Stable Expression and Rapid Purification ofEscherichia coliGroEL and GroES Chaperonins

This publication has 18 references indexed in Scilit:

• Increased Efficiency of GroE-assisted Protein Folding by Manganese Ions
  Published by Elsevier ,1995
• A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone
  Published by Elsevier ,1995
• Monomer-Heptamer Equilibrium of the Escherichia coli Chaperonin GroES
  Biochemistry, 1995
• MOLECULAR CHAPERONES
  Annual Review of Biochemistry, 1991
• GroE facilitates refolding of citrate synthase by suppressing aggregation
  Biochemistry, 1991
• Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent
  Biochemistry, 1990
• Hyperexpression and purification ofEscherichia coliadenylate cyclase using a vector designed for expression of lethal gene products
  Nucleic Acids Research, 1989
• GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
  Nature, 1989
• Analysis of nutR, a site required for transcription antitermination in phage lambda.
  Proceedings of the National Academy of Sciences, 1987
• Crystalline Rhodanese. I. Purification and Physicochemical Examination.
  Acta Chemica Scandinavica, 1953