Structural Complexity of a Composite Amyloid Fibril-Reference-Cited by-同舟云学术

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Structural Complexity of a Composite Amyloid Fibril

Published:2011-08-23 Issue:37 Volume:133 Page:14686-14698
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lewandowski Józef R.¹,van der Wel Patrick C. A.¹,Rigney Mike²,Grigorieff Nikolaus²,Griffin Robert G.¹

Affiliation:

1. Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States

2. Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja203736z

Reference69 articles.

1. Structure of the cross-β spine of amyloid-like fibrils

2. Atomic structures of amyloid cross-β spines reveal varied steric zippers

3. The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35

4. Replica exchange molecular dynamics simulations of amyloid peptide aggregation

5. Protein Misfolding and Amyloid Formation for the Peptide GNNQQNY from Yeast Prion Protein Sup35: Simulation by Reaction Path Annealing

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