Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach - PubMed (original) (raw)
Review
doi: 10.1021/ar050063s.
Noel D Lazo, Gal Bitan, Summer Bernstein, Thomas Wyttenbach, Michael T Bowers, Andrij Baumketner, Joan-Emma Shea, Brigita Urbanc, Luis Cruz, Jose Borreguero, H Eugene Stanley
Affiliations
- PMID: 16981680
- DOI: 10.1021/ar050063s
Free article
Review
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach
David B Teplow et al. Acc Chem Res. 2006 Sep.
Free article
Abstract
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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- AG023661/AG/NIA NIH HHS/United States
- AG027818/AG/NIA NIH HHS/United States
- AG18921/AG/NIA NIH HHS/United States
- NS38328/NS/NINDS NIH HHS/United States
- NS44147/NS/NINDS NIH HHS/United States