Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
Published 2011 View Full Article
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Title
Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
Authors
Keywords
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Journal
Nature Chemical Biology
Volume 7, Issue 9, Pages 602-609
Publisher
Springer Nature
Online
2011-08-01
DOI
10.1038/nchembio.624
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Note: Only part of the references are listed.- The Japanese Mutant Aβ (ΔE22-Aβ1−39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ1−40into Atypical Fibrils by ΔE22-Aβ1−39
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- Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
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- Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
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- Structure-neurotoxicity relationships of amyloid -protein oligomers
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- A new amyloid β variant favoring oligomerization in Alzheimer's-type dementia
- (2008) Takami Tomiyama et al. ANNALS OF NEUROLOGY
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- (2008) Beena Krishnan et al. CHEMISTRY & BIOLOGY
- Amyloid β-Protein Assembly and Alzheimer Disease
- (2008) Robin Roychaudhuri et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
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- Formation of Toxic Oligomeric α-Synuclein Species in Living Cells
- (2008) Tiago Fleming Outeiro et al. PLoS One
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