GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine

This publication has 62 references indexed in Scilit:

• A structural model for GroEL–polypeptide recognition
  Proceedings of the National Academy of Sciences, 1997
• The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
  Nature Structural & Molecular Biology, 1996
• The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.
  Proceedings of the National Academy of Sciences, 1995
• Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
  Nature Structural & Molecular Biology, 1995
• The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
  Journal of Molecular Biology, 1995
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
  Nature, 1994
• Characterization of a Functional GroEL ₁₄ (GroES ₇ ) ₂ Chaperonin Hetero-Oligomer
  Science, 1994
• A polypeptide bound by the chaperonin groEL is localized within a central cavity.
  Proceedings of the National Academy of Sciences, 1993
• GroE facilitates refolding of citrate synthase by suppressing aggregation
  Biochemistry, 1991
• Principles that Govern the Folding of Protein Chains
  Science, 1973