Pseudo-T-even Bacteriophage RB49 Encodes CocO, a Cochaperonin for GroEL, Which Can Substitute for Escherichia coli's GroES and Bacteriophage T4's Gp31
Open Access
- 23 March 2001
- journal article
- Published by Elsevier
- Vol. 276 (12), 8720-8726
- https://doi.org/10.1074/jbc.m008477200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDINGAnnual Review of Biochemistry, 1998
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- Protein folding Folding with a two-stroke motorNature, 1997
- The crystal structure of the GroES co-chaperonin at 2.8 Å resolutionNature, 1996
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Role of the Major Heat Shock Proteins as Molecular ChaperonesAnnual Review of Cell Biology, 1993
- Characterization of a functionally important mobile domain of GroESNature, 1993
- MOLECULAR CHAPERONESAnnual Review of Biochemistry, 1991
- The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperaturesJournal of Bacteriology, 1989