The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen.
Open Access
- 1 December 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (35) , 17144-17148
- https://doi.org/10.1016/s0021-9258(18)45502-0
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- 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
- Prolyl isomerization: How significant for in vivo protein folding?Biopolymers, 1985
- Conformational specificity of chymotrypsin toward proline-containing substratesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Formation of the triple helix of type I procollagen in cellulo. Temperature-dependent kinetics support a model based on cis trans isomerization of peptide bondsEuropean Journal of Biochemistry, 1984
- Physical and chemical properties of human type III procollagenBiochemistry, 1983
- Folding Mechanism of the Triple Helix in Type‐III Collagen and Type‐III pN–CollagenEuropean Journal of Biochemistry, 1980
- An explanation for the rare occurrence of cis peptide units in proteins and polypeptidesJournal of Molecular Biology, 1976
- Nmr studies of the molecular conformations in the linear oligopeptides H-(L-Ala)n-L-Pro-OHBiopolymers, 1976
- Evidence for cis peptide bonds in copolypeptides of glycine and prolineBiochemistry, 1972
- The Configurational Changes of Poly-L-proline in SolutionJournal of the American Chemical Society, 1960