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Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach
Journal article   Open access   Peer reviewed

Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach

David B Teplow, Noel D Lazo, Gal Bitan, Summer Bernstein, Thomas Wyttenbach, Michael T Bowers, Andrij Baumketner, Joan-Emma Shea, Brigita Urbanc, Luis Cruz, …
Accounts of chemical research, v 39(9), pp 635-645
Sep 2006
PMID: 16981680
url
https://escholarship.org/uc/item/8207498cView

Abstract

Amino Acid Sequence Thermodynamics Models, Molecular Molecular Sequence Data Protein Conformation Amyloid beta-Peptides - chemistry Protein Folding
Oligomeric, neurotoxic amyloid protein assemblies are thought to be causative agents in Alzheimer's and other neurodegenerative diseases. Development of oligomer-specific therapeutic agents requires a mechanistic understanding of the oligomerization process. This is a daunting task because amyloidogenic protein oligomers often are metastable and comprise structurally heterogeneous populations in equilibrium with monomers and fibrils. A single methodological approach cannot elucidate the entire protein assembly process. An integrated multidisciplinary program is required. We discuss here the synergistic application of in hydro, in vacuo, and in silico methods to the study of the amyloid beta-protein, the key pathogenetic agent in Alzheimer's disease.

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Collaboration types
Domestic collaboration
Web of Science research areas
Chemistry, Multidisciplinary
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