GroEL/GroES-dependent Reconstitution of α2β2 Tetramers of Human Mitochondrial Branched Chain α-Ketoacid Decarboxylase

This publication has 39 references indexed in Scilit:

• The Hsp70 and Hsp60 Chaperone Machines
  Cell, 1998
• The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
  Nature, 1997
• Molecular chaperones in cellular protein folding
  Nature, 1996
• Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae
  Science, 1996
• The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
  Nature, 1996
• Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
  Cell, 1995
• Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
  Trends in Biochemical Sciences, 1994
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
  Nature, 1994
• Symmetric Complexes of GroE Chaperonins as Part of the Functional Cycle
  Science, 1994
• MOLECULAR CHAPERONES
  Annual Review of Biochemistry, 1991