Journal article Open Access
Kummer, Markus P; Heneka, Michael T
<?xml version='1.0' encoding='UTF-8'?> <record xmlns="http://www.loc.gov/MARC21/slim"> <leader>00000nam##2200000uu#4500</leader> <controlfield tag="005">20200120154902.0</controlfield> <controlfield tag="001">16477</controlfield> <datafield tag="700" ind1=" " ind2=" "> <subfield code="u">Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany and German Center for Neurodegenerative Diseases (DZNE), Holbeinstrasse 15, 53117 Bonn, Germany.</subfield> <subfield code="a">Heneka, Michael T</subfield> </datafield> <datafield tag="856" ind1="4" ind2=" "> <subfield code="s">862178</subfield> <subfield code="z">md5:c9569da59a12f3f373b47fc746ea102b</subfield> <subfield code="u">https://zenodo.org/record/16477/files/Kummer_AlzResTher_2014-P21.pdf</subfield> </datafield> <datafield tag="542" ind1=" " ind2=" "> <subfield code="l">open</subfield> </datafield> <datafield tag="260" ind1=" " ind2=" "> <subfield code="c">2014-05-26</subfield> </datafield> <datafield tag="909" ind1="C" ind2="O"> <subfield code="p">openaire</subfield> <subfield code="p">user-ecfunded</subfield> <subfield code="p">user-inmind</subfield> <subfield code="o">oai:zenodo.org:16477</subfield> </datafield> <datafield tag="909" ind1="C" ind2="4"> <subfield code="c">28</subfield> <subfield code="n">3</subfield> <subfield code="p">Alzheimers Res Ther. </subfield> <subfield code="v">6</subfield> <subfield code="y">2014</subfield> </datafield> <datafield tag="100" ind1=" " ind2=" "> <subfield code="u">Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany</subfield> <subfield code="a">Kummer, Markus P</subfield> </datafield> <datafield tag="245" ind1=" " ind2=" "> <subfield code="a">Truncated and modified amyloid-beta species</subfield> </datafield> <datafield tag="980" ind1=" " ind2=" "> <subfield code="a">user-inmind</subfield> </datafield> <datafield tag="980" ind1=" " ind2=" "> <subfield code="a">user-ecfunded</subfield> </datafield> <datafield tag="536" ind1=" " ind2=" "> <subfield code="c">278850</subfield> <subfield code="a">Imaging of Neuroinflammation in Neurodegenerative Diseases</subfield> </datafield> <datafield tag="540" ind1=" " ind2=" "> <subfield code="u">https://creativecommons.org/licenses/by/4.0/legalcode</subfield> <subfield code="a">Creative Commons Attribution 4.0 International</subfield> </datafield> <datafield tag="650" ind1="1" ind2="7"> <subfield code="a">cc-by</subfield> <subfield code="2">opendefinition.org</subfield> </datafield> <datafield tag="520" ind1=" " ind2=" "> <subfield code="a"><p>Alzheimer&rsquo; s disease pathology is closely connected to the processing of the amyloid precursor protein (APP)&nbsp;resulting in the formation of a variety of amyloid-beta (A&beta; ) peptides. They are found as insoluble aggregates in&nbsp;senile plaques, the histopathological hallmark of the disease. These peptides are also found in soluble, mostly&nbsp;monomeric and dimeric, forms in the interstitial and cerebrospinal fluid. Due to the combination of several&nbsp;enzymatic activities during APP processing, A&beta;&nbsp; peptides exist in multiple isoforms possessing different N-termini&nbsp;and C-termini. These peptides include, to a certain extent, part of the juxtamembrane and transmembrane domain&nbsp;of APP. Besides differences in size, post-translational modifications of A&beta; &ndash;&nbsp; including oxidation, phosphorylation,&nbsp;nitration, racemization, isomerization, pyroglutamylation, and glycosylation &ndash;&nbsp; generate a plethora of peptides with&nbsp;different physiological and pathological properties that may modulate disease progression.</p></subfield> </datafield> <datafield tag="024" ind1=" " ind2=" "> <subfield code="a">10.1186/alzrt258</subfield> <subfield code="2">doi</subfield> </datafield> <datafield tag="980" ind1=" " ind2=" "> <subfield code="a">publication</subfield> <subfield code="b">article</subfield> </datafield> </record>
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