Journal article Open Access

Truncated and modified amyloid-beta species

Kummer, Markus P; Heneka, Michael T


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{
  "DOI": "10.1186/alzrt258", 
  "container_title": "Alzheimers Res Ther. ", 
  "title": "Truncated and modified amyloid-beta species", 
  "issued": {
    "date-parts": [
      [
        2014, 
        5, 
        26
      ]
    ]
  }, 
  "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>", 
  "author": [
    {
      "given": "Markus P", 
      "family": "Kummer"
    }, 
    {
      "given": "Michael T", 
      "family": "Heneka"
    }
  ], 
  "page": "28", 
  "volume": "6", 
  "type": "article-journal", 
  "issue": "3", 
  "id": "16477"
}
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