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Cited by 301

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

Michnick, Stephen W., Rosen, Michael K., Wandless, Thomas J., Karplus, Martin, Schreiber, Stuart L.·1991·Science

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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Crossref · 10.1126/science.1709301

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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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CoChat. (2026). Citation check: Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin. https://app.cochat.ai/papers/10.1126/science.1709301
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Michnick, S. W., Rosen, M. K., Wandless, T. J., Karplus, M., & Schreiber, S. L. (1991). Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin. Science. https://doi.org/10.1126/science.1709301

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.