Mechanisms for GroEL/GroES-mediated Folding of a Large 86-kDa Fusion Polypeptide in Vitro

This publication has 49 references indexed in Scilit:

• The Hsp70 and Hsp60 Chaperone Machines
  Cell, 1998
• Molecular chaperones in cellular protein folding
  Nature, 1996
• Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10
  FEBS Letters, 1995
• Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
  Trends in Biochemical Sciences, 1994
• Cytosolic chaperonin confirmed
  Nature, 1992
• Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro.
  Proceedings of the National Academy of Sciences, 1992
• MOLECULAR CHAPERONES
  Annual Review of Biochemistry, 1991
• Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
  Nature, 1989
• Homologous plant and bacterial proteins chaperone oligomeric protein assembly
  Nature, 1988
• Amino-Acid Sequence Homology of a Polymorphic Cellular Protein from Human Lymphocytes and the Chaperonins fromEscherichia coli (groEL)and Chloroplasts (Rubisco-Binding Protein)
  Biological Chemistry Hoppe-Seyler, 1988