GroEL-mediated folding of structurally homologous dihydrofolate reductases 1 1Edited by P. E. Wright

This publication has 60 references indexed in Scilit:

• Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli β‐galactosidase
  Protein Science, 1996
• The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
  Nature Structural & Molecular Biology, 1996
• Determination of Regions in the Dihydrofolate Reductase Structure That Interact with the Molecular Chaperonin GroEL
  Biochemistry, 1996
• Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
  Nature Structural & Molecular Biology, 1995
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
  Nature, 1994
• Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
  Biochemistry, 1991
• Effects of point mutations in a hinge region on the stability, folding, and enzymic activity of Escherichia coli dihydrofolate reductase
  Biochemistry, 1991
• Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM—A flexible, portable system
  Analytical Biochemistry, 1983
• Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase
  Biochemistry, 1981
• Purification and properties of Escherichia coli dihydrofolate reductase
  Biochemistry, 1975