FKBP, thought to be identical to PKCI-2, does not inhibit protein kinase C
- 1 January 1991
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry Letters
- Vol. 1 (4) , 205-210
- https://doi.org/10.1016/s0960-894x(00)80253-x
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein.Molecular and Cellular Biology, 1991
- FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences, 1991
- Rapamycin and FK506 binding proteins (immunophilins)Journal of the American Chemical Society, 1991
- Chemistry and Biology of the Immunophilins and Their Immunosuppressive LigandsScience, 1991
- Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin.Proceedings of the National Academy of Sciences, 1990
- Probing Immunosuppressant Action with a Nonnatural Immunophilin LigandScience, 1990
- Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein foldingNature, 1990
- 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
- Cyclophilin: A Specific Cytosolic Binding Protein for Cyclosporin AScience, 1984