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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|April 15, 2000
Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein foldingR Dickson, C Weiss, R J Howard, et al.The 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.Molecular Microbiology|April 20, 2001
Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosolT Tomoyasu, A Mogk, H Langen, et al.Nucleic Acids Research|January 24, 1986
The enigma of the gene coding for ribosomal protein S12 in the chloroplasts of NicotianaH Fromm, M Edelman, B Koller, et al.Proceedings of the National Academy of Sciences of the United States of America|November 26, 1999
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone networkP Goloubinoff, A Mogk, A P Zvi, et al.Plant Molecular Biology|November 26, 2013
Characterization of the photosystem II 32 kDa protein in Synechococcus PCC7942P Goloubinoff, J Brusslan, S S Golden, et al.Nature|December 21, 1989
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATPP Goloubinoff, J T Christeller, A A Gatenby, et al.Proceedings of the National Academy of Sciences of the United States of America|December 23, 1998
Minimal and optimal mechanisms for GroE-mediated protein foldingA P Ben-Zvi, J Chatellier, A R Fersht, et al.Pageof 92