On the role of groES in the chaperonin-assisted folding reaction. Three case studies.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference59 articles.
1. Protein folding in the cell
2. Homologous plant and bacterial proteins chaperone oligomeric protein assembly
3. Purification and properties of the groES morphogenetic protein of Escherichia coli.
4. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
5. Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria
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1. Evolution and Diversification of the GroEL/Chaperonin Paralogs in Cyanobacteria;Ecophysiology and Biochemistry of Cyanobacteria;2021
2. Chaperonin-assisted protein folding: a chronologue;Quarterly Reviews of Biophysics;2020
3. Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones;Protein Science;2019-12-23
4. Repetitive Protein Unfolding by the trans Ring of the GroEL-GroES Chaperonin Complex Stimulates Folding;Journal of Biological Chemistry;2013-10
5. Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented;FEBS Letters;2011-05-20
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