NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations-Reference-Cited by-同舟云学术

NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations

Published:2018-07-04 Issue:30 Volume:57 Page:4421-4430
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Leach Benjamin I.¹^ORCID,Zhang Xin²^ORCID,Kelly Jeffery W.³^ORCID,Dyson H. Jane¹^ORCID,Wright Peter E.¹^ORCID

Affiliation:

1. Department of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States

2. Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, United States

3. Department of Chemistry and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States

Funder

National Institute of Diabetes and Digestive and Kidney Diseases

Skaggs Institute for Chemical Biology

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00642

Reference46 articles.

1. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

2. The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into Amyloid