High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure,-Reference-Cited by-同舟云学术

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High-Resolution MAS NMR Analysis of PI3-SH3 Amyloid Fibrils: Backbone Conformation and Implications for Protofilament Assembly and Structure,

Published:2010-08-13 Issue:35 Volume:49 Page:7474-7484
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bayro Marvin J.¹,Maly Thorsten¹,Birkett Neil R.²,MacPhee Cait E.³,Dobson Christopher M.²,Griffin Robert G.¹

Affiliation:

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

2. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.

3. SUPA, School of Physics and Astronomy, University of Edinburgh, Edinburgh EH9 3JZ, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi100864t

Reference97 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

3. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation

4. Amyloid formation by globular proteins under native conditions

5. Therapeutic strategies for human amyloid diseases

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