Identification of Essential Residues in the Type II Hsp40 Sis1 That Function in Polypeptide Binding

This publication has 48 references indexed in Scilit:

• The Crystal Structure of a GroEL/Peptide Complex
  Cell, 1999
• The Human DnaJ Homologue dj2 Facilitates Mitochondrial Protein Import and Luciferase Refolding
  The Journal of cell biology, 1997
• Nuclear Magnetic Resonance Solution Structure of the Human Hsp40 (HDJ-1) J-domain
  Journal of Molecular Biology, 1996
• Structure-Function Analysis of the Zinc Finger Region of the DnaJ Molecular Chaperone
  Published by Elsevier ,1996
• Molecular chaperones in cellular protein folding
  Nature, 1996
• ATP Hydrolysis Is Required for the DnaJ-dependent Activation of DnaK Chaperone for Binding to Both Native and Denatured Protein Substrates
  Journal of Biological Chemistry, 1995
• Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation
  FEBS Letters, 1995
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
  Nature, 1994
• Disulfide-Rearranged Molten Globule State of .alpha.-Lactalbumin
  Biochemistry, 1994
• YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
  Cell, 1992