Journal article Open Access

Truncated and modified amyloid-beta species

Kummer, Markus P; Heneka, Michael T

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  "description": "<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>", 
  "license": "", 
  "creator": [
      "affiliation": "Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany", 
      "@type": "Person", 
      "name": "Kummer, Markus P"
      "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.", 
      "@type": "Person", 
      "name": "Heneka, Michael T"
  "headline": "Truncated and modified amyloid-beta species", 
  "image": "", 
  "datePublished": "2014-05-26", 
  "url": "", 
  "@context": "", 
  "identifier": "", 
  "@id": "", 
  "@type": "ScholarlyArticle", 
  "name": "Truncated and modified amyloid-beta species"
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