Biochemical Characterization of Symmetric GroEL-GroES Complexes

This publication has 22 references indexed in Scilit:

• Residues in chaperonin GroEL required for polypeptide binding and release
  Nature, 1994
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
  Nature, 1994
• GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
  Cell, 1994
• Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding
  Science, 1994
• Characterization of a Functional GroEL ₁₄ (GroES ₇ ) ₂ Chaperonin Hetero-Oligomer
  Science, 1994
• The formation of symmetrical GroEL‐GroES complexes in the presence of ATP
  FEBS Letters, 1994
• Transmission Electron Microscopy of GroEL, GroES, and the Symmetrical GroEL/ES Complex
  Journal of Structural Biology, 1994
• The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
  Nature, 1993
• Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
  Biochemistry, 1993
• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
  Nature, 1991