期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 36, 期 6, 页码 338-345出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2011.02.002
关键词
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资金
- DFG [SFB 610]
- Alzheimer Forschungs-Initiative
- Exzellenznetzwerk Biowissenschaften (Sachsen-Anhalt)
- NIH [P01 GM-62580]
The formation of amyloid fibrils, protofibrils and oligomers from the beta-amyloid (A beta) peptide represents a hallmark of Alzheimer's disease. A beta-peptide-derived assemblies might be crucial for disease onset, but determining their atomic structures has proven to be a major challenge. Progress over the past 5 years has yielded substantial new data obtained with improved methodologies including electron cryo-microscopy and NMR. It is now possible to resolve the global fibril topology and the cross-beta sheet organization within protofilaments, and to identify residues that are crucial for stabilizing secondary structural elements and peptide conformations within specific assemblies. These data have significantly enhanced our understanding of the mechanism of A beta aggregation and have illuminated the possible relevance of specific conformers for neurodegenerative pathologies.
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