Journal article Open Access
Kummer, Markus P; Heneka, Michael T
<?xml version='1.0' encoding='utf-8'?> <resource xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns="http://datacite.org/schema/kernel-4" xsi:schemaLocation="http://datacite.org/schema/kernel-4 http://schema.datacite.org/meta/kernel-4.1/metadata.xsd"> <identifier identifierType="URL">https://zenodo.org/record/16477</identifier> <creators> <creator> <creatorName>Kummer, Markus P</creatorName> <givenName>Markus P</givenName> <familyName>Kummer</familyName> <affiliation>Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany</affiliation> </creator> <creator> <creatorName>Heneka, Michael T</creatorName> <givenName>Michael T</givenName> <familyName>Heneka</familyName> <affiliation>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.</affiliation> </creator> </creators> <titles> <title>Truncated and modified amyloid-beta species</title> </titles> <publisher>Zenodo</publisher> <publicationYear>2014</publicationYear> <dates> <date dateType="Issued">2014-05-26</date> </dates> <resourceType resourceTypeGeneral="Text">Journal article</resourceType> <alternateIdentifiers> <alternateIdentifier alternateIdentifierType="url">https://zenodo.org/record/16477</alternateIdentifier> </alternateIdentifiers> <relatedIdentifiers> <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1186/alzrt258</relatedIdentifier> <relatedIdentifier relatedIdentifierType="URL" relationType="IsPartOf">https://zenodo.org/communities/inmind</relatedIdentifier> <relatedIdentifier relatedIdentifierType="URL" relationType="IsPartOf">https://zenodo.org/communities/ecfunded</relatedIdentifier> </relatedIdentifiers> <rightsList> <rights rightsURI="https://creativecommons.org/licenses/by/4.0/legalcode">Creative Commons Attribution 4.0 International</rights> <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights> </rightsList> <descriptions> <description descriptionType="Abstract"><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></description> </descriptions> <fundingReferences> <fundingReference> <funderName>European Commission</funderName> <funderIdentifier funderIdentifierType="Crossref Funder ID">10.13039/501100000780</funderIdentifier> <awardNumber awardURI="info:eu-repo/grantAgreement/EC/FP7/278850/">278850</awardNumber> <awardTitle>Imaging of Neuroinflammation in Neurodegenerative Diseases</awardTitle> </fundingReference> </fundingReferences> </resource>
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