change in shape of cells at the dorsal-most (leading) edge of the epidermis from being polygonal to being elongated in the dorsal/ventral axis.
Dorsally-directed movement of a cell at the leading edge of the epithelium over the amnioserosa.
Closure of the dorsal hole. Filopodia extending from each leading edge interdigitate at the dorsal midline and appear to prime the formation of adherens junctions between the two rows of leading edge cells. Newly formed septate junctions are also used to seal the dorsal hole.
Morphogenesis of an animal organ. An organ is defined as a tissue or set of tissues that work together to perform a specific function or functions. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
The process whose specific outcome is the progression of a tissue over time, from its formation to the mature structure.
The process whose specific outcome is the progression of a tissue over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the ectoderm over time, from its formation to the mature structure. In animal embryos, the ectoderm is the outer germ layer of the embryo, formed during gastrulation.
The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a neuroblast cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this process is found in Mus musculus.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a neuroblast cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this process is found in Mus musculus.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a neuroblast cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this process is found in Mus musculus.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a neuroblast cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this process is found in Mus musculus.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a neuroblast cell regardless of its environment; upon determination, the cell fate cannot be reversed. An example of this process is found in Mus musculus.
A organ system process carried out by any of the organs or tissues of neurological system.
A organ system process carried out by any of the organs or tissues of neurological system.
A organ system process carried out by any of the organs or tissues of neurological system.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a ganglion mother cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a glial cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The expansion of a neuroblast population by cell division. A neuroblast is any cell that will divide and give rise to a neuron.
The expansion of a neuroblast population by cell division. A neuroblast is any cell that will divide and give rise to a neuron.
Any process that stops, prevents, or reduces the frequency, rate or extent of the proliferation of neuroblasts.
Any process that stops, prevents, or reduces the frequency, rate or extent of the proliferation of neuroblasts.
Any process that stops, prevents, or reduces the frequency, rate or extent of the proliferation of neuroblasts.
Any process that stops, prevents, or reduces the frequency, rate or extent of the proliferation of neuroblasts.
Any process that stops, prevents, or reduces the frequency, rate or extent of the proliferation of neuroblasts.
A change in the morphology or behavior of a neuroblast resulting from exposure to an activating factor such as a cellular or soluble ligand.
A change in the morphology or behavior of a neuroblast resulting from exposure to an activating factor such as a cellular or soluble ligand.
De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The process in which an axon recognizes and binds to a set of cells with which it may form stable connections.
The collection of axons into a bundle of rods, known as a fascicle.
Separation of axons away from a bundle of axons known as a fascicle.
Separation of a motor axon away from a bundle of axons known as a fascicle.
The aggregation, arrangement and bonding together of a set of components to form a synapse.  This process ends when the synapse is mature (functional).
The aggregation, arrangement and bonding together of a set of components to form a synapse.  This process ends when the synapse is mature (functional).
The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
The process whose specific outcome is the progression of the ventral midline over time, from its formation to the mature structure. In protostomes (such as insects, snails and worms) as well as deuterostomes (vertebrates), the midline is an embryonic region that functions in patterning of the adjacent nervous tissue. The ventral midline in insects is a cell population extending along the ventral surface of the embryo and is the region from which cells detach to form the ventrally located nerve cords. In vertebrates, the midline is originally located dorsally. During development, it folds inwards and becomes the ventral part of the dorsally located neural tube and is then called the ventral midline, or floor plate.
The process whose specific outcome is the progression of the ventral cord over time, from its formation to the mature structure. The ventral cord is one of the distinguishing traits of the central nervous system of all arthropods (such as insects, crustaceans and arachnids) as well as many other invertebrates, such as the annelid worms.
The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
The process whose specific outcome is the progression of the stomatogastric nervous system over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the peripheral nervous system over time, from its formation to the mature structure. The peripheral nervous system is one of the two major divisions of the nervous system. Nerves in the PNS connect the central nervous system (CNS) with sensory organs, other organs, muscles, blood vessels and glands.
The process whose specific outcome is the progression of sensory organs over time, from its formation to the mature structure.
The process whose specific outcome is the progression of an open tracheal system over time, from its formation to the mature structure. An open tracheal system is a respiratory system, a branched network of epithelial tubes that supplies oxygen to target tissues via spiracles. An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into an epithelial cell within an open tracheal system regardless of its environment; upon determination, the cell fate cannot be reversed. Tracheal cells are set aside as 10 clusters of approximately 80 cells on each side of the embryo (termed tracheal placodes). An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into an epithelial cell within an open tracheal system regardless of its environment; upon determination, the cell fate cannot be reversed. Tracheal cells are set aside as 10 clusters of approximately 80 cells on each side of the embryo (termed tracheal placodes). An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into an epithelial cell within an open tracheal system regardless of its environment; upon determination, the cell fate cannot be reversed. Tracheal cells are set aside as 10 clusters of approximately 80 cells on each side of the embryo (termed tracheal placodes). An example of this is found in Drosophila melanogaster.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into an epithelial cell within an open tracheal system regardless of its environment; upon determination, the cell fate cannot be reversed. Tracheal cells are set aside as 10 clusters of approximately 80 cells on each side of the embryo (termed tracheal placodes). An example of this is found in Drosophila melanogaster.
The projection of branches of an open tracheal system towards their target tissues. An example of this is found in Drosophila melanogaster.
The orderly movement of epithelial cells during development of an open tracheal system. An example of this is found in Drosophila melanogaster.
The orderly movement of epithelial cells during development of an open tracheal system. An example of this is found in Drosophila melanogaster.
Formation of primary branches in the open tracheal system. These form from small groups of cells that migrate out at specific positions, organizing into tubes as they migrate. An example of this is found in Drosophila melanogaster.
Sprouting of secondary branches in an open tracheal system. These form from the tips of primary branches and are formed by individual cells that roll up into unicellular tubes. An example of this is found in Drosophila melanogaster.
Formation of terminal branches in the open tracheal system. These are long cytoplasmic extensions that form fine tubules that transport oxygen directly to the tissues. An example of the process is found in Drosophila melanogaster.
The process whose specific outcome is the progression of the salivary gland over time, from its formation to the mature structure. Salivary glands include any of the saliva-secreting exocrine glands of the oral cavity.
Determination of where the salivary gland forms, the total number of salivary gland cells and how many cells are allocated to each of the specialised cell types within the salivary gland.
Determination in a larval organism of where the salivary gland forms, the total number of salivary gland cells and how many cells are allocated to each of the specialised cell types within the salivary gland.
Determination in an adult organism of where the salivary gland forms, the total number of salivary gland cells and how many cells are allocated to each of the specialised cell types within the salivary gland.
The process in which the anatomical structures of the salivary gland are generated and organized.
The process, occurring in the larva, by which the anatomical structures of the salivary gland are generated and organized.
The process in which the anatomical structures of the adult salivary gland are generated and organized.
The process whose specific outcome is the progression of the oenocyte over time, from its formation to the mature structure. The oenocytes are large secretory cells found in clusters underlying the epidermis of larval abdominal segments.
The process whose specific outcome is the progression of the ectodermal digestive tract over time, from its formation to the mature structure. The ectodermal digestive tract includes those portions that are derived from ectoderm.
The process in which the anatomical structures of the foregut are generated and organized.
The process in which the anatomical structures of the anterior midgut (ectodermal) are generated and organized.
The process in which the anatomical structures of the hindgut are generated and organized.
The process in which the anatomical structures of the Malpighian tubule are generated and organized. This process takes place entirely during the embryonic phase. A Malpighian tubule is a fine, thin-walled excretory tubule in insects which leads into the posterior part of the gut.
The process whose specific outcome is the progression of the imaginal disc over time, from its formation to the metamorphosis to form adult structures. Imaginal discs are epithelial infoldings in the larvae of holometabolous insects that develop into adult structures (legs, antennae, wings, etc.).
Allocation of embryonic cells to the imaginal disc founder populations, groups of cells that are committed to contribute to the formation of an imaginal disc compartment.
The increase in mass of imaginal discs by cell proliferation prior to metamorphosis. Imaginal discs are epithelial infoldings in the larvae of holometabolous insects that develop into adult structures (legs, antennae, wings, etc.) during metamorphosis from larval to adult form.
The regionalization process that results in defined areas of the imaginal disc that will undergo specific cell differentaiton. Imaginal discs are epithelial infoldings in the larvae of holometabolous insects that develop into adult appendages (legs, antennae, wings, etc.) during metamorphosis from larval to adult form.
The establishment, maintenance and elaboration of the anterior/posterior axis of the imaginal disc. Imaginal discs are epithelial infoldings in the larvae of holometabolous insects that rapidly develop into adult appendages during metamorphosis from larval to adult form.
The establishment, maintenance and elaboration of the proximal/distal axis of the imaginal disc. Imaginal disks are masses of hypodermic cells, carried by the larvae of some insects after leaving the egg, from which masses the wings and legs of the adult are subsequently formed.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the imaginal disc. Imaginal disks are masses of hypodermic cells, carried by the larvae of some insects after leaving the egg, from which masses the wings and legs of the adult are subsequently formed.
The establishment, maintenance and elaboration of the dorsal/ventral axis of the imaginal disc. Imaginal disks are masses of hypodermic cells, carried by the larvae of some insects after leaving the egg, from which masses the wings and legs of the adult are subsequently formed.
Formation and/or maintenance of a lineage boundary between dorsal and ventral compartments that cells cannot cross, thus separating the populations of cells in each compartment.
Formation and/or maintenance of a lineage boundary between dorsal and ventral compartments that cells cannot cross, thus separating the populations of cells in each compartment.
The process in which the anatomical structures derived from the clypeo-labral disc are generated and organized. This includes the transformation of a clypeo-labal imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into recognizable adult structures including the labrum, anterior and posterior cibarial plates, fish trap bristles, epistomal sclerite and clypeus.
The process in which the anatomical structures derived from the clypeo-labral disc are generated and organized. This includes the transformation of a clypeo-labal imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into recognizable adult structures including the labrum, anterior and posterior cibarial plates, fish trap bristles, epistomal sclerite and clypeus.
The process in which the anatomical structures derived from the labial disc are generated and organized. This includes the transformation of a labial imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into recognizable adult structures including parts of the proboscis.
The process in which the anatomical structures derived from the eye-antennal disc are generated and organized. This includes the transformation of an eye-antennal imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into recognizable adult structures including the eye, antenna, head capsule and maxillary palps.
The morphogenetic furrow is a dorsoventral indentation which sweeps anteriorly across the eye disc. Ommatidia begin to form along the furrow, resulting in a graded series of ommatidial development across the anterior/posterior axis of the disc.
The process in which the R8 photoreceptor commits to its cell fate. The R8 receptor contributes the central part of the rhabdomere in the basal parts of the ommatidium.
The process in which the R8 photoreceptor commits to its cell fate. The R8 receptor contributes the central part of the rhabdomere in the basal parts of the ommatidium.
The process in which the R1/R6 photoreceptors commit to their cell fate. R1 and R6 are paired photoreceptors which contribute the outer rhabdomeres.
The process in which the R2/R5 photoreceptors commit to their cell fate. R2 and R5 are paired photoreceptors which contribute the outer rhabdomeres.
The process in which the R3/R4 photoreceptors commit to their cell fate. R3 and R4 are paired photoreceptors which contribute the outer rhabdomeres.
The process in which the R7 photoreceptor commits to its cell fate. The R7 receptor contributes the central part of the rhabdomere in the apical parts of the ommatidium.
Any process that modulates the frequency, rate or extent of rhodopsin gene expression. This includes transcriptional, translational, or posttranslational regulation.
The process whose specific outcome is the progression of the antenna over time, from its formation to the mature structure. The antenna are the sensory structures on the head that are capable of detecting various environmental stimuli.
The process in which the anatomical structures derived from the prothoracic disc are generated and organized. This includes the transformation of a prothoracic imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into the recognizable adult humerous and anterior spiracle.
The process in which the anatomical structures derived from the wing disc are generated and organized. This includes the transformation of a wing imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into recognizable adult structures including the wing hinge, wing blade and pleura.
The establishment, maintenance and elaboration of the proximal/distal axis of the wing disc, a precursor to the adult wing.
The regionalization process in which the area of a imaginal disc-derived wing that will form a wing vein is specified.
The coming together of the dorsal and ventral surfaces of the imaginal disc-derived wing during the conversion of a folded single layered wing disc to a flat bilayered wing.
The process in which the anatomical structures of the imaginal disc-derived wing are generated and organized. The wing is an appendage modified for flying.
The process whose specific outcome is the progression of the dorsal part of the body over time, from its formation to the mature structure.
The process in which the anatomical structures derived from the leg disc are generated and organized. This includes the transformation of a leg imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into recognizable adult structures including the leg, coxa and ventral thoracic pleura.
The establishment, maintenance and elaboration of the proximal/distal axis of the leg imaginal disc, a precursor to the adult leg.
The process in which the anatomical structures of a leg derived from an imaginal disc are generated and organized. A leg is a limb on which an animal walks and stands. An example of this is found in Drosophila melanogaster.
