Cited by 4,116Signaling Pathways in DiseaseCalpain Protease Function and RegulationS100 Proteins and Annexins

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Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

Liu, Jun, Farmer, Jesse D., Lane, Willam S., Friedman, Jeff, Weissman, Irving, Schreiber, Stuart L.·1991·Cell

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Abstract

Although the immediate receptors (immunophilins) of the immunosuppressants cyclosporin A (CsA) and FK506 are distinct, their similar mechanisms of inhibition of cell signaling suggest that their associated immunophilin complexes interact with a common target. We report here that the complexes cyclophilin-CsA and FKBP-FK506 (but not cyclophilin, FKBP, FKBP-rapamycin, or FKBP-506BD) competitively bind to and inhibit the Ca(2+)- and calmodulin-dependent phosphatase calcineurin, although the binding and inhibition of calcineurin do not require calmodulin. These results suggest that calcineurin is involved in a common step associated with T cell receptor and IgE receptor signaling pathways and that cyclophilin and FKBP mediate the actions of CsA and FK506, respectively, by forming drug-dependent complexes with and altering the activity of calcineurin-calmodulin.

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“Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
Burnette, W. N. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90281-5 · Cited by 8,432
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,844
Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast
Heitman, J., Movva, N. R., & Hall, M. N. (1991) · Science · doi:10.1126/science.1715094 · Cited by 2,055
Cyclophilin: A Specific Cytosolic Binding Protein for Cyclosporin A
Handschumacher, R. E., Harding, M. W., Rice, J. S., Drugge, R. J., & Speicher, D. W. (1984) · Science · doi:10.1126/science.6238408 · Cited by 1,675
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Schreiber, S. L. (1991) · Science · doi:10.1126/science.1702904 · Cited by 1,494
Self-citation
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
Fischer, G., Wittmann‐Liebold, B., Lang, K., Kiefhaber, T., & Schmid, F. X. (1989) · Nature · doi:10.1038/337476a0 · Cited by 1,408
A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase
Harding, M. W., Gałat, A., Uehling, D., & Schreiber, S. L. (1989) · Nature · doi:10.1038/341758a0 · Cited by 1,396
Self-citation
Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
Takahashi, N., Hayano, T., & Suzuki, M. (1989) · Nature · doi:10.1038/337473a0 · Cited by 1,075
A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
Siekierka, J. J., Hung, S. H. Y., Poe, M., Lin, C. S., & SIGAL, N. H. (1989) · Nature · doi:10.1038/341755a0 · Cited by 1,016
Calmodulin
Klee, C. B., & VANAMAN, T. C. (1982) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60470-2 · Cited by 778

