The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism-Reference-Cited by-同舟云学术

The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

Published:2018-10-30 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Iadanza Matthew G.^ORCID,Silvers Robert^ORCID,Boardman Joshua,Smith Hugh I.,Karamanos Theodoros K.,Debelouchina Galia T.^ORCID,Su Yongchao^ORCID,Griffin Robert G.^ORCID,Ranson Neil A.^ORCID,Radford Sheena E.^ORCID

Funder

Wellcome Trust

EC | European Research Council

Deutsche Forschungsgemeinschaft

U.S. Department of Health & Human Services | National Institutes of Health

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-06761-6.pdf

Reference76 articles.

1. Sipe, J. D. et al. Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines. Amyloid 23, 209–213 (2016).

2. Pham, C. L. L., Kwan, A. H. & Sunde, M. Functional amyloid: widespread in nature, diverse in purpose. Essays Biochem. 56, 207–219 (2014).

3. Fowler, D. M., Koulov, A. V., Balch, W. E. & Kelly, J. W. Functional amyloid—from bacteria to humans. Trends Biochem. Sci. 32, 217–224 (2007).

4. Knowles, T. P. J. & Buehler, M. J. Nanomechanics of functional and pathological amyloid materials. Nat. Nanotechnol. 6, 469–479 (2011).

5. Gallardo, R. et al. De novo design of a biologically active amyloid. Science 354, aah4949 (2016).

Cited by 125 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. NMR studies of amyloid interactions;Progress in Nuclear Magnetic Resonance Spectroscopy;2024-11

2. Supersaturation, a Critical Factor Underlying Proteostasis of Amyloid Fibril Formation;Journal of Molecular Biology;2024-07

3. Exploring the Molecular Pathology of Iatrogenic Amyloidosis;Journal of Molecular Pathology;2024-06-05

4. Atomic resolution structure of full-length human insulin fibrils;Proceedings of the National Academy of Sciences;2024-05-29

5. Molecular Crowding: The History and Development of a Scientific Paradigm;Chemical Reviews;2024-03-11