Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroEL(E461K).
J.Struct.Biol. (2006)
Crystal structure of wild-type chaperonin GROEL
J.Mol.Biol. (2005)
;Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study
;
Protein Sci. (2005)
A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation
Nat.Struct.Mol.Biol. (2004)
GroEL stability and function. Contribution of the ionic interactions at the inter-ring contact sites
J.Biol.Chem. (2003)
Salt bridges at the inter-ring interface regulate the thermostat of GroEL
J.Biol.Chem. (2002)
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
Nature (1997)
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution
Nature (1995)