The process in which the anatomical structures derived from the haltere disc are generated and organized. This includes the transformation of a haltere imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into the recognizable adult capitellum, pedicel, haltere sclerite, metathoracic spiracle and metanotum.
The process whose specific outcome is the progression of the haltere over time, from its formation to the mature structure. The haltere is the club-shaped 'balancers' found on each side of the metathorax among the true flies (Diptera). They are the much-modified hind wings.
The process in which the anatomical structures derived from the genital disc are generated and organized. This includes the transformation of a genital imaginal disc from a monolayered epithelium in the larvae of holometabolous insects into the recognizable adult genital structures, the anal plates and the hind gut.
The process whose specific outcome is the progression of the genitalia over time, from formation as part of the genital disc to the mature structure. An example of this is found in Drosophila melanogaster.
The process whose specific outcome is the progression of the male genitalia over time, from formation as part of the genital disc to the mature structure. An example of this is found in Drosophila melanogaster.
The process whose specific outcome is the progression of the female genitalia over time, from formation as part of the genital disc to the mature structure. An example of this is found in Drosophila melanogaster.
The process whose specific outcome is the progression of the analia over time, from its formation to the mature structure. The analia is the posterior-most vertral appendage that develops from the genital disc. An example of this process is analia development in Drosophila melanogaster.
The process in which the anatomical structures derived from the histoblast disc are generated and organized. This includes the transformation of histoblast cells into adult structures during pupal metamorphosis. Histoblast cells are cells founded in the embryo that are the progenitors to the adult abdomen.
The negative regulation of the differentiation of polytenized larval hypodermal cells from abdominal histoblasts. The abdominal histoblasts remain a small cluster of diploid cells among the polytenized larval hypodermal cells.
The process in which the anatomical structures of the tergite are generated and organized. The tergite is the primary plate or sclerite forming the dorsal surface of any insect body segment.
The process in which the anatomical structures of the sternite are generated and organized. The sternite is the plate or sclerite on the underside of a body segment.
The process whose specific outcome is the progression of the endoderm over time, from its formation to the mature structure. The endoderm is the innermost germ layer that develops into the gastrointestinal tract, the lungs and associated tissues.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into an endoderm cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The process whose specific outcome is the progression of the midgut over time, from its formation to the mature structure. The midgut is the middle part of the alimentary canal from the stomach, or entrance of the bile duct, to, or including, the large intestine.
The process of cell-cell signaling between visceral mesoderm cells and endoderm cells that is involved in the differentiation of cells in the midgut.
The process whose specific outcome is the progression of the anterior midgut over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the posterior midgut over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the mesoderm over time, from its formation to the mature structure. The mesoderm is the middle germ layer that develops into muscle, bone, cartilage, blood and connective tissue.
A cell-cell signaling process occurring between the two gastrulation-generated layers of the ectoderm and the mesoderm.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a mesoderm cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a mesoderm cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
The process whose specific outcome is the progression of the digestive tract mesoderm over time, from its formation to the mature structure. The digestive tract mesoderm is portion of the middle layer of the three primary germ layers of the embryo which will go on to form part of the digestive tract of the organism.
The process whose specific outcome is the progression of the fat body over time, from its formation to the mature structure. A fat body is an insect gland dorsal to the insect gut, with a function analogous to that of the vertebrate liver. It is a storage organ for fats, glycogen and protein and is a major site of intermediary metabolism.
The process whose specific outcome is the progression of the larval fat body over time, from its formation to the mature structure. The larval fat body consists of a bilaterally symmetrical monolayer of cells lying between the gut and the muscles of the body wall. As in other tissues of the larva, the cells of the fat body complete their divisions in the embryo and increase in size and ploidy during larval life.
The process whose specific outcome is the progression of the adult fat body over time, from its formation to the mature structure. Larval fat body cells that remain at eclosion degenerate in the first 2 to 4 days of adult life, leaving behind the smaller cells of the adult fat body.
The process whose specific outcome is the progression of the gonadal mesoderm over time, from its formation to the mature structure. The gonadal mesoderm is the middle layer of the three primary germ layers of the embryo which will go on to form the gonads of the organism.
The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
The process whose specific outcome is the progression of the larval heart over time, from its formation to the mature structure. In Drosophila the larval heart (dorsal vessel) is a continuous tube of mesodormal cells that runs beneath the dorsal midline of the epidermis, divided into an anterior aorta and a posterior heart proper.
The migration of mesodermal cells during gastrulation to help establish the multilayered body plan of the organism.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a cardioblast cell regardless of its environment; upon determination, the cell fate cannot be reversed. A cardioblast is a cardiac precursor cell. It is a cell that has been committed to a cardiac fate, but will undergo more cell division rather than terminally differentiating.
The process whose specific outcome is the progression of the adult heart over time, from its formation to the mature structure.
The process whose specific outcome is the progression of lymph nodes over time, from their formation to the mature structure. A lymph node is a round, oval, or bean shaped structure localized in clusters along the lymphatic vessels, with a distinct internal structure including specialized vasculature and B- and T-zones for the activation of lymphocytes.
The process whose specific outcome is the progression of the lymph gland over time, from its formation to the mature structure. The lymph gland is one of the sites of hemocyte differentiation. It consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The process whose specific outcome is the progression of the lymph gland over time, from its formation to the mature structure. The lymph gland is one of the sites of hemocyte differentiation. It consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The process whose specific outcome is the progression of the lymph gland over time, from its formation to the mature structure. The lymph gland is one of the sites of hemocyte differentiation. It consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The process whose specific outcome is the progression of the lymph gland over time, from its formation to the mature structure. The lymph gland is one of the sites of hemocyte differentiation. It consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The process whose specific outcome is the progression of the hemocyte over time, from its formation to the mature structure. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen.
The process whose specific outcome is the progression of the muscle over time, from its formation to the mature structure. The muscle is an organ consisting of a tissue made up of various elongated cells that are specialized to contract and thus to produce movement and mechanical work.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a myoblast regardless of its environment; upon determination, the cell fate cannot be reversed. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers.
The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are: the fusion of myoblasts to form myotubes that increase in size by further fusion to them of myoblasts, the formation of myofibrils within their cytoplasm and the establishment of functional neuromuscular junctions with motor neurons. At this stage they can be regarded as mature muscle fibers.
The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are: the fusion of myoblasts to form myotubes that increase in size by further fusion to them of myoblasts, the formation of myofibrils within their cytoplasm and the establishment of functional neuromuscular junctions with motor neurons. At this stage they can be regarded as mature muscle fibers.
A process in which non-proliferating myoblasts fuse to existing fibers or to myotubes to form new fibers. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into a muscle cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The process whose specific outcome is the progression of the visceral muscle over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the larval visceral muscle over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the adult visceral muscle over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the somatic muscle over time, from its formation to the mature structure. Somatic muscles are striated muscle structures that connect to the exoskeleton or cuticle.
The process whose specific outcome is the progression of the larval somatic muscle over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the adult somatic muscle over time, from its formation to the mature structure.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuromuscular junction.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuromuscular junction.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuromuscular junction.
The biological process in which a synapse between a motor neuron and a muscle is initially formed.
Any process that establishes and transmits the specification of sexual status of an individual organism.
Any process that establishes and transmits the specification of mating type upon an individual. Mating types are the equivalent in microorganisms of the sexes in higher organisms.
Any mating-type specific process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
Any mating-type specific process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
The conversion of a single-cell organism from one mating type to another by the precise replacement of a DNA sequence at the expressed mating type locus with a copy of a sequence from a donor locus.
The conversion of the mating-type locus from one allele to another resulting from the recombinational repair of a site-specific double-strand break at the mating-type locus with information from a silent donor sequence. There is no reciprocal exchange of information because the mating-type locus copies information from the donor sequence and the donor sequence remains unchanged.
The process that determines which donor locus a cell uses, in preference to another, in mating type switching.
The activation of recombination at a mating type locus, such that it is used in preference to the other donor locus for mating type switching; exemplified by the HML locus and surrounding sequences on Chromosome III in Saccharomyces cerevisiae.
The inactivation of recombination at sequences around a mating type donor locus, with the consequence that the other donor is the only one available for mating type switching; exemplified by the HML locus and surrounding sequences on Chromosome III in Saccharomyces cerevisiae.
The sex determination process that results in the initial specification of sexual status of an individual organism.
The transmission of information about sexual status from the initial, general, determination to signals specific to the soma.
The developmental process in which an organism senses the number of X chromosomes and autosomes in its genomic complement and responds to it.
The developmental process in which an organism interprets its X to autosomal chromosomal complement.
The transmission of information about sexual status, from the initial general determination, to signals specific to the germ-line.
The process that mediates the interactions between somatic cells and gonadal cells that ultimately results in the specification of sexual status of the organism.
The sex determination processes that take place after the initial transmission of the sexual phenotype to specific information pathways.
The events determining the somatic sexual phenotype after the initial transmission of that phenotype to soma-specific information pathways.
The events determining the germ-line sexual phenotype after the initial transmission of that phenotype to germ-line-specific information pathways.
The establishment of the sex of an organism by physical differentiation.
Compensating for the variation in the unpaired sex chromosome:autosome chromosome ratios between sexes by activation or inactivation of genes on one or both of the sex chromosomes.
A biological process in which an animal physically develops after birth or hatching, involving a conspicuous and relatively abrupt change in the animal's form or structure. Examples include the change from tadpole to frog, and the change from larva to adult. An example of this is found in Drosophila melanogaster.
A biological process in which an animal physically develops after birth or hatching, involving a conspicuous and relatively abrupt change in the animal's form or structure. Examples include the change from tadpole to frog, and the change from larva to adult. An example of this is found in Drosophila melanogaster.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving ecdysteroids, a group of polyhydroxylated ketosteroids which initiate post-embryonic development, including the metamorphosis of immature forms and the development of the reproductive system and the maturation of oocytes in adult females.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ecdysteroids.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ecdysteroids.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ecdysteroids.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ecdysteroids.
Any process that modulates the frequency, rate or extent of the regulated release of ecdysteroid from a cell.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving juvenile hormone.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of juvenile hormone.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of juvenile hormone.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of juvenile hormone.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of juvenile hormone.
Any process that modulates the frequency, rate or extent of juvenile hormone secretion.
Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538).
Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538).
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
The process in which the anatomical structures derived from an imaginal disc are generated and organized. The imaginal discs are epithelial infoldings in the larvae of holometabolous insects that develop into adult appendages (legs, antennae, wings, etc.) during metamorphosis from larval to adult form.
The process in which the anatomical structures derived from an imaginal disc are generated and organized. The imaginal discs are epithelial infoldings in the larvae of holometabolous insects that develop into adult appendages (legs, antennae, wings, etc.) during metamorphosis from larval to adult form.
The eversion (turning inside out) of imaginal discs from their peripodial sacs, resulting in movement of the epithelium to the outside of the larval epidermis.
The emergence of an adult insect from a pupa case.
Any process that modulates the frequency, rate or extent of the emergence of an insect from a pupa-case or of a larva from an egg.
Any process that modulates the frequency, rate or extent of chitin-based cuticular tanning.
Any process that modulates the frequency, rate or extent of chitin-based cuticular tanning.
The set of physiological processes that allow an embryo or foetus to develop within the body of a female animal. It covers the time from fertilization of a female ovum by a male spermatozoon until birth.
The set of physiological processes that allow an embryo or foetus to develop within the body of a female animal. It covers the time from fertilization of a female ovum by a male spermatozoon until birth.
Attachment of the blastocyst to the uterine lining.
The reproductive process in which the parent is separated from its offspring either by giving birth to live young or by laying eggs.
The reproductive process in which the parent is separated from its offspring either by giving birth to live young or by laying eggs.
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
An aging process that has as participant a cell after a cell has stopped dividing. Cell aging may occur when a cell has temporarily stopped dividing through cell cycle arrest (GO:0007050) or when a cell has permanently stopped dividing, in which case it is undergoing cellular senescence (GO:0090398). May precede cell death (GO:0008219) and succeed cell maturation (GO:0048469).
A developmental process that arises as the cell progresses toward the end of its lifespan and cause changes cellular metabolism, resulting in a decline in cell function; for example, one aspect of general metabolic decline is a decrease in the efficiency of protein synthesis.
A developmental process that arises as the cell progresses toward the end of its lifespan and cause changes cellular metabolism, resulting in a decline in cell function; for example, one aspect of general metabolic decline is a decrease in the efficiency of protein synthesis.
A developmental process that arises as the cell progresses toward the end of its lifespan and cause changes cellular metabolism, resulting in a decline in cell function; for example, one aspect of general metabolic decline is a decrease in the efficiency of protein synthesis.
A developmental process that arises as the cell progresses toward the end of its lifespan and cause changes cellular metabolism, resulting in a decline in cell function; for example, one aspect of general metabolic decline is a decrease in the efficiency of protein synthesis.
The cell aging process that results in the nucleolus breaking down into fragments.
The cell aging process that results in the nucleolus breaking down into fragments.
A form of programmed cell death that is accompanied by the formation of autophagosomes. Autophagic cell death is characterized by lack of chromatin condensation and massive vacuolization of the cytoplasm, with little or no uptake by phagocytic cells.
