The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin
Abstract
Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel β-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.
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A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase
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Cited by
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Self-citationThe mechanism of action of cyclosporin A and FK506
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Self-citationFeng, S., Chen, J. K., Yu, H., Simon, J. A., & Schreiber, S. L. (1994) · Science · doi:10.1126/science.7526465 · Cited by 687
Self-citationChemically induced proximity in biology and medicine
Stanton, B. Z., Chory, E. J., & Crabtree, G. R. (2018) · Science · doi:10.1126/science.aao5902 · Cited by 475
Molecular Glues for Targeted Protein Degradation: From Serendipity to Rational Discovery
Dong, G., Ding, Y., He, S., & Sheng, C. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00895 · Cited by 369
Metadata
- Authors
- Michnick, S. W., Rosen, M. K., Wandless, T. J., Karplus, M., & Schreiber, S. L.
- Venue
- Science
- Published
- 1991-05-10
- Volume
- 252
- Issue
- 5007
- Pages
- 836-839
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1990664560
- Cited by
- 301
- References
- 34
- FWCI
- 14.84
- Type
- journal article
- Language
- en
- Open access
- closed
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