Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates α-helix formation of the polyQ tract but suppresses its aggregation-Reference-Cited by-同舟云学术

Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates α-helix formation of the polyQ tract but suppresses its aggregation

Published:2019-05-16 Issue:1 Volume:9 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Hong Jun-Ye,Wang Dong-Dong,Xue Wei,Yue Hong-Wei,Yang Hui,Jiang Lei-Lei,Wang Wen-Ning,Hu Hong-Yu

Funder

National Natural Science Foundation of China

the National Basic Research Program of China

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-019-43926-9.pdf

Reference65 articles.

1. Li, S. H. & Li, X. J. Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats. Human molecular genetics 7, 777–782 (1998).

2. Scherzinger, E. et al. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington’s disease pathology. Proceedings of the National Academy of Sciences of the United States of America 96, 4604–4609 (1999).

3. Yang, H. & Hu, H. Y. Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology. The FEBS journal 283, 3705–3717, https://doi.org/10.1111/febs.13722 (2016).

4. Temussi, P. A., Masino, L. & Pastore, A. From Alzheimer to Huntington: why is a structural understanding so difficult? EMBO J 22, 355–361, https://doi.org/10.1093/emboj/cdg044 (2003).

5. Hoop, C. L. et al. Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance. Biochemistry 53, 6653–6666, https://doi.org/10.1021/bi501010q (2014).

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