Amyloid-? annular protofibrils evade fibrillar fate in Alzheimer disease brain.
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ABSTRACT:
SUBMITTER: Lasagna-Reeves CA
PROVIDER: S-EPMC3121356 | biostudies-literature | 2011 Jun
REPOSITORIES: biostudies-literature
Publications
Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain.
Lasagna-Reeves Cristian A CA Glabe Charles G CG Kayed Rakez R
The Journal of biological chemistry 20110420 25
Annular protofibrils (APFs) represent a new and distinct class of amyloid structures formed by disease-associated proteins. In vitro, these pore-like structures have been implicated in membrane permeabilization and ion homeostasis via pore formation. Still, evidence for their formation and relevance in vivo is lacking. Herein, we report that APFs are in a distinct pathway from fibril formation in vitro and in vivo. In human Alzheimer disease brain samples, amyloid-β APFs were associated with dif ...[more]
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