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Methods in Enzymology|April 16, 1998
Structural analysis of GroE chaperonin complexes using chemical cross-linkingA Azem, C Weiss, P GoloubinoffThe Journal of Biological Chemistry|November 24, 1995
Increased efficiency of GroE-assisted protein folding by manganese ionsS Diamant, A Azem, C Weiss, et al.FEBS Letters|April 28, 1997
GroES binding regulates GroEL chaperonin activity under heat shockP Goloubinoff, S Diamant, C Weiss, et al.Biochemistry|January 10, 1995
Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14S Diamant, A Azem, C Weiss, et al.Proceedings of the National Academy of Sciences of the United States of America|December 19, 1995
The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomerA Azem, S Diamant, M Kessel, et al.Science (New York, N.Y.)|July 29, 1994
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomerA Azem, M Kessel, P GoloubinoffBiochemistry|May 31, 1994
Effect of divalent cations on the molecular structure of the GroEL oligomerA Azem, S Diamant, P GoloubinoffThe Journal of Biological Chemistry|June 9, 1995
A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysisC Weiss, P GoloubinoffBiochemistry|July 10, 1998
Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentrationS Diamant, P GoloubinoffAnnales De Cardiologie Et D'Angeiologie|May 20, 2006
[The toxic aggregation of proteins: a kind of "molecular delinquency" actively fought in the cell by molecular chaperones and proteases]M P Hinault, P GoloubinoffPageof 92