The role of pro regions in protein folding

This publication has 32 references indexed in Scilit:

• Correct folding of alpha-lytic protease is required for its extracellular secretion from Escherichia coli.
  The Journal of cell biology, 1992
• Protease pro region required for folding is a potent inhibitor of the mature enzyme
  Proteins-Structure Function and Bioinformatics, 1992
• A non-covalent NH₂-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence inEscherichia coli
  FEMS Microbiology Letters, 1992
• Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen
  FEBS Letters, 1991
• Pro‐peptide as an intermolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro‐peptide
  Molecular Microbiology, 1991
• Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.
  The Journal of cell biology, 1990
• The αlytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
  Nature, 1989
• Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
  Nature, 1989
• Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity
  Journal of Bacteriology, 1989
• Molecular analysis of the gene encoding α-lytic protease: evidence for a preproenzyme
  Gene, 1988