A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone
Open Access
- 1 September 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (35) , 20404-20409
- https://doi.org/10.1074/jbc.270.35.20404
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- The Hydrophobic Nature of GroEL-Substrate BindingJournal of Biological Chemistry, 1995
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Characterization of a Functional GroEL 14 (GroES 7 ) 2 Chaperonin Hetero-OligomerScience, 1994
- Symmetric Complexes of GroE Chaperonins as Part of the Functional CycleScience, 1994
- Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ionBiochemistry, 1993
- ATP induces large quaternary rearrangements in a cage-like chaperonin structureCurrent Biology, 1993
- A polypeptide bound by the chaperonin groEL is localized within a central cavity.Proceedings of the National Academy of Sciences, 1993
- Cooperativity in ATP hydrolysis by GroEL is increased by GroESFEBS Letters, 1991
- (Mg–ATP)-dependent self-assembly of molecular chaperone GroELNature, 1990