Catalysis, Commitment and Encapsulation during GroE-mediated Folding

This publication has 78 references indexed in Scilit:

• Nucleotide-Dependent Complex Formation between the Escherichia coli Chaperonins GroEL and GroES Studied under Equilibrium Conditions
  Biochemistry, 1997
• Probing the Structural Role of an αβ Loop of Maltose-binding Protein by Mutagenesis: Heat-shock Induction by Loop Variants of the Maltose-binding Protein that Form Periplasmic Inclusion Bodies
  Journal of Molecular Biology, 1996
• Release of both native and non-native proteins from a cis-only GroEL ternary complex
  Nature, 1996
• 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
• Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
  Nature, 1994
• Characterization of a Functional GroEL ₁₄ (GroES ₇ ) ₂ Chaperonin Hetero-Oligomer
  Science, 1994
• To Fold or Not to Fold . . .
  Science, 1993
• GroE facilitates refolding of citrate synthase by suppressing aggregation
  Biochemistry, 1991
• Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
  Gene, 1988