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X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex
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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
Cited by
Serine/threonine phosphatases: mechanism through structure
Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488
Crabtree, G. R., & Olson, E. N. (2002) · Cell · doi:10.1016/s0092-8674(02)00699-2 · Cited by 1,323
Nucleases: diversity of structure, function and mechanism
Yang, W. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000181 · Cited by 692
Structural basis of lenalidomide-induced CK1α degradation by the CRL4CRBN ubiquitin ligase
Petzold, G., Fischer, E. S., & Thomä, N. H. (2016) · Nature · doi:10.1038/nature16979 · Cited by 620
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459
Graef, I. A., Wang, F., Charron, F., Chen, L., Neilson, J., Tessier-Lavigne, M., & Crabtree, G. R. (2003) · Cell · doi:10.1016/s0092-8674(03)00390-8 · Cited by 379
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
Calcineurin is essential for survival during membrane stress in Candida albicans
Cruz, M. C., Goldstein, A. L., Blankenship, J. R., Del Poeta, M., Davis, D., Cardenas, M. E., Perfect, J. R., McCusker, J. H., & Heitman, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.4.546 · Cited by 342
Harnessing calcineurin as a novel anti-infective agent against invasive fungal infections.
Steinbach, W. J., Reedy, J. L., Cramer, R. A., Perfect, J. R., & Heitman, J. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1680 · Cited by 313
Onyewu, C., Blankenship, J. R., Del Poeta, M., & Heitman, J. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.3.956-964.2003 · Cited by 282
Hughes, S. J., & Ciulli, A. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170041 · Cited by 240
Calcineurin: Structure, function, and inhibition
Hemenway, C. S., & Heitman, J. (1999) · Cell Biochemistry and Biophysics · doi:10.1007/bf02737887 · Cited by 227
Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates
Brautigan, D. L., & Shenolikar, S. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012332 · Cited by 191
Fox, D. S., Cruz, M. C., Sia, R. A. L., Ke, H., Cox, G. M., Cardenas, M. E., & Heitman, J. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02295.x · Cited by 175
FKBP Ligands—Where We Are and Where to Go?
Kolos, J. M., Voll, A. M., Bauder, M., & Hausch, F. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01425 · Cited by 158
Refined structure of the FKBP12–rapamycin–FRB ternary complex at 2.2 Å resolution
Liang, J., Choi, J., & Clardy, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998014747 · Cited by 148
Good fungi gone bad: The corruption of calcineurin
Fox, D. S., & Heitman, J. (2002) · BioEssays · doi:10.1002/bies.10157 · Cited by 137
Rapamycin-inspired macrocycles with new target specificity
Guo, Z., Hong, S. Y., Wang, J., Rehan, S., Liu, W., Peng, H., Das, M., Li, W., Bhat, S., Peiffer, B., et al. (2019) · Nature Chemistry · doi:10.1038/s41557-018-0187-4 · Cited by 120
Juvvadi, P. R., Fox, D., Bobay, B. G., Hoy, M. J., Gobeil, S. M. C., Venters, R. A., Chang, Z., Lin, J. J., Averette, A. F., Cole, D. C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12199-1 · Cited by 116
Anders, C., Higuchi, Y., Koschinsky, K., Bartel, M., Schumacher, B., Thiel, P., Nitta, H., Preisig-Müller, R., Schlichthörl, G., Renigunta, V., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.015 · Cited by 106
Signal-transduction cascades as targets for therapeutic intervention by natural products
Cardenas, M. E., Sanfridson, A., Cutler, N. S., & Heitman, J. (1998) · Trends in Biotechnology · doi:10.1016/s0167-7799(98)01239-6 · Cited by 101
Bifunctional chemical probes inducing protein–protein interactions
Maniaci, C., & Ciulli, A. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.07.003 · Cited by 100
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90
Bracher, A., Kozany, C., Thost, A.-K., & Hausch, F. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911013862 · Cited by 62
Brath, U., Akke, M., Yang, D., Kay, L. E., & Mulder, F. A. A. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0570279 · Cited by 57
Wu, X., Wang, L., Han, Y., Regan, N., Li, P.-K., Villalona, M. A., Hu, X., Briesewitz, R., & Pei, D. (2011) · ACS Combinatorial Science · doi:10.1021/co200057n · Cited by 36
Brath, U., & Akke, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.047 · Cited by 36
Multi-timescale dynamics study of FKBP12 along the rapamycin–mTOR binding coordinate
Sapienza, P. J., Mauldin, R. V., & Lee, A. L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.037 · Cited by 32
Structure of the N-terminal domain of human FKBP52
Li, P., Ding, Y., Wu, B., Shu, C., Shen, B., & Rao, Z. (2003) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902017523 · Cited by 32
Peptidylprolylisomerases, Protein Folders, or Scaffolders? The Example of FKBP51 and FKBP52
Rein, T. (2020) · BioEssays · doi:10.1002/bies.201900250 · Cited by 25
Analysing the visible conformational substates of the FK506 binding protein FKBP12
Mustafi, S. M., Chen, H., Li, H., LeMaster, D. M., & Hernández, G. (2013) · Biochemical Journal · doi:10.1042/bj20130276 · Cited by 19
Mustafi, S. M., Brecher, M., Zhang, J., Li, H., Lemaster, D. M., & Hernández, G. (2014) · Biochemical Journal · doi:10.1042/bj20131429 · Cited by 15
Shihoya, W., Akasaka, H., Jordan, P. A., Lechner, A., Okada, B. K., Costa Machado da Cruz, G., Sano, F. K., Tanaka, T., Kawahara, R., Chaudhari, R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57960-x · Cited by 8
Ren, C., Wu, L., Zhang, S., Qi, K., Zhang, Y., Xu, J., Ruan, Y., & Feng, M. (2024) · Carcinogenesis · doi:10.1093/carcin/bgae028 · Cited by 5
Metadata
- Authors
- Griffith, J. P., Kim, J. L., Kim, E. E., Sintchak, M. D., Thomson, J. A., Fitzgibbon, M. J., Fleming, M. A., Caron, P. R., Hsiao, K., & Navia, M. A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-08
- Volume
- 82
- Issue
- 3
- Pages
- 507-522
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2080169144
- Cited by
- 834
- References
- 1
- FWCI
- 17.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.