Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds
- 1 September 1980
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 142 (1) , 43-62
- https://doi.org/10.1016/0022-2836(80)90205-3
Abstract
No abstract availableThis publication has 52 references indexed in Scilit:
- Intermediates in the refolding of reduced ribonuclease AJournal of Molecular Biology, 1979
- Experimental studies of protein folding and unfoldingProgress in Biophysics and Molecular Biology, 1979
- Possible implications of many proline residues for the kinetics of protein unfolding and refoldingJournal of Molecular Biology, 1978
- Stimulation of reduced lysozyme regeneration by transferrin and lactoferrinArchives of Biochemistry and Biophysics, 1977
- Kinetics of refolding of reduced ribonucleaseJournal of Molecular Biology, 1977
- Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1977
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1975
- The identity of the insulin degrading thiol-protein disulfide oxidoreductase (glutathione-insulin transhydrogenase) with the sulfhydryl-disulfide interchange enzymeFEBS Letters, 1973
- Dithiothreitol, a New Protective Reagent for SH Groups*Biochemistry, 1964