Binding by design
- 1 May 1991
- journal article
- editorial
- Published by Springer Nature in Nature
- Vol. 351 (6323) , 185-186
- https://doi.org/10.1038/351185a0
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Atomic Structure of FKBP-FK506, an Immunophilin-Immunosuppressant ComplexScience, 1991
- Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and RapamycinScience, 1991
- Solution structure of the major binding protein for the immunosuppressant FK506Nature, 1991
- Molecular cloning and overexpression of the human FK506-binding protein FKBPNature, 1990
- Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerizationBiochemistry, 1990
- Cyclosporin A Specifically Inhibits Function of Nuclear Proteins Involved in T Cell ActivationScience, 1989
- A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomeraseNature, 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
- FK-506 — How much potential?Immunology Today, 1989