Journal article Open Access

Truncated and modified amyloid-beta species

Kummer, Markus P; Heneka, Michael T

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    <subfield code="u">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.</subfield>
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    <subfield code="p">Alzheimers Res Ther. </subfield>
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    <subfield code="u">Department of Neurology, University Hospital Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany</subfield>
    <subfield code="a">Kummer, Markus P</subfield>
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    <subfield code="a">Truncated and modified amyloid-beta species</subfield>
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    <subfield code="a">Imaging of Neuroinflammation in Neurodegenerative Diseases</subfield>
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    <subfield code="a">&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;</subfield>
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