A form of programmed cell death that is accompanied by the formation of autophagosomes. Autophagic cell death is characterized by lack of chromatin condensation and massive vacuolization of the cytoplasm, with little or no uptake by phagocytic cells.
A form of programmed cell death that is accompanied by the formation of autophagosomes. Autophagic cell death is characterized by lack of chromatin condensation and massive vacuolization of the cytoplasm, with little or no uptake by phagocytic cells.
A form of programmed cell death that is accompanied by the formation of autophagosomes. Autophagic cell death is characterized by lack of chromatin condensation and massive vacuolization of the cytoplasm, with little or no uptake by phagocytic cells.
A form of programmed cell death that is accompanied by the formation of autophagosomes. Autophagic cell death is characterized by lack of chromatin condensation and massive vacuolization of the cytoplasm, with little or no uptake by phagocytic cells.
Repression of transcription at silent mating-type loci by alteration of the structure of chromatin.
Repression of transcription at silent mating-type loci by alteration of the structure of chromatin.
Repression of transcription at silent mating-type loci by alteration of the structure of chromatin.
Repression of transcription at silent mating-type loci by alteration of the structure of chromatin.
Repression of transcription at silent mating-type loci by alteration of the structure of chromatin.
Increase in abundance, as cells age, of circular DNA molecules that originate in the chromosome but are excised and circularized, often by intramolecular homologous recombination between direct tandem repeats, and replicated independently of chromosomal replication.
Increase in abundance, as cells age, of circular DNA molecules that originate in the chromosome but are excised and circularized, often by intramolecular homologous recombination between direct tandem repeats, and replicated independently of chromosomal replication.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus.
The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms.
The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms.
The whole of the physical, chemical, and biochemical processes carried out by multicellular organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.
The elimination by an organism of the waste products that arise as a result of metabolic activity. These products include water, carbon dioxide (CO2), and nitrogenous compounds.
The controlled release of a fluid by a cell or tissue in an animal.
The periodic shedding of part or all of a chitin-based cuticle, which is then replaced by a new cuticle. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a chitin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Drosophila melanogaster.
The process of hardening of a chitin-based cuticle.
The process of hardening of a chitin-based cuticle.
The process of hardening of a chitin-based cuticle.
The adhesion of the puparia of Diptera to their substrate; normally effected by a 'glue' secreted by the larval salivary gland and expectorated at the time of pupariation.
The regulated release of milk from the mammary glands and the period of time that a mother lactates to feed her young.
A protein activation cascade that contributes to blood coagulation and consists of the interactions among high molecular weight kininogen, prekallikrein, and factor XII that lead to the activation of clotting factor X.
A protein activation cascade that contributes to blood coagulation and consists of the self-limited process linking exposure and activation of tissue factor to the activation of clotting factor X.
The stopping of bleeding (loss of body fluid) or the arrest of the circulation to an organ or part.
The series of events required for an organism to receive a sensory stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
The sequence of reactions within a cell required to convert absorbed photons into a molecular signal.
The sequence of reactions within a cell required to convert absorbed photons from visible light into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm.
The sequence of reactions within a cell required to convert absorbed photons from visible light into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm.
The sequence of reactions within a cell required to convert absorbed photons from UV light into a molecular signal; ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 400 nanometers.
The sequence of reactions within a cell required to convert absorbed photons from UV light into a molecular signal; ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 400 nanometers.
The sequence of reactions within a cell required to convert absorbed photons from UV light into a molecular signal; ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 400 nanometers.
The sequence of reactions within a cell required to convert absorbed photons from UV light into a molecular signal; ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 400 nanometers.
The sequence of reactions within a cell required to convert absorbed photons from UV light into a molecular signal; ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 400 nanometers.
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
The series of events required for an organism to receive a sensory chemical stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events required for an organism to receive a gustatory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Gustation involves the direct detection of chemical composition, usually through contact with chemoreceptor cells. This is a neurological process.
The series of events required for an organism to receive a gustatory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Gustation involves the direct detection of chemical composition, usually through contact with chemoreceptor cells. This is a neurological process.
The series of events required for an organism to receive a gustatory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Gustation involves the direct detection of chemical composition, usually through contact with chemoreceptor cells. This is a neurological process.
The series of events required for an organism to receive a gustatory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Gustation involves the direct detection of chemical composition, usually through contact with chemoreceptor cells. This is a neurological process.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
The series of events required for an organism to receive an olfactory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Olfaction involves the detection of chemical composition of an organism's ambient medium by chemoreceptors. This is a neurological process.
The series of events required for an organism to receive an olfactory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Olfaction involves the detection of chemical composition of an organism's ambient medium by chemoreceptors. This is a neurological process.
The series of events required for an organism to receive an olfactory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Olfaction involves the detection of chemical composition of an organism's ambient medium by chemoreceptors. This is a neurological process.
The series of events required for an organism to receive an olfactory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Olfaction involves the detection of chemical composition of an organism's ambient medium by chemoreceptors. This is a neurological process.
The internally coordinated responses (actions or inactions) of animals (individuals or groups) to internal or external stimuli, via a mechanism that involves nervous system activity.
The internally coordinated responses (actions or inactions) of animals (individuals or groups) to internal or external stimuli, via a mechanism that involves nervous system activity.
The internally coordinated responses (actions or inactions) of animals (individuals or groups) to internal or external stimuli, via a mechanism that involves nervous system activity.
The internally coordinated responses (actions or inactions) of animals (individuals or groups) to internal or external stimuli, via a mechanism that involves nervous system activity.
The internally coordinated responses (actions or inactions) of animals (individuals or groups) to internal or external stimuli, via a mechanism that involves nervous system activity.
The acquisition and processing of information and/or the storage and retrieval of this information over time.
Any process in an organism in which a relatively long-lasting adaptive behavioral change occurs as the result of experience.
The activities involved in the mental information processing system that receives (registers), modifies, stores, and retrieves informational stimuli. The main stages involved in the formation and retrieval of memory are encoding (processing of received information by acquisition), storage (building a permanent record of received information as a result of consolidation) and retrieval (calling back the stored information and use it in a suitable way to execute a given task).
The memory process that deals with the storage, retrieval and modification of information received a short time (up to about 30 minutes) ago. This type of memory is typically dependent on direct, transient effects of second messenger activation.
The memory process that results in the formation of consolidated memory resistant to disruption of the patterned activity of the brain, without requiring protein synthesis.
The memory process that deals with the storage, retrieval and modification of information a long time (typically weeks, months or years) after receiving that information. This type of memory is typically dependent on gene transcription regulated by second messenger activation.
The behavioral interactions between organisms for the purpose of mating, or sexual reproduction resulting in the formation of zygotes.
The pairwise union of individuals for the purpose of sexual reproduction, ultimately resulting in the formation of zygotes.
The behavioral interactions between organisms for the purpose of attracting sexual partners.
The act of sexual union between male and female, involving the transfer of sperm.
Any process that stops, prevents or reduces the receptiveness of a female to male advances.
Any process that stops, prevents or reduces the receptiveness of a female to male advances.
Any process that stops, prevents or reduces the receptiveness of a female to male advances.
Any process that stops, prevents or reduces the receptiveness of a female to male advances.
The specific behavior of an organism that recur with measured regularity.
The specific behavior of an organism that recur with measured regularity.
The specific behavior of an organism that recur with measured regularity.
Any biological process in an organism that recurs with a regularity of approximately 24 hours.
Any biological process in an organism that recurs with a regularity of approximately 24 hours.
Any biological process in an organism that recurs with a regularity of approximately 24 hours.
Any biological process in an organism that recurs with a regularity of approximately 24 hours.
The specific actions or reactions of an organism that recur with a regularity more frequent than every 24 hours.
The specific behavior of an organism relating to grooming, cleaning and brushing to remove dirt and parasites.
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
Behavior in a larval form of an organism, an immature organism that must undergo metamorphosis to assume adult characteristics.
Behavior in a larval form of an organism, an immature organism that must undergo metamorphosis to assume adult characteristics.
The behavior of an adult relating to the progression of that organism along the ground by the process of lifting and setting down each leg.
The response to external or internal stimuli that results in the locomotory process of flight. Flight is the self-propelled movement of an organism through the air.
The sudden, usually upward, movement off the ground or other surface through sudden muscular effort in the legs, following exposure to an external stimulus.
Behavior associated with the intake of food.
Behavior associated with the intake of food.
Behavior associated with the intake of food.
Behavior associated with the intake of food.
Behavior associated with the intake of food.
The behavior of an organism in response to a visual stimulus.
The behavior of an organism in response to a visual stimulus.
The behavior of an organism in response to a visual stimulus.
The actions or reactions of an individual in response to the orientation of a visual pattern. This is exemplified by some classes of insects which are able to detect and learn the orientation of a set of stripes and subsequently behaviorally discriminate between horizontal, vertical or 45 degree stripes.
The actions or reactions of an individual in response to the orientation of a visual pattern. This is exemplified by some classes of insects which are able to detect and learn the orientation of a set of stripes and subsequently behaviorally discriminate between horizontal, vertical or 45 degree stripes.
The behavior of an organism pertaining to movement of the eyes and of objects in the visual field, as in nystagmus.
Behavior that is dependent upon the sensation of chemicals.
Behavior that is dependent upon the sensation of chemicals.
Behavior that is dependent upon the sensation of chemicals.
The sudden, usually upward, movement off the ground or other surface through sudden muscular effort in the legs, following exposure to a chemical substance.
The sudden, usually upward, movement off the ground or other surface through sudden muscular effort in the legs, following exposure to a chemical substance.
The extension, through direct muscle actions, of the proboscis (the trunk-like extension of the mouthparts on the adult external head) in response to a sugar stimulus.
The extension, through direct muscle actions, of the proboscis (the trunk-like extension of the mouthparts on the adult external head) in response to a sugar stimulus.
Behavior that is dependent upon the sensation of a mechanical stimulus.
Behavior that is dependent upon the sensation of a mechanical stimulus.
Behavior that is dependent upon the sensation of a mechanical stimulus.
Any biological process involved in the maintenance of the steady-state number of cells within a population of cells in the meristem.
The function of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria.
The action of a molecule that contributes to the structural integrity of the chitin-based cuticle of a larva. An example of this is found in Drosophila melanogaster.
The action of a molecule that contributes to the structural integrity of the chitin-based cuticle of a pupa. An example of this is found in Drosophila melanogaster.
The action of a molecule that contributes to the structural integrity of the chitin-based cuticle of an adult organism. An example of this is found in Drosophila melanogaster.
Interacting selectively and non-covalently with the beta subunit of the catenin complex.
The attachment of one cell to another cell via adhesion molecules that require the presence of calcium for the interaction.
The flow of blood through the body of an animal, enabling the transport of nutrients to the tissues and the removal of waste products.
The flow of blood through the body of an animal, enabling the transport of nutrients to the tissues and the removal of waste products.
Any process that modulates the frequency, rate or extent of heart contraction. Heart contraction is the process in which the heart decreases in volume in a characteristic way to propel blood through the body.
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
Combining with a pathogen-associated molecular pattern (PAMP), a structure conserved among microbial species, or damage-associated molecular pattern (DAMP), an endogenous molecule released from damaged cells), and transmitting a signal to initiate a change in cell activity.
Combining with a pathogen-associated molecular pattern (PAMP), a structure conserved among microbial species, or damage-associated molecular pattern (DAMP), an endogenous molecule released from damaged cells), and transmitting a signal to initiate a change in cell activity.
Combining with incidental electromagnetic radiation, particularly visible light, and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with incidental electromagnetic radiation, particularly visible light, and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with incidental electromagnetic radiation, particularly visible light, and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with incidental electromagnetic radiation, particularly visible light, and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
Any protein complex that interacts with RNA polymerase II to increase (positive transcription elongation factor) or reduce (negative transcription elongation factor) the rate of transcription elongation.
A transcription elongation factor complex that facilitates the transition from abortive to productive elongation by phosphorylating the CTD domain of the large subunit of DNA-directed RNA polymerase II, holoenzyme. Contains a cyclin and a cyclin-dependent protein kinase catalytic subunit.
Interacting selectively and non-covalently with the peripheral benzodiazepine receptor (PBR).
Interacting selectively and non-covalently with the peripheral benzodiazepine receptor (PBR).
Any process that modulates the frequency, rate or extent of the regulated release of insulin.
Interacting selectively and non-covalently with diazepam, one of the most widely used benzodiazepine drugs. It is used as an anti-anxiety-hypnotic agent and has the proprietary name Valium.
Interacting selectively and non-covalently with diazepam, one of the most widely used benzodiazepine drugs. It is used as an anti-anxiety-hypnotic agent and has the proprietary name Valium.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor.
Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor.
Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor.
Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of acyl-CoA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of acyl-CoA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of acyl-CoA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of acyl-CoA.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
Enables the transfer of monocarboxylic acids from one side of a membrane to the other. A monocarboxylic acid is an organic acid with one COOH group.
Enables the transfer of monocarboxylic acids from one side of a membrane to the other. A monocarboxylic acid is an organic acid with one COOH group.
