On the Maximum Size of Proteins to Stay and Fold in the Cavity of GroEL underneath GroES

This publication has 37 references indexed in Scilit:

• The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
  Cell, 1996
• Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
  Cell, 1996
• Protein folding in the central cavity of the GroEL–GroES chaperonin complex
  Nature, 1996
• Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
  Current Biology, 1996
• Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding
  Science, 1994
• Green Fluorescent Protein as a Marker for Gene Expression
  Science, 1994
• Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
  Protein Science, 1992
• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
  Nature, 1991
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970