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Nucleic Acids Research|December 21, 1984
Chloroplast-coded atrazine resistance in Solanum nigrum: psbA loci from susceptible and resistant biotypes are isogenic except for a single codon changeP Goloubinoff, M Edelman, R B HallickProceedings of the National Academy of Sciences of the United States of America|March 1, 1993
Evolution of maize inferred from sequence diversity of an Adh2 gene segment from archaeological specimensP Goloubinoff, S Pääbo, A C WilsonThe Journal of Biological Chemistry|August 23, 2001
Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stressesS Diamant, N Eliahu, D Rosenthal, 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.The Journal of Biological Chemistry|November 24, 1995
Increased efficiency of GroE-assisted protein folding by manganese ionsS Diamant, A Azem, C Weiss, et al.The Journal of Biological Chemistry|June 6, 1998
The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone networkL Veinger, S Diamant, J Buchner, et al.Nature|January 5, 1989
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coliP Goloubinoff, A A Gatenby, G H LorimerThe Journal of Biological Chemistry|May 10, 2000
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machineryS Diamant, A P Ben-Zvi, B Bukau, 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.Pageof 4