Interactions between the GroE Chaperonins and Rhodanese

This publication has 35 references indexed in Scilit:

• The Hydrophobic Nature of GroEL-Substrate Binding
  Journal of Biological Chemistry, 1995
• Residues in chaperonin GroEL required for polypeptide binding and release
  Nature, 1994
• Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.
  Proceedings of the National Academy of Sciences, 1993
• Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
  Cell, 1993
• To Fold or Not to Fold . . .
  Science, 1993
• Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
  Nature, 1992
• Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
  Protein Science, 1992
• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
  Nature, 1991
• GroE facilitates refolding of citrate synthase by suppressing aggregation
  Biochemistry, 1991
• Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
  Nature, 1989