Peptidyl-prolyl cis-trans isomerases, cyclophilin, FK506-binding protein, and ninaA: Four of a kind
- 1 December 1990
- journal article
- review article
- Published by Elsevier in Current Opinion in Cell Biology
- Vol. 2 (6) , 1104-1107
- https://doi.org/10.1016/0955-0674(90)90163-9
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymesBiochemistry, 1990
- Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortionBiochemistry, 1990
- Cyclosporin A Specifically Inhibits Function of Nuclear Proteins Involved in T Cell ActivationScience, 1989
- Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiaeNature, 1989
- A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomeraseNature, 1989
- A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilinNature, 1989
- Kinetic β‐deuterium isotope effects suggest a covalent mechanism for the protein folding enzyme peptidylprolyl cis/trans‐isomeraseFEBS Letters, 1989
- The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding proteinNature, 1989
- Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteinsNature, 1989
- Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilinNature, 1989