Prolyl Isomerases: Role in Protein Folding
- 1 January 1993
- book chapter
- Published by Elsevier in Advances in Protein Chemistry
- Vol. 44, 25-66
- https://doi.org/10.1016/s0065-3233(08)60563-x
Abstract
No abstract availableThis publication has 117 references indexed in Scilit:
- Kinetic coupling between protein folding and prolyl isomerizationJournal of Molecular Biology, 1992
- Kinetic coupling between protein folding and prolyl isomerizationJournal of Molecular Biology, 1992
- Ribonuclease T1: Structure, Function, and StabilityAngewandte Chemie International Edition in English, 1991
- A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilinNature, 1989
- Construction and characterization of mutant iso-2-cytochromes c with replacement of conserved prolinesBiochemistry, 1988
- Catalysis of proline isomerization during protein-folding reactionsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- The disulphide folding pathway of ribonuclease T1Journal of Molecular Biology, 1986
- The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomeraseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Folding of homologous proteinsJournal of Molecular Biology, 1983
- The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentrationJournal of Molecular Biology, 1979