4.8 Article

Multistep Conformation Selection in Amyloid Assembly

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 47, Pages 17007-17010

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b09362

Keywords

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Funding

  1. McDonnell Foundation (21st Century Science Initiative Grant on Studying Complex Systems) [220020271]
  2. NSF [CHE-1507932, NSF/DMR-BSF 1610377]
  3. NIH Alzheimer's Disease Research Center [P50AG025688]
  4. Direct For Mathematical & Physical Scien
  5. Division Of Chemistry [1507932] Funding Source: National Science Foundation
  6. Direct For Mathematical & Physical Scien
  7. Division Of Materials Research [1610377] Funding Source: National Science Foundation

Ask authors/readers for more resources

Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global beta-sheet/beta-sheet facial complementarity is a critical determinant for amyloid nucleation and structural selection.

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