Enables the transfer of monocarboxylic acids from one side of a membrane to the other. A monocarboxylic acid is an organic acid with one COOH group.
Combining with a pentraxin and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with a neuronal pentraxin and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
The action characteristic of eclosion hormone, a peptide hormone that, upon receptor binding, triggers the death of certain muscles and neurons during insect metamorphosis.
The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
Interacting selectively and non-covalently with a lipopeptide, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds and containing a nonprotein group consisting of a lipid or lipids.
Interacting selectively and non-covalently with a lipopeptide, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds and containing a nonprotein group consisting of a lipid or lipids.
Interacting selectively and non-covalently with a lipoprotein particle. A lipoprotein particle, also known as a lipoprotein, is a clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids.
Interacting selectively and non-covalently with a lipoprotein particle. A lipoprotein particle, also known as a lipoprotein, is a clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids.
Interacting selectively and non-covalently with a lipoprotein particle. A lipoprotein particle, also known as a lipoprotein, is a clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids.
Interacting selectively and non-covalently with high-density lipoprotein particle, a lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE.
Combining with a diuretic hormone and transmitting the signal to initiate a change in cell activity.
The process in which a cell in an organism interprets its surroundings.
The process in which a neuronal cell in a multicellular organism interprets its surroundings.
The process in which a neuronal cell in a multicellular organism interprets signals produced by potential target cells, with which it may form synapses.
A ferritin complex located in the cell. Intracellular ferritin complexes contain 24 subunits, in a mixture of L (light) chains and H (heavy) chains.
Behavior in a fully developed and mature organism.
Behavior in a fully developed and mature organism.
Behavior in a fully developed and mature organism.
The process in which the migration of an axon growth cone of a motor neuron is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a motor neuron is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a motor neuron is directed to a specific target site in response to a combination of attractive and repulsive cues.
Combining with an extracellular messenger and transmitting the signal from one side of the membrane to the other to results in a change in cellular activity involved in axon guidance.
Binds to and increases the activity of an enzyme.
Binds to and increases the activity of an enzyme.
Binds to and increases the activity of guanylate cyclase in response to a change in calcium ion concentration.
The behavior of a male, for the purpose of attracting a sexual partner. An example of this process is found in Drosophila melanogaster.
The behavior of a male, for the purpose of attracting a sexual partner. An example of this process is found in Drosophila melanogaster.
The behavior of a female, for the purpose of attracting a sexual partner.
The process in which boundaries between a sensory organ and the surrounding tissue are established and maintained.
Merging of two or more mitochondria within a cell to form a single compartment.
The chemical reactions and pathways resulting in the formation of ocellus pigments, any general or particular coloring matter in living organisms, found or utilized in the ocellus, a minute simple eye found in many invertebrates.
The chemical reactions and pathways resulting in the formation of ocellus pigments, any general or particular coloring matter in living organisms, found or utilized in the ocellus, a minute simple eye found in many invertebrates.
The chemical reactions and pathways resulting in the formation of ocellus pigments, any general or particular coloring matter in living organisms, found or utilized in the ocellus, a minute simple eye found in many invertebrates.
The chemical reactions and pathways resulting in the formation of ocellus pigments, any general or particular coloring matter in living organisms, found or utilized in the ocellus, a minute simple eye found in many invertebrates.
The process whose specific outcome is the progression of the ocellus over time, from its formation to the mature structure. The ocellus is a simple visual organ of insects.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the eye.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the eye.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the eye.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the eye.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the eye.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the ocellus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of intracellular pigment storage granules in the ocellus.
Interacting selectively and non-covalently with chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
The timing of the emergence of the adult fly from its pupal case, which usually occurs at dawn.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Toll on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Toll on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Toll on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any process that modulates the frequency, rate or extent of the assembly or disassembly of actin filaments by the addition or removal of actin monomers from a filament.
The establishment of the barrier between the perineurium of peripheral nerves and the vascular endothelium of endoneurial capillaries. The perineurium acts as a diffusion barrier, but ion permeability at the blood-nerve barrier is still higher than at the blood-brain barrier.
Combining with glutamate and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Enables the transmembrane transfer of a chloride ion by a channel that opens when  glutamate is bound by the channel complex or one of its constituent parts on the extracellular side of the plasma membrane.
Polarization of the ovarian follicle cells along the dorsal/ventral axis. An example of this process is found in Drosophila melanogaster.
Polarization of the ovarian follicle cells along the dorsal/ventral axis. An example of this process is found in Drosophila melanogaster.
Polarization of the ovarian follicle cells along the dorsal/ventral axis. An example of this process is found in Drosophila melanogaster.
Polarization of the ovarian follicle cells along the dorsal/ventral axis. An example of this process is found in Drosophila melanogaster.
Polarization of the ovarian follicle cells along the dorsal-ventral axis by a gene product encoded by cells of the germ line.
Polarization of the ovarian follicle cells along the dorsal-ventral axis by a gene product encoded by cells of the germ line.
Polarization of the ovarian follicle cells along the dorsal-ventral axis by a gene product encoded by somatic cells. An example of this process is found in Drosophila melanogaster.
Polarization of the ovarian follicle cells along the dorsal-ventral axis by a gene product encoded by somatic cells. An example of this process is found in Drosophila melanogaster.
Polarization of the ovarian follicle cells along the dorsal-ventral axis by a gene product encoded by somatic cells. An example of this process is found in Drosophila melanogaster.
The stopping, prevention or reduction of the activity of the enzyme ornithine decarboxylase.
Complex that possesses guanylate cyclase activity and is not bound to a membrane.
A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential.
A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential.
A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential.
The orderly movement of mesodermal cells from one site to another.
Functions in the termination of translation.
Catalysis of the transfer of an acetyl group to a nitrogen atom on the acceptor molecule.
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
The function that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation.
Interacting selectively and non-covalently with an imaginal disc growth factor receptor.
Enables the transmembrane transfer of a calcium ion by a voltage-gated channel that is activated in response to light. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a voltage-gated channel that is activated in response to light. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
A protein complex that forms a transmembrane channel through which calcium ions may cross a cell membrane in response to changes in membrane potential generated in response to a light stimulus.
A protein complex that forms a transmembrane channel through which calcium ions may cross a cell membrane in response to changes in membrane potential generated in response to a light stimulus.
A protein complex that forms a transmembrane channel through which calcium ions may cross a cell membrane in response to changes in membrane potential generated in response to a light stimulus.
The directed movement of organelles or molecules along microtubules in neuron projections.
The directed movement of organelles or molecules along microtubules in neuron projections.
The directed movement of organelles or molecules along microtubules in neuron projections.
The directed movement of organelles or molecules along microtubules from the cell body toward the cell periphery in nerve cell axons.
The directed movement of organelles or molecules along microtubules from the cell periphery toward the cell body in nerve cell axons.
Membrane associated dimeric protein (240 and 220 kDa) of erythrocytes. Forms a complex with ankyrin, actin and probably other components of the membrane cytoskeleton, so that there is a mesh of proteins underlying the plasma membrane, potentially restricting the lateral mobility of integral proteins.
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
The binding activity of a molecule that brings together a cytoskeletal protein and one or more other molecules, permitting them to function in a coordinated way.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of single- or double-stranded DNA, and it drives another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of single- or double-stranded DNA, and it drives another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of single- or double-stranded DNA, and it drives another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of single- or double-stranded DNA, and it drives another reaction.
Catalysis of the hydrolysis of the epoxide in a juvenile hormone to the corresponding diol.
Interacting selectively and non-covalently with 5S ribosomal RNA, the smallest RNA constituent of a ribosome.
Interacting selectively and non-covalently with the unprocessed 5S ribosomal RNA transcript.
A series of molecular signals initiated by the binding of decapentaplegic (dpp) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of decapentaplegic (dpp) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of decapentaplegic (dpp) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of decapentaplegic (dpp) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of decapentaplegic (dpp) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Establishment and maintenance of a specific axis of polarity of the oocyte microtubule network. The axis is set so that the minus and plus ends of the microtubules of the mid stage oocyte are positioned along the anterior cortex and at the posterior pole, respectively. An example of this is found in Drosophila melanogaster.
Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+.
Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+.
Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+.
Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: GDP-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-R.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: alpha-D-galactose 1-phosphate + UDP-D-glucose = alpha-D-glucose 1-phosphate + UDP-D-galactose.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: 2-oxoglutarate + L-histidine = 3-(imidazol-5-yl)pyruvate + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + L-histidine = 3-(imidazol-5-yl)pyruvate + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + L-histidine = 3-(imidazol-5-yl)pyruvate + L-glutamate.
Catalysis of the reaction: (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + nicotinamide = 1-methylnicotinamide + S-adenosyl-L-homocysteine.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + nicotinamide = 1-methylnicotinamide + S-adenosyl-L-homocysteine.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reactions: peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin, and L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the S enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: 6-phospho-D-gluconate + NADP+ = 6-phospho-2-dehydro-D-gluconate + NADPH.
Catalysis of the reaction: H(2)O + O(2) + sarcosine = formaldehyde + glycine + H(2)O(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: prostaglandin H(2) = prostaglandin I(2).
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein.
Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein.
Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein.
Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein.
Catalysis of the reaction: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Catalysis of the reaction: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Catalysis of the reaction: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Catalysis of the reaction: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Catalysis of the reaction: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Catalysis of the reaction: UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.
Catalysis of the reaction: cholesterol + NADPH + H+ + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.
Catalysis of the reaction: cholesterol + NADPH + H+ + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.
Catalysis of the reaction: cholesterol + NADPH + H+ + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.
Catalysis of the reaction: cholesterol + NADPH + H+ + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.
Catalysis of the reaction: cholesterol + NADPH + H+ + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H(2)O.
Catalysis of the reaction: an acetic ester + H2O = an alcohol + acetate.
Catalysis of the reaction: an acetic ester + H2O = an alcohol + acetate.
Catalysis of the reaction: an acetic ester + H2O = an alcohol + acetate.
Catalysis of the reaction: an acetic ester + H2O = an alcohol + acetate.
Catalysis of the reaction: an acetic ester + H2O = an alcohol + acetate.
Catalysis of the reaction: an acetic ester + H2O = an alcohol + acetate.
Catalysis of the reaction: H(+) + O(2) + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO.
Catalysis of the reaction: H(+) + O(2) + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO.
Catalysis of the reaction: H(+) + O(2) + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO.
Catalysis of the reaction: a primary amine + H2O + O2 = an aldehyde + NH3 + hydrogen peroxide.
Catalysis of the reaction: a primary amine + H2O + O2 = an aldehyde + NH3 + hydrogen peroxide.
Catalysis of the reaction: a primary amine + H2O + O2 = an aldehyde + NH3 + hydrogen peroxide.
Catalysis of the reaction: a primary amine + H2O + O2 = an aldehyde + NH3 + hydrogen peroxide.
Catalysis of the reaction: a primary amine + H2O + O2 = an aldehyde + NH3 + hydrogen peroxide.
Functions during translation by interacting selectively and non-covalently with RNA during polypeptide synthesis at the ribosome.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reaction: NADH + H+ + ubiquinone = NAD+ + ubiquinol.
Catalysis of the reactions: protein serine + H2O = protein serine + phosphate; protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Interacting selectively and non-covalently with a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus.
Interacting selectively and non-covalently with a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus.
Interacting selectively and non-covalently with a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus.
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
Interacting selectively and non-covalently with oxysterol, an oxidized form of cholesterol.
Interacting selectively and non-covalently with a drug, any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease.
Interacting selectively and non-covalently with phenylalkylamine or any of its derivatives.
Catalysis of the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the hydroxyl group of an acceptor, producing the sulfated derivative and 3'-phosphoadenosine 5'-phosphate.
The action of a molecule that contributes to the structural integrity of bone.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
Catalysis of the reaction: L-glutamine + chorismate = 4-amino-4-deoxychorismate + L-glutamate. It is composed of two enzymatic activities (which may be present on one or two polypeptides); the first is a glutaminase which yields ammonia from glutamine, releasing glutamate. The ammonia is used by the second activity which catalyzes the amination of chorismate to form 4-amino-4-deoxychorismate.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
The chemical reactions and pathways resulting in the formation of para-aminobenzoic acid, an intermediate in the synthesis of folic acid, a compound which some organisms, e.g. prokaryotes, eukaryotic microbes, and plants, can synthesize de novo. Others, notably mammals, cannot. In yeast, it is present as a factor in the B complex of vitamins.
Assembly or disassembly of actin filaments by the addition or removal of actin monomers from a filament.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA replication.
Interacting selectively and non-covalently with the enzyme protein phosphatase 1.
