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Recent progress in understanding Alzheimer s beta-amyloid structures Fandrich M; Schmidt M; Grigorieff NTrends Biochem Sci 2011[Jun]; 36 (6): 338-45The formation of amyloid fibrils, protofibrils and oligomers from the beta-amyloid (Abeta) peptide represents a hallmark of Alzheimer's disease. Abeta-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 Abeta aggregation and have illuminated the possible relevance of specific conformers for neurodegenerative pathologies.|Alzheimer Disease/*metabolism/pathology[MESH]|Amyloid beta-Peptides/*chemistry/metabolism[MESH]|Amyloid/chemistry/metabolism[MESH]|Animals[MESH]|Humans[MESH]|Protein Conformation[MESH] |
