Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate 2-microglobulin amyloid assembly
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference37 articles.
1. The Adaptable Major Histocompatibility Complex (MHC) Fold: Structure and Function of Nonclassical and MHC Class I–Like Molecules
2. A Systematic Study of the Effect of Physiological Factors on β2-Microglobulin Amyloid Formation at Neutral pH
3. Glycosaminoglycans Enhance the Trifluoroethanol-Induced Extension of 2-Microglobulin-Related Amyloid Fibrils at a Neutral pH
4. Folding and Fibrillogenesis: Clues from β2-Microglobulin
5. A native to amyloidogenic transition regulated by a backbone trigger
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