Intermolecular Alignment in β2-Microglobulin Amyloid Fibrils-Reference-Cited by-同舟云学术

Intermolecular Alignment in β2-Microglobulin Amyloid Fibrils

Published:2010-11-15 Issue:48 Volume:132 Page:17077-17079
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Debelouchina Galia T.¹,Platt Geoffrey W.¹,Bayro Marvin J.¹,Radford Sheena E.¹,Griffin Robert G.¹

Affiliation:

1. Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States, and Astbury Centre for Structural Molecular Biology and Institute of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, U.K.

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja107987f

Reference35 articles.

1. A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin

2. Glimpses of the molecular mechanisms of β2 -microglobulin fibril formation in vitro: Aggregation on a complex energy landscape

3. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly

4. A Common β-Sheet Architecture Underlies in Vitro and in Vivo β2-Microglobulin Amyloid Fibrils

5. Fibril Fragmentation Enhances Amyloid Cytotoxicity

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