Inter and intra-subunit interactions at the subunit interface of chaperonin GroEL are essential for its stability and assembly-Reference-Cited by-同舟云学术

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Inter and intra-subunit interactions at the subunit interface of chaperonin GroEL are essential for its stability and assembly

Published:2019-03 Issue:3 Volume:1867 Page:331-343
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Puri Sarita,Chaudhuri Tapan K.

Funder

IIT Delhi

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference38 articles.

1. Molecular chaperone functioning of Heat-shock Proteins;Hendrick;Annu. Rev. Biochem.,1993

2. Heat shock proteins as molecular chaperones;Becker;FEBS J.,1994

3. Review, molecular chaperones in protein folding and proteostasis;Hartl;Nature,2011

4. Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism;Todd;Proc. Natl. Acad. Sci. U. S. A.,1996

5. Folding in-vivo of bacterial cytoplasmic proteins - the role of GroEL;Horwich;Cell,1993

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