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>", 
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    "title": "Truncated and modified amyloid-beta species", 
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      "volume": "6", 
      "year": "2014", 
      "issue": "3", 
      "pages": "28", 
      "title": "Alzheimers Res Ther. "
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    "publication_date": "2014-05-26", 
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        "affiliation": "Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany", 
        "name": "Kummer, Markus P"
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        "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.", 
        "name": "Heneka, Michael T"
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