Combining with a member of the hedgehog protein family and transmitting the signal across the membrane to initiate a change in cell activity.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Increases the activity of a phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a tyrosyl phenolic group of a protein.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a carbamate stimulus. Carbamates are a group of insecticides and parasiticides that act by inhibiting cholinesterase.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a carbamate stimulus. Carbamates are a group of insecticides and parasiticides that act by inhibiting cholinesterase.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cyclodiene stimulus. A cyclodiene is any organic insecticide (as dieldrin or chlordane) with a chlorinated methylene group forming a bridge across a 6-membered carbon ring.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cyclodiene stimulus. A cyclodiene is any organic insecticide (as dieldrin or chlordane) with a chlorinated methylene group forming a bridge across a 6-membered carbon ring.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a DDT stimulus. DDT, dichlorodiphenyltrichloroethane, is a chlorinated hydrocarbon pesticide moderately toxic to humans and other animals.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a DDT stimulus. DDT, dichlorodiphenyltrichloroethane, is a chlorinated hydrocarbon pesticide moderately toxic to humans and other animals.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organophosphorus stimulus. Organophosphorus is a compound containing phosphorus bound to an organic molecule; several organophosphorus compounds are used as insecticides, and they are highly toxic cholinesterase inhibitors.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organophosphorus stimulus. Organophosphorus is a compound containing phosphorus bound to an organic molecule; several organophosphorus compounds are used as insecticides, and they are highly toxic cholinesterase inhibitors.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pyrethroid stimulus. Pyrethroids are a group of growth regulators, analogous to insect juvenile hormones, that interfere with the development of insect larvae and are used in the control of insects that are harmful in the adult stage.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pyrethroid stimulus. Pyrethroids are a group of growth regulators, analogous to insect juvenile hormones, that interfere with the development of insect larvae and are used in the control of insects that are harmful in the adult stage.
Any process involved directly in viral genome replication, including viral nucleotide metabolism.
Any process involved directly in viral genome replication, including viral nucleotide metabolism.
Catalysis of the transfer of a methyl group to an acceptor molecule.
Catalysis of the transfer of a methyl group to an acceptor molecule.
Catalysis of the transfer of a methyl group to the carbon atom of an acceptor molecule.
Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.
Catalysis of the transfer of a methyl group to the oxygen atom of an acceptor molecule.
Catalysis of the transfer of a methyl group to the sulfur atom of an acceptor molecule.
Catalysis of the transfer of a methyl group from a donor to a nucleoside residue in an RNA molecule.
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a nucleoside residue in an mRNA molecule.
Catalysis of the transfer of a methyl group from a donor to a nucleoside residue in a tRNA molecule.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
Interacting selectively and non-covalently with the enzyme adenylate cyclase.
A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome.
A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome.
A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome.
Catalysis of the reaction: glycogen + phosphate = maltodextrin + alpha-D-glucose 1-phosphate.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of RNA, and it drives another reaction.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of RNA, and it drives another reaction.
Interacting selectively and non-covalently with any stretch of pyrimidines (cytosine or uracil) in an RNA molecule.
Combining with a neuropeptide to initiate a change in cell activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
Interacting selectively and non-covalently with eukaryotic initiation factor 4E, a polypeptide factor involved in the initiation of ribosome-mediated translation.
Stops, prevents or reduces the activity of metalloendopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain and contain a chelated metal ion at their active sites which is essential to their catalytic activity.
Stops, prevents or reduces the activity of metalloendopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain and contain a chelated metal ion at their active sites which is essential to their catalytic activity.
Catalysis of the posttranscriptional addition of a guanyl residue to the 5' end of an RNA molecule.
Catalysis of the posttranscriptional addition of a guanyl residue to the 5' end of a tRNA molecule; observed for His tRNAs.
Catalysis of the transfer of a glycosyl group from a UDP-sugar to a small hydrophobic molecule.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Receiving vitellogenin, and delivering vitellogenin into the cell via endocytosis.
Interacting selectively and non-covalently with ferrous iron, Fe(II).
Interacting selectively and non-covalently with ferric iron, Fe(III).
Stops, prevents, or reduces the activity of an ion channel.
Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways involving steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus.
The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues.
The chemical reactions and pathways involving ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds. It is the most important of the D provitamins and is converted to vitamin D2 on irradiation with UV light.
The chemical reactions and pathways involving ecdysone, (22R)-2-beta,3-beta,14,22,25-pentahydroxycholest-7-en-6-one, an ecdysteroid found in insects. It is the inactive prohormone of the moulting hormone ecdysterone and may have intrinsic hormonal activity at other stages of insect development.
The chemical reactions and pathways involving bile acids, any of a group of steroid carboxylic acids occurring in bile, where they are present as the sodium salts of their amides with glycine or taurine.
The chemical reactions and pathways involving C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the breakdown of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the breakdown of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways resulting in the breakdown of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
The chemical reactions and pathways involving androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics.
The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
The chemical reactions and pathways involving glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.
The chemical reactions and pathways involving glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.
The chemical reactions and pathways involving glucocorticoids, hormonal C21 corticosteroids synthesized from cholesterol. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.
The chemical reactions and pathways involving mineralocorticoids, hormonal C21 corticosteroids synthesized from cholesterol. Mineralocorticoids act primarily on water and electrolyte balance.
The addition of an alkyl group to a protein amino acid. An alkyl group is any group derived from an alkane by removal of one hydrogen atom.
The removal of an alkyl group from a protein amino acid. An alkyl group is any group derived from an alkane by removal of one hydrogen atom.
The chemical reactions and pathways involving spermine, a polybasic amine found in human sperm, in ribosomes and in some viruses, which is involved in nucleic acid packaging. Synthesis is regulated by ornithine decarboxylase which plays a key role in control of DNA replication.
The chemical reactions and pathways involving spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
The production of light by certain enzyme-catalyzed reactions in cells.
The rupture of cell membranes and the loss of cytoplasm.
The rupture of cell membranes and the loss of cytoplasm.
The rupture of cell membranes and the loss of cytoplasm.
The rupture of cell membranes and the loss of cytoplasm.
The rupture of cell membranes and the loss of cytoplasm.
The rupture of cell membranes and the loss of cytoplasm.
The rupture of cell membranes and the loss of cytoplasm.
A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues.
A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues.
Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
Combining with the biogenic amine tyramine to initiate a change in cell activity. Tyramine is a sympathomimetic amine derived from tyrosine with an action resembling that of epinephrine.
Combining with an extracellular amine and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an extracellular amine and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an extracellular amine and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
The process in which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody.
A heterodimeric complex containing the products of the insect genes Ecdysone receptor (EcR) and ultraspiracle (usp). Binding of ecdysone promotes association between the two subunits, and the receptor complex then initiates molting and metamorphosis by binding DNA and regulating the transcription of target genes.
A protein complex consisting of a heterodimer of Ecdysone receptor (EcR) and ultraspiracle (usp) plus an associated corepressor such as SMRTER, which represses transcription of target genes.
A protein complex consisting of a heterodimer of Ecdysone receptor (EcR) and ultraspiracle (usp) bound to the ligand ecdysone, which activates transcription of target genes.
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain, in a reaction that requires a free N-terminal amino group, C-terminal carboxyl group or both.
Catalysis of the removal of terminal peptide residues that are substituted, cyclized or linked by isopeptide bonds (peptide linkages other than those of alpha-carboxyl to alpha-amino groups).
A proton-transporting two-sector ATPase complex found in the lysosomal membrane, where it acts as a proton pump to mediate acidification of the lysosomal lumen.
A proton-transporting two-sector ATPase complex found in the lysosomal membrane, where it acts as a proton pump to mediate acidification of the lysosomal lumen.
An enzyme complex composed of two catalytic alpha subunits, which form a catalytic dimer, and a non-catalytic, regulatory beta subunit; the catalytic dimer may be an alpha1/alpha1 or alpha2/alpha2 homodimer, or an alpha1/alpha2 heterodimer. Modulates the action of platelet-activating factor (PAF).
An enzyme complex composed of two catalytic alpha subunits, which form a catalytic dimer, and a non-catalytic, regulatory beta subunit; the catalytic dimer may be an alpha1/alpha1 or alpha2/alpha2 homodimer, or an alpha1/alpha2 heterodimer. Modulates the action of platelet-activating factor (PAF).
The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.
The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.
A protein complex that is found in the endoplasmic reticulum membrane of eukaryotes and transfers lipid-linked oligosaccharide precursor to asparagine residues on nascent proteins. In yeast, the complex includes at least nine different subunits, whereas in mammalian cells at least three different forms of the complex have been detected.
A protein complex that is found in the endoplasmic reticulum membrane of eukaryotes and transfers lipid-linked oligosaccharide precursor to asparagine residues on nascent proteins. In yeast, the complex includes at least nine different subunits, whereas in mammalian cells at least three different forms of the complex have been detected.
Catalysis of the reaction: adenosine + H2O = inosine + NH3, in a tRNA molecule.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a nucleotide + H2O = a nucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
The action characteristic of ecdysis-triggering hormone, a peptide hormone that, upon receptor binding, initiates pre-ecdysis and ecdysis (i.e. cuticle shedding) through direct action on the central nervous system.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine.
Movement of the anterior ectoderm to the interior of the embryo.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
Combining with allatostatin to initiate a change in cell activity.
Catalysis of the removal of mismatched pyrimidine bases in DNA. Enzymes with this activity recognize and remove pyrimidines present in mismatches by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apyrimidinic (AP) site.
Catalysis of the sulfurylation of the desulfo form of molybdenum cofactor (MoCo), a cofactor required for the activity of some enzymes, such as aldehyde oxidase.
Catalysis of the sulfurylation of the desulfo form of molybdenum cofactor (MoCo), a cofactor required for the activity of some enzymes, such as aldehyde oxidase.
Catalysis of the sulfurylation of the desulfo form of molybdenum cofactor (MoCo), a cofactor required for the activity of some enzymes, such as aldehyde oxidase.
Interacting selectively and non-covalently with a sequence of uracil residues in an RNA molecule.
Interacting selectively and non-covalently with a polyglutamine tract, i.e. a series of consecutive glutamine residues, in a protein.
The binding activity of a molecule that brings together two molecules of the JAK signal transduction pathway, permitting them to function in a coordinated way.
Interacting selectively and non-covalently with zinc (Zn) ions.
Enables the secondary active transfer of sulfate from one side of a membrane to the other. Secondary active transport is the transfer of a solute across a membrane, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.
Enables the secondary active transfer of sulfate from one side of a membrane to the other. Secondary active transport is the transfer of a solute across a membrane, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.
Enables the secondary active transfer of sulfate from one side of a membrane to the other. Secondary active transport is the transfer of a solute across a membrane, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.
The directed movement of sulfate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of sulfate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Ca2+(in) + K+(in) + Na+(out) = Ca2+(out) + K+(out) + Na+(in).
A multiprotein complex composed of gamma-tubulin and other non-tubulin proteins that forms a flexible open ring structure thought to be the unit of nucleation at the minus end of a microtubule.
A complex usually comprising two gamma-tubulin molecules and two conserved non-tubulin proteins. Some gamma-tubulin small complexes are thought to be the repeating unit making up the core of the gamma-tubulin ring complex.
Catalysis of the transfer of a methyl group (CH3-) to a protein.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
Any process that modulates the frequency, rate or extent of G protein-coupled receptor signaling pathway.
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
A protein complex that is required for sister chromatid cohesion in eukaryotes. The cohesin complex forms a molecular ring complex, and is composed of structural maintenance of chromosomes (SMC) and kleisin proteins. For example, in yeast, the complex is composed of the SMC proteins Smc1p and Smc3p, and the kleisin protein Scc1p. In vertebrates, the complex is composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domains to a kleisin (RAD21, REC8 or RAD21L) which links them, and one STAG protein (STAG1, STAG2 or STAG3).
Combining with sulfonylurea, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity.
The multiplication or reproduction of cells, resulting in the expansion of a cell population.
Any process that activates or increases the rate or extent of cell proliferation.
Any process that activates or increases the rate or extent of cell proliferation.
Any process that activates or increases the rate or extent of cell proliferation.
Any process that activates or increases the rate or extent of cell proliferation.
Any process that activates or increases the rate or extent of cell proliferation.
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
The series of molecular signals generated as a consequence of the insulin receptor binding to insulin.
The series of molecular signals generated as a consequence of the insulin receptor binding to insulin.
A complex, normally consisting of a catalytic and a regulatory subunit, which catalyzes the removal of a phosphate group from a serine or threonine residue of a protein.
A heterodimer consisting of alpha and beta subunits that binds to and caps the barbed ends of actin filaments, thereby regulating the polymerization of actin monomers but not severing actin filaments.
The chemical reactions and pathways involving acetylcholine, the acetic acid ester of the organic base choline. Acetylcholine is a major neurotransmitter and neuromodulator both in the central and peripheral nervous systems. It also acts as a paracrine signal in various non-neural tissues.
The chemical reactions and pathways resulting in the formation of acetylcholine, the acetic acid ester of the organic base choline.
The chemical reactions and pathways resulting in the formation of acetylcholine, the acetic acid ester of the organic base choline.
The chemical reactions and pathways resulting in the formation of acetylcholine, the acetic acid ester of the organic base choline.
The chemical reactions and pathways resulting in the formation of acetylcholine, the acetic acid ester of the organic base choline.
A series of molecular signals initiated by the binding of an extracellular ligand to torso (a receptor tyrosine kinase) on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Catalysis of the reaction: ATP = 3',5'-cyclic AMP + diphosphate, stimulated by calcium-bound calmodulin.
