The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase.
Open Access
- 1 December 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (34) , 21011-21015
- https://doi.org/10.1016/s0021-9258(17)45319-1
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cellBiochemistry, 1990
- 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
- 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
- Induction of Interleukin 2 Messenger RNA Inhibited by Cyclosporin AScience, 1984
- Design and preparation of affinity columns for the purification of eukaryotic messenger ribonucleic acid cap binding proteinBiochemistry, 1981
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976