May 26, 2014 Journal article Open Access

Kummer, Markus P; Heneka, Michael T

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  <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>
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  <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">&lt;p&gt;Alzheimer&amp;rsquo; s disease pathology is closely connected to the processing of the amyloid precursor protein (APP)&amp;nbsp;resulting in the formation of a variety of amyloid-beta (A&amp;beta; ) peptides. They are found as insoluble aggregates in&amp;nbsp;senile plaques, the histopathological hallmark of the disease. These peptides are also found in soluble, mostly&amp;nbsp;monomeric and dimeric, forms in the interstitial and cerebrospinal fluid. Due to the combination of several&amp;nbsp;enzymatic activities during APP processing, A&amp;beta;&amp;nbsp; peptides exist in multiple isoforms possessing different N-termini&amp;nbsp;and C-termini. These peptides include, to a certain extent, part of the juxtamembrane and transmembrane domain&amp;nbsp;of APP. Besides differences in size, post-translational modifications of A&amp;beta; &amp;ndash;&amp;nbsp; including oxidation, phosphorylation,&amp;nbsp;nitration, racemization, isomerization, pyroglutamylation, and glycosylation &amp;ndash;&amp;nbsp; generate a plethora of peptides with&amp;nbsp;different physiological and pathological properties that may modulate disease progression.&lt;/p&gt;</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>
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