ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation-Reference-Cited by-同舟云学术

ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation

Published:2016-10-06 Issue:1 Volume:7 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Seo Ji Hae,Park Ji-Hyeon,Lee Eun Ji,Vo Tam Thuy Lu,Choi Hoon,Kim Jun Yong,Jang Jae Kyung,Wee Hee-Jun,Lee Hye Shin,Jang Se Hwan,Park Zee Yong,Jeong Jaeho,Lee Kong-Joo,Seok Seung-Hyeon,Park Jin Young,Lee Bong Jin,Lee Mi-Ni,Oh Goo Taeg,Kim Kyu-Won

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/ncomms12882.pdf

Reference57 articles.

1. Ellis, J. Proteins as molecular chaperones. Nature 328, 378–379 (1987).

2. Hartl, F. U. Molecular chaperones in cellular protein folding. Nature 381, 571–579 (1996).

3. Pelham, H. R. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46, 959–961 (1986).

4. Rothman, J. E. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59, 591–601 (1989).

5. Gething, M. J. & Sambrook, J. Protein folding in the cell. Nature 355, 33–45 (1992).

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