Binding of an N-terminal Rhodanese Peptide to DnaJ and to Ribosomes

This publication has 20 references indexed in Scilit:

• Analysis of Three DnaK Mutant Proteins Suggests That Progression through the ATPase Cycle Requires Conformational Changes
  Published by Elsevier ,1995
• Large activation energy barriers to chaperone-peptide complex formation and dissociation
  Biochemistry, 1995
• Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication
  Journal of Biological Chemistry, 1995
• The Importance of the N-terminal Segment for DnaJ-mediated Folding of Rhodanese While Bound to Ribosomes as Peptidyl-tRNA
  Published by Elsevier ,1995
• Modulation of the ATPase Activity of the Molecular Chaperone DnaK by Peptides and the DnaJ and GrpE Heat Shock Proteins
  Journal of Biological Chemistry, 1995
• Contribution of cotranslational folding to the rate of formation of native protein structure.
  Proceedings of the National Academy of Sciences, 1995
• Chaperone-dependent Folding and Activation of Ribosome-bound Nascent Rhodanese: Analysis by Fluorescence
  Journal of Molecular Biology, 1994
• Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA
  Published by Elsevier ,1994
• Specificity of DnaK-peptide Binding
  Journal of Molecular Biology, 1994
• Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.
  Proceedings of the National Academy of Sciences, 1993