Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution-Reference-Cited by-同舟云学术

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Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution

Published:2012-01-17 Issue:4 Volume:586 Page:411-415
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Lee Yoo-Sup,Ryu Kyoung-Seok,Kim Seo-Jin,Ko Hyun-Suk,Sim Dae-Won,Jeon Young Ho,Kim Eun-Hee,Choi Wahn-Soo,Won Hyung-Sik

Funder

Korea Research Foundation Grant

Basic Science Research Program

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2012.01.011/fullpdf

Reference22 articles.

1. Chaperone activity with a redox switch;Jakob;Cell,1999

2. Redox-regulated molecular chaperones;Graf;Cell. Mol. Life Sci.,2002

3. Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity;Chi;FEBS Lett.,2011

4. Unfolding of metastable linker region is at the core of Hsp33’s activation as a redox-regulated chaperone;Cremers;J. Biol. Chem.,2010

5. The redox-switch domain of Hsp33 functions as dual stress sensor;Ilbert;Nat. Struct. Mol. Biol.,2007

Cited by 6 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. Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33;Biology;2021-11-12

2. Unique Unfoldase/Aggregase Activity of a Molecular Chaperone Hsp33 in its Holding-Inactive State;Journal of Molecular Biology;2019-03

3. Oxidation-induced conformational change of Hsp33, monitored by NMR;Journal of the Korean Magnetic Resonance Society;2015-12-20

4. Semi-Empirical Structure Determination of Escherichia coli Hsp33 and Identification of Dynamic Regulatory Elements for the Activation Process;Journal of Molecular Biology;2015-12

5. Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists;Progress in Nuclear Magnetic Resonance Spectroscopy;2015-04

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