Catalysis of the reaction: ATP = 3',5'-cyclic AMP + diphosphate, stimulated by calcium-bound calmodulin.
The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule.
Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a single-stranded DNA molecule.
Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a single-stranded DNA molecule.
Any process in which mRNA is transported to, or maintained in, a specific location within the cell.
Any process in which mRNA is transported to, or maintained in, a specific location within the cell.
Any process in which mRNA is transported to, or maintained in, a specific location within the cell.
Any process in which mRNA is transported to, or maintained in, a specific location within the cell.
Any process in which mRNA is transported to, or maintained in, a specific location within the cell.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the formation of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The chemical reactions and pathways resulting in the breakdown of any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.
The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.
Recruitment and organization of actin filaments in female germline ring canals.
Recruitment and organization of actin filaments in female germline ring canals.
Recruitment and organization of actin filaments in female germline ring canals.
A protein complex that is located in the cytosol and contains one or more cysteine-type endopeptidases (also called caspases), which give the complex a peptidase activity with specificity for the hydrolysis of aspartyl bonds. These complexes may be involved e.g. in apoptotic or inflammation processes.
The eukaryotic translation initiation factor 4F complex is composed of eIF4E, eIF4A and eIF4G; it is involved in the recognition of the mRNA cap, ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of the mRNA to the ribosome.
The eukaryotic translation initiation factor 4F complex is composed of eIF4E, eIF4A and eIF4G; it is involved in the recognition of the mRNA cap, ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of the mRNA to the ribosome.
Learning by associating a stimulus (the cause) with a particular outcome (the effect).
Learning by associating a stimulus (the cause) with a particular outcome (the effect).
Learning by associating a stimulus (the cause) with a particular outcome (the effect).
Learning by associating a stimulus (the cause) with a particular outcome (the effect).
The action of a molecule that contributes to the structural integrity of a muscle fiber.
Enables the transmembrane transfer of an anion by a voltage-gated channel. An anion is a negatively charged ion. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of an anion by a voltage-gated channel. An anion is a negatively charged ion. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of an anion by a voltage-gated channel. An anion is a negatively charged ion. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Catalysis of the sequential cleavage of mononucleotides from a free 5' or 3' terminus of a double-stranded DNA molecule.
Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule.
Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule.
Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a double-stranded DNA molecule.
Interacting selectively and non-covalently with 7S RNA, the RNA component of the signal recognition particle (SRP).
Combining with the ligand Gurken to initiate a change in cell activity.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to the ligand Gurken.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to the ligand Gurken.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to the ligand Gurken.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to the ligand Gurken.
The cell cycle process in which a cell progresses from meiotic G2 phase to M phase of meiosis I.
The cell cycle process in which a cell progresses from meiotic G2 phase to M phase of meiosis I.
The cell cycle process in which a cell progresses from meiotic G2 phase to M phase of meiosis I.
The action of a molecule that contributes to the structural integrity of the vitelline membrane of an egg. An example of this is found in Drosophila melanogaster.
Interacting selectively and non-covalently with the gurken growth factor receptor.
Catalysis of the covalent addition of an isoprenoid group such as a farnesyl or geranylgeranyl group via thioether linkages to a cysteine residue in a protein.
Enables the transfer of a protein from one side of a membrane to the other.
Enables the transfer of a protein from one side of a membrane to the other.
Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ral family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ral family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
Feeding behavior in a larval (immature) organism.
Enables the transfer of cation from one side of a membrane to the other.
Interacting selectively and non-covalently with a methylated cytosine/guanine dinucleotide.
A multimeric assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand-gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex.
Catalysis of the reactions: protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Enables the transmembrane transfer of a calcium ion by a high voltage-gated channel. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a high voltage-gated channel. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a high voltage-gated channel. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a high voltage-gated channel. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a high voltage-gated channel. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a high voltage-gated channel. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a low voltage-gated channel. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a low voltage-gated channel. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a calcium ion by a low voltage-gated channel. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
The directed movement of substances from endosomes to lysosomes.
The chemical reactions and pathways involving an mRNA encoding a histone.
The chemical reactions and pathways involving an mRNA encoding a histone.
Maintenance of the structural integrity of the ring canals connecting the female germline cyst.
Maintenance of the structural integrity of the ring canals connecting the female germline cyst.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
Catalysis of the reaction: 2-oxoglutarate + 4-(trimethylammonio)butanoate + O(2) = carnitine + CO(2) + succinate.
The control of viability and duration in the adult phase of the life-cycle.
Any process that results in a change in the behavior of an organism as a result of a cocaine stimulus.
Feeding behavior in a fully developed and mature organism.
Locomotory behavior in a fully developed and mature organism.
Locomotory behavior in a larval (immature) organism.
The behavior of a larval organism relating to the progression of that organism along the ground by the process of lifting and setting down each leg.
The orderly movement of a glial cell, non-neuronal cells that provide support and nutrition, maintain homeostasis, form myelin, and participate in signal transmission in the nervous system.
The orderly movement of a glial cell, non-neuronal cells that provide support and nutrition, maintain homeostasis, form myelin, and participate in signal transmission in the nervous system.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of an antimicrobial humoral response.
Catalysis of the phosphorylation of serine and threonine residues in a mitogen-activated protein kinase kinase kinase (MAPKKK), resulting in activation of MAPKKK. MAPKKK signaling pathways relay, amplify and integrate signals from the plasma membrane to the nucleus in response to a diverse range of extracellular stimuli.
Catalysis of the phosphorylation of serine and threonine residues in a mitogen-activated protein kinase kinase kinase (MAPKKK), resulting in activation of MAPKKK. MAPKKK signaling pathways relay, amplify and integrate signals from the plasma membrane to the nucleus in response to a diverse range of extracellular stimuli.
The process in which a microtubule is broken down into smaller segments. Severing enzymes remove dimers from the middle of the filament to create new ends, unlike depolymerizing kinesins that use ATP to uncap microtubules at their ends
A complex possessing an activity that couples ATP hydrolysis to the severing of microtubules; usually a heterodimer comprising a catalytic subunit (often 60kDa) and a regulatory subunit (often 80 kDa).
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats.
The orderly movement of a cell specialized to produce haploid gametes through the embryo from its site of production to the place where the gonads will form.
The orderly movement of a cell specialized to produce haploid gametes through the embryo from its site of production to the place where the gonads will form.
Any process in an organism in which a relatively long-lasting adaptive behavioral change occurs in response to (repeated) exposure to an olfactory cue.
The asymmetric division of cells to produce two daughter cells with different developmental potentials. It is of fundamental significance for the generation of cell diversity.
The asymmetric division of cells to produce two daughter cells with different developmental potentials. It is of fundamental significance for the generation of cell diversity.
The asymmetric division of cells to produce two daughter cells with different developmental potentials. It is of fundamental significance for the generation of cell diversity.
The specification of the anterior/posterior axis of the embryo by gradients of maternally-transcribed gene products; exemplified in insects by the morphogens, bicoid and nanos.
Any process that modulates the frequency, rate or extent of the process in which bicoid mRNA is transported to, or maintained in, a specific location.
Any process that modulates the surface configuration of a cell.
Any process that modulates the surface configuration of a cell.
Any process that modulates the size of a cell.
Synthesis, including the chemical reactions and pathways resulting in the formation of chitin and other components, and deposition of a chitin-based embryonic cuticle by the underlying epidermal epithelium. This tough, waterproof cuticle layer is essential to provide structural integrity of the larval body. An example of this is found in Drosophila melanogaster.
Synthesis, including the chemical reactions and pathways resulting in the formation of chitin and other components, and deposition of a chitin-based embryonic cuticle by the underlying epidermal epithelium. This tough, waterproof cuticle layer is essential to provide structural integrity of the larval body. An example of this is found in Drosophila melanogaster.
Synthesis, including the chemical reactions and pathways resulting in the formation of chitin and other components, and deposition of a chitin-based embryonic cuticle by the underlying epidermal epithelium. This tough, waterproof cuticle layer is essential to provide structural integrity of the larval body. An example of this is found in Drosophila melanogaster.
Synthesis, including the chemical reactions and pathways resulting in the formation of chitin and other components, and deposition of a chitin-based embryonic cuticle by the underlying epidermal epithelium. This tough, waterproof cuticle layer is essential to provide structural integrity of the larval body. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based larval cuticle. The insect larval cuticle is a secretion from epidermal cells that is shed at each molt. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based larval cuticle. The insect larval cuticle is a secretion from epidermal cells that is shed at each molt. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based larval cuticle. The insect larval cuticle is a secretion from epidermal cells that is shed at each molt. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based larval cuticle. The insect larval cuticle is a secretion from epidermal cells that is shed at each molt. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based pupal cuticle. At the end of the prepupal period the insect is covered by the pupal cuticle which continues to be elaborated into the pupal period. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based pupal cuticle. At the end of the prepupal period the insect is covered by the pupal cuticle which continues to be elaborated into the pupal period. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a chitin-based pupal cuticle. At the end of the prepupal period the insect is covered by the pupal cuticle which continues to be elaborated into the pupal period. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Synthesis and deposition of the chitin-based cuticle of adults following the apolysis of the pupal cuticle. The adult insect cuticle contains cuticullin, a protein epicuticle and a lamellate procuticle. An example of this process is adult chitin-based cuticle development in Drosophila melanogaster.
Any process in which the axon of a neuron is insulated, and that insulation maintained, thereby preventing dispersion of the electrical signal.
Any process in which the axon of a neuron is insulated, and that insulation maintained, thereby preventing dispersion of the electrical signal.
Any process in which the axon of a neuron is insulated, and that insulation maintained, thereby preventing dispersion of the electrical signal.
Any process in which the axon of a neuron is insulated, and that insulation maintained, thereby preventing dispersion of the electrical signal.
Catalysis of the transfer of sialic acid to an acceptor molecule, typically the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins.
Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an oligosaccharide.
The process in which the detection of light triggers the release of internally sequestered calcium ions.
The process in which the detection of light triggers the release of internally sequestered calcium ions.
The process in which the detection of light triggers the release of internally sequestered calcium ions.
Catalysis of the transfer of a galactosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
Catalysis of the reaction: thioredoxin + hydrogen peroxide = thioredoxin disulfide + H2O.
Catalysis of the reaction: thioredoxin + hydrogen peroxide = thioredoxin disulfide + H2O.
Catalysis of the reaction: thioredoxin + hydrogen peroxide = thioredoxin disulfide + H2O.
Catalysis of the reaction: thioredoxin + hydrogen peroxide = thioredoxin disulfide + H2O.
Enables the transmembrane transfer of an ion by a channel that opens in response to a mechanical stress.
Enables the transmembrane transfer of an ion by a channel that opens in response to a mechanical stress.
Enables the transmembrane transfer of an ion by a channel that opens in response to a mechanical stress.
Enables the transmembrane transfer of an ion by a channel that opens in response to a mechanical stress.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
A trimeric protein complex that phosphorylates inhibitory-kappaB (I-kappaB) proteins. The complex is composed of two kinase subunits (alpha and beta) and a regulatory gamma subunit (also called NEMO). In a resting state, NF-kappaB dimers are bound to inhibitory IKB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
A trimeric protein complex that phosphorylates inhibitory-kappaB (I-kappaB) proteins. The complex is composed of two kinase subunits (alpha and beta) and a regulatory gamma subunit (also called NEMO). In a resting state, NF-kappaB dimers are bound to inhibitory IKB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
A trimeric protein complex that phosphorylates inhibitory-kappaB (I-kappaB) proteins. The complex is composed of two kinase subunits (alpha and beta) and a regulatory gamma subunit (also called NEMO). In a resting state, NF-kappaB dimers are bound to inhibitory IKB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
Catalysis of the reaction: a steroid + donor-H2 + O2 = 7-alpha-hydroxysteroid + H2O.
Catalysis of the reaction: testosterone + donor-H2 + O2 = 15-alpha-hydroxytestosterone + H2O.
Catalysis of the reaction: coumarin + O2 + NADPH + H+ = hydroxycoumarin + H2O + NADP+.
Catalysis of the reaction: testosterone + donor-H2 + O2 = 16-alpha-hydroxytestosterone + H2O.
Catalysis of the reaction: testosterone + donor-H2 + O2 = 16-alpha-hydroxytestosterone + H2O.
Catalysis of the reaction: testosterone + donor-H2 + O2 = 16-alpha-hydroxytestosterone + H2O.
Catalysis of the reaction: testosterone + donor-H2 + O2 = 16-alpha-hydroxytestosterone + H2O.
Catalysis of the reaction: testosterone + donor-H2 + O2 = 16-alpha-hydroxytestosterone + H2O.
Catalysis of the incorporation of one atom from molecular oxygen into arachidonic acid and the reduction of the other atom of oxygen to water.
Catalysis of an NADPH- and oxygen-dependent reaction that converts arachidonic acid to a cis-epoxyeicosatrienoic acid.
Catalysis of an NADPH- and oxygen-dependent reaction that converts arachidonic acid to a cis-epoxyeicosatrienoic acid.
Catalysis of the formation of a hydroxyl group on a steroid by incorporation of oxygen from O2.
