The Amino-terminal 118 Amino Acids of Escherichia coli Trigger Factor Constitute a Domain That Is Necessary and Sufficient for Binding to Ribosomes

This publication has 11 references indexed in Scilit:

• Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
  The EMBO Journal, 1997
• The Escherichia coli trigger factor
  FEBS Letters, 1996
• Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
  Proceedings of the National Academy of Sciences, 1996
• Identification of the prolyl isomerase domain of Escherichia coli trigger factor
  FEBS Letters, 1996
• An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity
  FEBS Letters, 1996
• Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family
  FEBS Letters, 1995
• Prediction of Protein Secondary Structure at Better than 70% Accuracy
  Journal of Molecular Biology, 1993
• The “trigger factor cycle” includes ribosomes, presecretory proteins, and the plasma membrane
  Cell, 1988
• 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