Protein folding: Chaperones get Hip

This publication has 13 references indexed in Scilit:

• Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle
  Cell, 1995
• The Dissociation of ATP from hsp70 of Saccharomyces cerevisiae Is Stimulated by Both Ydj1p and Peptide Substrates
  Journal of Biological Chemistry, 1995
• The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.
  Proceedings of the National Academy of Sciences, 1994
• A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation.
  Proceedings of the National Academy of Sciences, 1994
• DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70
  Trends in Biochemical Sciences, 1994
• Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
  Cell, 1994
• Kinetics of Molecular Chaperone Action
  Science, 1994
• Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
  Biochemistry, 1992
• Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
  Nature, 1992
• Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
  Proceedings of the National Academy of Sciences, 1991