Catalysis of the formation of a hydroxyl group on a steroid by incorporation of oxygen from O2.
Catalysis of the formation of a hydroxyl group on a steroid by incorporation of oxygen from O2.
Catalysis of the reaction: an oxysterol + NADPH + O2 = 7-alpha-hydroxylated oxysterol + NADP+ + H2O.
Catalysis of the reaction: a steroid + donor-H2 + O2 = 12-alpha-hydroxysteroid + H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the reaction: obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 3 H2O.
Catalysis of the conversion of naphthalene to naphthalene 1,2-oxide.
Catalysis of the conversion of retinoic acid to 4-hydroxy-retinoic acid.
Catalysis of the hydroxylation of C-24 of 25-hydroxycholecalciferol (25-hydroxyvitamin D3) to form 24(R),25-dihydroxycholecalciferol.
Catalysis of the hydroxylation of C-24 of 25-hydroxycholecalciferol (25-hydroxyvitamin D3) to form 24(R),25-dihydroxycholecalciferol.
Catalysis of the hydroxylation of C-24 of 25-hydroxycholecalciferol (25-hydroxyvitamin D3) to form 24(R),25-dihydroxycholecalciferol.
Catalysis of an NADPH- and oxygen-dependent reaction that converts arachidonic acid to cis-14,15-epoxyeicosatrienoic acid.
Catalysis of an NADPH- and oxygen-dependent reaction that converts arachidonic acid to cis-14,15-epoxyeicosatrienoic acid.
Catalysis of an NADPH- and oxygen-dependent reaction that converts arachidonic acid to cis-11,12-epoxyeicosatrienoic acid.
The process whose specific outcome is the progression of the gonad over time, from its formation to the mature structure. The gonad is an animal organ that produces gametes; in some species it also produces hormones.
The process in which the anatomical structures of the chaeta are generated and organized. A chaeta is a sensory multicellular cuticular outgrowth of a specifically differentiated cell.
Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 5' end.
Catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor).
Catalysis of the transfer of a coenzyme A (CoA) group to 4-hydroxybutyrate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate = 8-oxo-7,8-dihydroguanosine phosphate + diphosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription.
Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate = 8-oxo-7,8-dihydroguanosine phosphate + diphosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription.
Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate = 8-oxo-7,8-dihydroguanosine phosphate + diphosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription.
Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate = 8-oxo-7,8-dihydroguanosine phosphate + diphosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription.
Catalysis of the transfer of a CDP-alcohol group from one compound to another.
Catalysis of the transfer of a fucosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
Catalysis of the reaction: protein-L-asparagine + H2O = protein-L-aspartate + NH3. This reaction is the deamidation of an N-terminal asparagine residue in a peptide or protein.
Catalysis of the hydrolysis of branched RNA structures that contain vicinal 2'-5'- and 3'-5'-phosphodiester bonds at a branch point nucleotide.
Catalysis of the reaction: phospho-(DNA-directed RNA polymerase II) + H2O = (DNA-directed RNA polymerase II) + phosphate.
Catalysis of the reaction: phospho-(DNA-directed RNA polymerase II) + H2O = (DNA-directed RNA polymerase II) + phosphate.
Catalysis of the reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a fatty acid anion + L-glutamate.
Catalysis of the reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a fatty acid anion + L-glutamate.
Catalysis of the reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a fatty acid anion + L-glutamate.
Catalysis of the reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a fatty acid anion + L-glutamate.
Catalysis of the reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a fatty acid anion + L-glutamate.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}-L-asparagine + GDP-L-fucose = N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine + GDP + H(+).
Catalysis of the reaction: 2-polyprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine = 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 2-polyprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine = 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 2-polyprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine = 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 2-polyprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine = 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 2-polyprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine = 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine.
Stops, prevents or reduces the activity of protein kinase C, an enzyme which phosphorylates a protein.
Stops, prevents or reduces the activity of protein kinase C, an enzyme which phosphorylates a protein.
Stops, prevents or reduces the activity of protein kinase C, an enzyme which phosphorylates a protein.
Stops, prevents or reduces the activity of protein kinase C, an enzyme which phosphorylates a protein.
Stops, prevents or reduces the activity of a calcium-dependent protein kinase.
Stops, prevents or reduces the activity of a ribonuclease, any enzyme that catalyzes the hydrolysis of phosphodiester bonds in chains of RNA.
Interacting selectively and non-covalently with phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine.
Interacting selectively and non-covalently with selenium (Se).
Interacting selectively and non-covalently with vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
Interacting selectively and non-covalently with vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
Interacting selectively and non-covalently with JUN kinase, an enzyme that catalyzes the phosphorylation and activation of members of the JUN family.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with calcitriol, the hormonally active form of vitamin D3, and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
The action characteristic of thyrotropin-releasing hormone (TRH), a hormone released by the mammalian hypothalamus into the hypophyseal-portal circulation in response to neural and/or chemical stimuli. Upon receptor binding, TRH increases the secretion of thyroid-stimulating hormone by the anterior pituitary.
The action characteristic of thyrotropin-releasing hormone (TRH), a hormone released by the mammalian hypothalamus into the hypophyseal-portal circulation in response to neural and/or chemical stimuli. Upon receptor binding, TRH increases the secretion of thyroid-stimulating hormone by the anterior pituitary.
Catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Catalysis of the reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Catalysis of the reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Catalysis of the reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Catalysis of the reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Catalysis of the reaction: adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Catalysis of the reaction: 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+.
Catalysis of the transfer of a phosphate group, usually from ATP, to a phosphofructose substrate molecule.
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + CDP-diacylglycerol = 3-(3-sn-phosphatidyl)-sn-glycerol 1-phosphate + CMP + H(+).
Catalysis of the reaction: D-aspartate + H2O + O2 = oxaloacetate + NH3 + hydrogen peroxide.
Catalysis of the reaction: D-aspartate + H2O + O2 = oxaloacetate + NH3 + hydrogen peroxide.
Catalysis of the reaction: D-aspartate + H2O + O2 = oxaloacetate + NH3 + hydrogen peroxide.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: GDP-alpha-D-mannose = GDP-4-dehydro-6-deoxy-alpha-D-mannose + H(2)O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: 2 L-ascorbate + O2 = 2 dehydroascorbate + 2 H2O.
Catalysis of the reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate.
Catalysis of the reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate.
Catalysis of the reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate.
Catalysis of the reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the hydrolysis of the 6-sulfate group of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + (N-acetyl-beta-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,4-(N-acetyl-D-glucosaminyl-1,2)-alpha-D-mannosyl-1,3-(beta-N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-beta-D-mannosyl-R.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide.
Catalysis of the reaction: (R)-carnitine + octanoyl-CoA = (S)-octanoylcarnitine + CoA.
Catalysis of the reaction: (R)-carnitine + octanoyl-CoA = (S)-octanoylcarnitine + CoA.
Catalysis of the reaction: (R)-carnitine + octanoyl-CoA = (S)-octanoylcarnitine + CoA.
Catalysis of the reaction: (R)-carnitine + octanoyl-CoA = (S)-octanoylcarnitine + CoA.
Catalysis of the reaction: (R)-carnitine + octanoyl-CoA = (S)-octanoylcarnitine + CoA.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
Catalysis of the reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O.
Catalysis of the reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O.
Catalysis of the reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O.
Catalysis of the reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O.
Catalysis of the reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O.
Catalysis of the reaction: dTDP-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H(2)O.
Catalysis of the reaction: N-formyl-L-methionine + H(2)O = L-methionine + formate.
Catalysis of the reaction: (R)-glycerate + NAD+ = hydroxypyruvate + NADH + H+.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: UDP-glucose + glycogenin = UDP + glucosylglycogenin.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate. The [heparan sulfate]-glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
Catalysis of the reaction: 3-methylbutanoyl-CoA + ETF = 3-methylbut-2-enoyl-CoA + reduced ETF.
Catalysis of the reaction: 3-methylbutanoyl-CoA + ETF = 3-methylbut-2-enoyl-CoA + reduced ETF.
Catalysis of the reaction: 3-methylbutanoyl-CoA + ETF = 3-methylbut-2-enoyl-CoA + reduced ETF.
Catalysis of the reaction: 3-methylbutanoyl-CoA + ETF = 3-methylbut-2-enoyl-CoA + reduced ETF.
Catalysis of an oxidation-reduction (redox) reaction in which a diphenol, or related compound, acts as a hydrogen or electron donor and reduces oxygen.
Catalysis of the reaction: L-ornithine = L-proline + NH(4)(+).
Catalysis of the reaction: L-ornithine = L-proline + NH(4)(+).
Catalysis of the reaction: L-ornithine = L-proline + NH(4)(+).
Catalysis of the reaction: L-ornithine = L-proline + NH(4)(+).
Catalysis of the reaction: L-ornithine = L-proline + NH(4)(+).
Catalysis of the reaction: palmitoyl-protein + H2O = palmitate + protein.
Catalysis of the reaction: palmitoyl-protein + H2O = palmitate + protein.
Catalysis of the reaction: palmitoyl-protein + H2O = palmitate + protein.
Catalysis of the reaction: palmitoyl-protein + H2O = palmitate + protein.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: tRNA guanine + queuine = tRNA queuine + guanine.
Catalysis of the reaction: sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein.
Catalysis of the reaction: sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein.
Catalysis of the reaction: sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein.
Catalysis of the reaction: sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein.
Catalysis of the reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate.
Catalysis of the reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate.
Catalysis of the reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate.
Catalysis of the reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate.
Catalysis of the reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate.
Catalysis of the reaction: ATP + sphinganine = ADP + sphinganine 1-phosphate.
Catalysis of the reaction: H(2)O + O(2) + sulfite = H(2)O(2) + H(+) + sulfate.
Catalysis of the reaction: H(2)O + O(2) + sulfite = H(2)O(2) + H(+) + sulfate.
Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
Catalysis of the reaction: RSO-R' + H2O = RSOOH + R'H. This reaction is the hydrolysis of any sulfuric ester bond, any ester formed from sulfuric acid, O=SO(OH)2.
Catalysis of the reaction: RSO-R' + H2O = RSOOH + R'H. This reaction is the hydrolysis of any sulfuric ester bond, any ester formed from sulfuric acid, O=SO(OH)2.
Catalysis of the reaction: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Catalysis of the reaction: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Catalysis of the reaction: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Catalysis of the reaction: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Catalysis of the reaction: peptidyl-glutamate + reduced vitamin K + CO2 + O2 = peptidyl-gamma-carboxyglutamate + vitamin K epoxide.
Catalysis of the reaction: UDP-D-galactose + a glucosylceramide = a lactosylceramide + uridine-5'-diphosphate. The glucosylceramide has sphinganine as the long chain base.
Catalysis of the reaction: UDP-D-galactose + a glucosylceramide = a lactosylceramide + uridine-5'-diphosphate. The glucosylceramide has sphinganine as the long chain base.
Catalysis of the reaction: UDP-D-galactose + a glucosylceramide = a lactosylceramide + uridine-5'-diphosphate. The glucosylceramide has sphinganine as the long chain base.
Enables the transfer of arsenite from one side of a membrane to the other, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.
Enables the transfer of arsenite from one side of a membrane to the other, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
The chemical reactions and pathways involving the nucleotide cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate).
Enables the transfer of tetracycline from one side of a membrane to the other. Tetracycline is a broad spectrum antibiotic that blocks binding of aminoacyl tRNA to the ribosomes of both Gram-positive and Gram-negative organisms (and those of organelles).
Enables the transfer of tetracycline from one side of a membrane to the other. Tetracycline is a broad spectrum antibiotic that blocks binding of aminoacyl tRNA to the ribosomes of both Gram-positive and Gram-negative organisms (and those of organelles).
Any of a group of soluble proteins functioning in the activation of ribosome-mediated translation of mRNA into a polypeptide.
Catalysis of the reaction: protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate.
Catalysis of the reaction: protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate.
Catalysis of the reaction: protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate.
Catalysis of the reaction: protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Catalysis of the random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
The movement of a population of phospholipid molecules from one leaflet of the plasma membrane bilayer to the opposite leaflet, resulting in loss of lipid asymmetry and surface exposure of phosphatidylserine (PS) and phosphatidylethanolamine (PE).
Catalysis of the reaction: UDP-galactose + N-acetylglucosamine = galactose-beta-1,3-N-acetylglucosamine + UDP.
Catalysis of the reaction: UDP-galactose + N-acetylglucosamine = galactose-beta-1,3-N-acetylglucosamine + UDP.
Catalysis of the reaction: UDP-galactose + N-acetylglucosamine = galactose-beta-1,3-N-acetylglucosamine + UDP.
Catalysis of the reaction: UDP-galactose + N-acetylglucosamine = galactose-beta-1,3-N-acetylglucosamine + UDP.
Interacting selectively and non-covalently with glycine, aminoethanoic acid.
Interacting selectively and non-covalently with glycine, aminoethanoic acid.
Interacting selectively and non-covalently with glycine, aminoethanoic acid.
