Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone-Reference-Cited by-同舟云学术

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Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone

Published:2018-06 Issue:12 Volume:430 Page:1760-1772
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Kim Jihong,Choi Dongwook,Cha So-Young,Oh Young-Mee,Hwang Eunha,Park Chankyu,Ryu Kyoung-Seok

Funder

National Research Foundation of Korea

Korea Basic Science Institute

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference45 articles.

1. Evolutionary and functional relationships within the DJ1 superfamily;Bandyopadhyay;BMC Evol. Biol.,2004

2. Identification of functional subclasses in the DJ-1 superfamily proteins;Wei;PLoS Comput. Biol.,2007

3. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism;Bonifati;Science,2003

4. Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK–DnaJ–GrpE system in the management of protein misfolding under severe stress conditions;Mujacic;Mol. Microbiol.,2004

5. Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31;Mujacic;Mol. Microbiol.,2006

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