Recent progress in understanding Alzheimer’s β-amyloid structures.

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Trends in Biochemical Sciences. 2011 Jun;36(6):338-45. doi: 10.1016/j.tibs.2011.02.002

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Recent progress in understanding Alzheimer’s β-amyloid structures. Grigorieff Lab

Fändrich M, Schmidt M, Grigorieff N

Note: Research in this publication was not performed at Janelia.

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Abstract

The formation of amyloid fibrils, protofibrils and oligomers from the β-amyloid (Aβ) peptide represents a hallmark of Alzheimer’s disease. Aβ-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-β 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 Aβ aggregation and have illuminated the possible relevance of specific conformers for neurodegenerative pathologies.

PMID: 21411326 [PubMed - indexed for MEDLINE]

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Recent progress in understanding Alzheimer’s β-amyloid structures.

Note: Research in this publication was not performed at Janelia.

Abstract

PMID: 21411326 [PubMed - indexed for MEDLINE]

Janelia Authors