Interacting selectively and non-covalently with glutamate, the anion of 2-aminopentanedioic acid.
Interacting selectively and non-covalently with thienylcyclohexylpiperidine.
Combining with melatonin, N-acetyl-5-methoxytryptamine, to initiate a change in cell activity. Melatonin is a neuroendocrine substance that stimulates the aggregation of melanosomes in melanophores, thus lightening the skin.
Combining with benzodiazepines, a class of drugs with hypnotic, anxiolytic, anticonvulsive, amnestic and myorelaxant properties, to initiate a change in cell activity.
Enables the transfer of monoamines, organic compounds that contain one amino group that is connected to an aromatic ring by an ethylene group (-CH2-CH2-), from one side of a membrane to the other.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: sucrose(out) + H+(out) = sucrose(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: sucrose(out) + H+(out) = sucrose(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: iodide(out) + Na+(out) = iodide(in) + Na+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: bile acid(out) + Na+(out) = bile acid(in) + Na+(in).
Enables the transfer of a negatively charged ion from one side of a membrane to the other.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Na+(out) + HCO3-(out) = Na+(in) + HCO3-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Na+(out) + HCO3-(out) = Na+(in) + HCO3-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Na+(out) + K+(out) + Cl-(out) = Na+(in) + K+(in) + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: sulfate(out) + H+(out) = sulfate(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: sulfate(out) + H+(out) = sulfate(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: sulfate(out) + H+(out) = sulfate(in) + H+(in).
Enables the transfer of organic cations from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Enables the transfer of organic cations from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Enables the transfer of organic cations from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Enables the transfer of organic anions from one side of a membrane to the other. Organic anions are atoms or small molecules with a negative charge which contain carbon in covalent linkage.
Enables the transfer of sucrose from one side of a membrane to the other. Sucrose is the disaccharide O-beta-D-fructofuranosyl-(2->1)-alpha-D-glucopyranoside, a sweet-tasting, non-reducing sugar isolated industrially from sugar beet or sugar cane.
Enables the transfer of sucrose from one side of a membrane to the other. Sucrose is the disaccharide O-beta-D-fructofuranosyl-(2->1)-alpha-D-glucopyranoside, a sweet-tasting, non-reducing sugar isolated industrially from sugar beet or sugar cane.
Enables the transfer of sucrose from one side of a membrane to the other. Sucrose is the disaccharide O-beta-D-fructofuranosyl-(2->1)-alpha-D-glucopyranoside, a sweet-tasting, non-reducing sugar isolated industrially from sugar beet or sugar cane.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: hexose(out) = hexose(in).
Enables the transfer of folic acid (pteroylglutamic acid) from one side of a membrane to the other. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
Enables the transfer of folic acid (pteroylglutamic acid) from one side of a membrane to the other. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
Enables the transfer of folic acid (pteroylglutamic acid) from one side of a membrane to the other. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
Enables the transfer of folic acid (pteroylglutamic acid) from one side of a membrane to the other. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
Enables the transfer of folic acid (pteroylglutamic acid) from one side of a membrane to the other. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Folate derivative (out) + anion (in) = folate derivative (in) + anion (out). The Reduced Folate Carrier (RCF(SLC19A1) acts by an antiport mechanism. RCF carries several folate derivatives: MTX, PMX, ratitrexed, pralatrexate, 5-methyl THF, and 5-formyl THF.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Folate derivative (out) + anion (in) = folate derivative (in) + anion (out). The Reduced Folate Carrier (RCF(SLC19A1) acts by an antiport mechanism. RCF carries several folate derivatives: MTX, PMX, ratitrexed, pralatrexate, 5-methyl THF, and 5-formyl THF.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Folate derivative (out) + anion (in) = folate derivative (in) + anion (out). The Reduced Folate Carrier (RCF(SLC19A1) acts by an antiport mechanism. RCF carries several folate derivatives: MTX, PMX, ratitrexed, pralatrexate, 5-methyl THF, and 5-formyl THF.
Enables the transfer of ammonium from one side of a membrane to the other. Ammonium is the cation NH4+ which is formed from N2 by root-nodule bacteria in leguminous plants and is an excretory product in ammonotelic animals.
Enables the transfer of ammonium from one side of a membrane to the other. Ammonium is the cation NH4+ which is formed from N2 by root-nodule bacteria in leguminous plants and is an excretory product in ammonotelic animals.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ascorbate(out) + Na+(out) = ascorbate(in) + Na+(in).
Enables the transfer of acetyl-CoA from one side of a membrane to the other. Acetyl-CoA is a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: multivitamin(out) + Na+(out) = multivitamin(in) + Na+(in). Multivitamins include pantothenate, biotin and lipoate.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: glucose 6-phosphate(out) + phosphate(in) = glucose 6-phosphate(in) + phosphate(out).
Enables the directed movement of phosphatidylcholine into, out of or within a cell, or between cells. Phosphatidylcholine refers to a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
Enables the directed movement of phosphatidylinositol into, out of or within a cell, or between cells. Phosphatidylinositol refers to any glycophospholipids with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
Combining with soluble compounds to initiate a change in cell activity. These receptors are responsible for the sense of taste.
Combining with a peptide and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with a peptide and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with a peptide and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with a peptide and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Catalysis of the reaction: ATP + riboflavin = ADP + FMN + 2 H(+).
Catalysis of the reaction: ATP + riboflavin = ADP + FMN + 2 H(+).
Catalysis of the reaction: ATP + riboflavin = ADP + FMN + 2 H(+).
Catalysis of the reaction: ATP + riboflavin = ADP + FMN + 2 H(+).
Catalysis of the reaction: ATP + riboflavin = ADP + FMN + 2 H(+).
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase), the terminal member of the respiratory chain of the mitochondrion and some aerobic bacteria. Cytochrome c oxidases are multi-subunit enzymes containing from 13 subunits in the mammalian mitochondrial form to 3-4 subunits in the bacterial forms.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase), the terminal member of the respiratory chain of the mitochondrion and some aerobic bacteria. Cytochrome c oxidases are multi-subunit enzymes containing from 13 subunits in the mammalian mitochondrial form to 3-4 subunits in the bacterial forms.
A multisubunit complex that activates the hydrolysis of small nonubiquitinated peptides by binding to the proteasome core complex.
Increases the activity of an endopeptidase, any enzyme that hydrolyzes nonterminal peptide bonds in polypeptides.
Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome.
The subcomplex of the proteasome regulatory particle that directly associates with the proteasome core complex.
The subcomplex of the proteasome regulatory particle that forms the peripheral lid, which is added on top of the base subcomplex.
Any process in an organism in which a change in behavior of an individual occurs in response to repeated exposure to a visual cue.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The process whose specific outcome is the progression of the epidermis over time, from its formation to the mature structure. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
Catalysis of the phosphorylation of tyrosine and threonine residues in a c-Jun NH2-terminal kinase (JNK), a member of a subgroup of mitogen-activated protein kinases (MAPKs), which signal in response to cytokines and exposure to environmental stress. JUN kinase kinase (JNKK) is a dual-specificity protein kinase kinase and requires activation by a serine/threonine kinase JUN kinase kinase kinase.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out).
Enables the transfer of cadmium (Cd) ions from one side of a membrane to the other.
Enables the transfer of cadmium (Cd) ions from one side of a membrane to the other.
Enables the transfer of cobalt (Co) ions from one side of a membrane to the other.
Enables the transfer of cobalt (Co) ions from one side of a membrane to the other.
Enables the transfer of lead (Pb) ions from one side of a membrane to the other.
Enables the transfer of nickel (Ni) cations from one side of a membrane to the other.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of ions across a membrane. The reaction is characterized by the transient formation of a high-energy aspartyl-phosphoryl-enzyme intermediate.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of ions across a membrane. The reaction is characterized by the transient formation of a high-energy aspartyl-phosphoryl-enzyme intermediate.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) -> ADP + phosphate + Na+(out); by a phosphorylative mechanism.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cl-(out) = ADP + phosphate + Cl-(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + guanine(out) = ADP + phosphate + guanine(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + guanine(out) = ADP + phosphate + guanine(in).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Catalysis of the reaction: ATP + H2O + xenobiotic(in) = ADP + phosphate + xenobiotic(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + protein+(in) -> ADP + phosphate + protein+(out); drives the concomitant secretion of proteins.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + protein+(in) -> ADP + phosphate + protein+(out); drives the concomitant secretion of proteins.
Enables the directed movement of proteins into, out of or within a cell, or between cells.
Enables the directed movement of proteins into, out of or within a cell, or between cells.
Enables the directed movement of proteins into, out of or within a cell, or between cells.
Enables the directed movement of proteins into, out of or within a cell, or between cells.
Enables the directed movement of proteins into, out of or within a cell, or between cells.
Enables the directed movement of proteins into, out of or within a cell, or between cells.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O = ADP + phosphate; drives the transport of proteins into the mitochondrion via the mitochondrial inner membrane translocase complex.
Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the severing of a microtubule at a specific spot along its length, coupled to the hydrolysis of ATP.
Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the severing of a microtubule at a specific spot along its length, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the minus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the minus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the minus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the minus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the minus end, coupled to the hydrolysis of ATP.
Movement of organelles or other particles along actin filaments, or sliding of actin filaments past each other, mediated by motor proteins.
Catalysis of movement along a microtubule toward the plus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the plus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the plus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the plus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the plus end, coupled to the hydrolysis of ATP.
Catalysis of movement along a microtubule toward the plus end, coupled to the hydrolysis of ATP.
The membrane organization process that joins two lipid bilayers to form a single membrane.
The membrane organization process that joins two lipid bilayers to form a single membrane.
The membrane organization process that joins two lipid bilayers to form a single membrane.
The membrane organization process that joins two lipid bilayers to form a single membrane.
Catalysis of the reaction: JUN kinase serine/threonine/tyrosine phosphate + H2O = JUN kinase serine/threonine/tyrosine + phosphate.
Any process that modulates the frequency, rate or extent of synaptic growth at neuromuscular junctions.
The process in which an undifferentiated cell acquires the features of a mystery cell. The mystery cells are a precluster of cells that emerge from the compound eye morphogenetic furrow, normally positioned between R3 and R4. They then disappear into the surrounding pool of undifferentiated cells and have no known fate in the mature ommatidium. An example of this process is found in Drosophila melanogaster.
The process whose specific outcome is the progression of the male gonad over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the male gonad over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the female gonad over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the female gonad over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the female gonad over time, from its formation to the mature structure.
The process in which anatomical structures of the veins on an imaginal disc-derived wing are generated and organized.
The process in which the anatomical structures of the imaginal disc-derived wing margin are generated and organized. The wing margin is a strip of cells in the third instar disc at the boundary between the presumptive dorsal and ventral surfaces of the wing blade.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of smoothened signaling.
Any process that modulates the frequency, rate or extent of the series of molecular signals initiated by binding of a Wnt protein to a receptor on the surface of the target cell where activated receptors leads to an increase in intracellular calcium and activation of protein kinase C (PKC).
Any process that modulates the frequency, rate or extent of the series of molecular signals initiated by binding of a Wnt protein to a receptor on the surface of the target cell where activated receptors leads to an increase in intracellular calcium and activation of protein kinase C (PKC).
Any process that modulates the frequency, rate or extent of the series of molecular signals initiated by binding of a Wnt protein to a receptor on the surface of the target cell where activated receptors leads to an increase in intracellular calcium and activation of protein kinase C (PKC).
Any process that modulates the frequency, rate or extent of the series of molecular signals initiated by binding of a Wnt protein to a receptor on the surface of the target cell where activated receptors leads to an increase in intracellular calcium and activation of protein kinase C (PKC).
Any process that modulates the frequency, rate or extent of the Tl signaling pathway.
Any process that modulates the frequency, rate or extent of the Tl signaling pathway.
Any process that modulates the frequency, rate or extent of the Tl signaling pathway.
Any process that modulates the frequency, rate or extent of the Notch signaling pathway.
Any process that modulates the frequency, rate or extent of the Notch signaling pathway.
Any process that modulates the frequency, rate or extent of the Notch signaling pathway.
The process in which the structures of a photoreceptor cell are generated and organized. This process occurs while the initially relatively unspecialized cell is acquiring the specialized features of a photoreceptor cell, a sensory cell that reacts to the presence of light. An example of this is found in Drosophila melanogaster.
The specification of the anterior/posterior axis of the embryo by the products of genes expressed maternally and genes expressed in the zygote.
Modulation of the activity of the enzyme calcium-dependent protein serine/threonine phosphatase.
Modulation of the activity of the enzyme cAMP-dependent protein kinase.
Modulation of the activity of the enzyme cAMP-dependent protein kinase.
Modulation of the activity of the enzyme cAMP-dependent protein kinase.
Modulation of the activity of the enzyme cAMP-dependent protein kinase.
Modulation of the activity of the enzyme cAMP-dependent protein kinase.
Modulates the activity of a protein kinase, an enzyme which phosphorylates a protein.
Modulation of the activity of the enzyme phosphorylase kinase.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
The process in which spindle microtubules become physically associated with the proteins making up the kinetochore complex.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion.
The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.
The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.
The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.
The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.