Mycobacterium tuberculosis GroEL Homologues Unusually Exist as Lower Oligomers and Retain the Ability to Suppress Aggregation of Substrate Proteins
- 2 August 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 342 (2) , 605-617
- https://doi.org/10.1016/j.jmb.2004.07.066
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- The chaperonin folding machineTrends in Biochemical Sciences, 2002
- Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein FoldingJournal of Biological Chemistry, 2000
- The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complexNature, 1997
- Distinct actions of cis and trans ATP within the double ring of the chaperonin GroELNature, 1997
- In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin SystemCell, 1997
- Mycobacterium tuberculosis expresses two chaperonin-60 homologs.Proceedings of the National Academy of Sciences, 1993
- Mycobacteria contain two groEL genes: the second Mycobacterium leprae groEL gene is arranged in an operon with groESMolecular Microbiology, 1992
- Characterization of the groEL-like genes in Streptomyces albusJournal of Bacteriology, 1991
- Linkage map of Escherichia coli K-12, edition 8.Microbiological Reviews, 1990
- The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperaturesJournal of Bacteriology, 1989