Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues

This publication has 48 references indexed in Scilit:

• GroEL‐Mediated protein folding
  Protein Science, 1997
• An Internal FK506‐Binding Domain is the Catalytic Core of the Prolyl Isomerase Activity Associated with the Bacillus Subtilis Trigger Factor
  European Journal of Biochemistry, 1997
• Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
  Cell, 1996
• Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein Folding
  Journal of Molecular Biology, 1996
• Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family
  FEBS Letters, 1995
• A Kinetic Partitioning Model of Selective Binding of Nonnative Proteins by the Bacterial Chaperone SecB
  Science, 1991
• Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
  Nature, 1989
• Calculation of protein extinction coefficients from amino acid sequence data
  Analytical Biochemistry, 1989
• ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle
  Cell, 1988
• Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.
  Proceedings of the National Academy of Sciences, 1987