Show all 46 references

Research works printed but not linked: 1

Klee, 1988, Calcineurin, Vol. 61, 149

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Bayle, J. H., Grimley, J. S., Stankunas, K., Gestwicki, J. E., Wandless, T. J., & Crabtree, G. R. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.10.017 · Cited by 211
The role of NF-AT transcription factors in T cell activation and differentiation11We dedicate this review to Prof. Dr. Rigomar Rieger (Gatersleben), a great scientist and man, on the occasion of his 70th birthday. One of us (E.S.) had the pleasure of working in his department.
Serfling, E., Berberich‐Siebelt, F., Chuvpilo, S. A., Jankevics, E., Klein‐Hessling, S., Twardzik, T., & Avots, A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00082-3 · Cited by 213
How self-tolerance and the immunosuppressive drug FK506 prevent B-cell mitogenesis
Glynne, R. J., Akkaraju, S., Healy, J. I., Rayner, J., Goodnow, C. C., & Mack, D. H. (2000) · Nature · doi:10.1038/35001102 · Cited by 210
Calcineurin Inhibition of Dynamin I GTPase Activity Coupled to Nerve Terminal Depolarization
Liu, J., Sim, A. T. R., & Robinson, P. J. (1994) · Science · doi:10.1126/science.8052858 · Cited by 210
Self-citation
Discovery of a molecular glue promoting CDK12-DDB1 interaction to trigger cyclin K degradation
Lv, L., Chen, P., Cao, L., Li, Y., Zeng, Z., Cui, Y., Wu, Q., Li, J., Wang, J.-H., Dong, M.-Q., et al. (2020) · eLife · doi:10.7554/elife.59994 · Cited by 215
Total synthesis of the-potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology
Sin, N., Kim, K. B., Elofsson, M., Meng, L., Auth, H., Kwok, B. H. B., & Crews, C. M. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00376-5 · Cited by 209
Axonal Degeneration Is Mediated by the Mitochondrial Permeability Transition Pore
Barrientos, S. A., Martínez, N. W., Yoo, S., Jara, J. S., Zamorano, S., Hetz, C. A., Twiss, J. L., Álvarez, J., & Court, F. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4065-10.2011 · Cited by 214
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Thiel, P., Kaiser, M., & Ottmann, C. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201107616 · Cited by 214
Lipid transport by TMEM24 at ER–plasma membrane contacts regulates pulsatile insulin secretion
Lees, J. A., Messa, M., Sun, E. W., Wheeler, H., Torta, F. T., Wenk, M. R., Camilli, P. V. D., & Reinisch, K. M. (2017) · Science · doi:10.1126/science.aah6171 · Cited by 208
Molecular chaperone interactions with steroid receptors: an update.
Cheung, J., & Smith, D. F. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.7.0489 · Cited by 198
The Loss of Cytoplasmic Potassium upon Host Cell Breakdown Triggers Egress of Toxoplasma gondii
Moudy, R. M., Manning, T. J., & Beckers, C. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106154200 · Cited by 204
Proximity-Based Modalities for Biology and Medicine
Liu, X., & Ciulli, A. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00395 · Cited by 206
Downregulation of Ca2+ and Mg2+ Transport Proteins in the Kidney Explains Tacrolimus (FK506)-Induced Hypercalciuria and Hypomagnesemia
Nijenhuis, T., Hoenderop, J. G. J., & Bindels, R. J. M. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000113318.56023.b6 · Cited by 203
High-throughput screening of small molecules in miniaturized mammalian cell-based assays involving post-translational modifications
Stockwell, B. R., Haggarty, S. J., & Schreiber, S. L. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80004-0 · Cited by 203
Self-citation
Ca2+-dependent Gene Expression Mediated by MEF2 Transcription Factors
Blaeser, F., Ho, N. Y., Prywes, R., & Chatila, T. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.197 · Cited by 203
Cell Surface Structures on Human Basophils and Mast Cells: Biochemical and Functional Characterization
Valent, P., & Bettelheim, P. (1992) · Advances in immunology · doi:10.1016/s0065-2776(08)60879-2 · Cited by 204
A CaMKII/Calcineurin Switch Controls the Direction of Ca2+-Dependent Growth Cone Guidance
Wen, Z., Guirland, C., Ming, G., & Zheng, J. Q. (2004) · Neuron · doi:10.1016/j.neuron.2004.08.037 · Cited by 195
Regulation of Lymphocyte Function by Protein Phosphorylation
Perlmutter, R. M., Levin, S. D., Appleby, M. W., Anderson, S., & Alberola‐Ila, J. (1993) · Annual Review of Immunology · doi:10.1146/annurev.immunol.11.1.451 · Cited by 202
Hedgehog Signaling Restrains Bladder Cancer Progression by Eliciting Stromal Production of Urothelial Differentiation Factors
Shin, K., Lim, A. Y.-L., Zhao, C., Sahoo, D., Pan, Y., Spiekerkoetter, E. F., Liao, J. C., & Beachy, P. A. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.09.001 · Cited by 200
Capsaicin and pain mechanisms
Winter, J., Bevan, S., & Campbell, E. A. (1995) · British Journal of Anaesthesia · doi:10.1093/bja/75.2.157 · Cited by 200
Identification of a novel cyclosporin-sensitive element in the human tumor necrosis factor alpha gene promoter.
Goldfeld, A. E., McCaffrey, P. G., Strominger, J. L., & Rao, A. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.178.4.1365 · Cited by 197
Unifying principles of bifunctional, proximity-inducing small molecules
Gerry, C. J., & Schreiber, S. L. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0469-1 · Cited by 199
Self-citation
Two essential regulatory elements in the human interferon gamma promoter confer activation specific expression in T cells.
Penix, L. A., Weaver, W. M., Pang, Y., Young, H. A., & Wilson, C. B. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.178.5.1483 · Cited by 199
Molecular Chaperones: Biology and Prospects for Pharmacological Intervention
Smith, D. F., Whitesell, L. J., & Katsanis, E. (1998) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01380-2 · Cited by 199
Calcium ions as second messengers in guard cell signal transduction
McAinsh, M. R., Brownlee, C., & Hetherington, A. M. (1997) · Physiologia Plantarum · doi:10.1034/j.1399-3054.1997.1000102.x · Cited by 198
Neural actions of immunophilin ligands
Snyder, S. H., Sabatini, D. M., Lai, M. M.-S., Steiner, J. P., Hamilton, G. S., & Suzdak, P. D. (1998) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)01146-2 · Cited by 198
High-dose, post-transplantation cyclophosphamide to promote graft-host tolerance after allogeneic hematopoietic stem cell transplantation
Luznik, L., & Fuchs, E. J. (2010) · Immunologic Research · doi:10.1007/s12026-009-8139-0 · Cited by 196
Spatiotemporal Dynamics of CREB Phosphorylation: Transient versus Sustained Phosphorylation in the Developing Striatum
Liu, F., & Graybiel, A. M. (1996) · Neuron · doi:10.1016/s0896-6273(00)80245-7 · Cited by 198
Yeast Protein Serine/Threonine Phosphatases: Multiple Roles and Diverse Regulation
Stark, M. J. R. (1996) · Yeast · doi:10.1002/(sici)1097-0061(199612)12:16 · Cited by 201
RelA/p65 is a molecular target for the immunosuppressive action of protein kinase A.
Neumann, M., Grieshammer, T., Chuvpilo, S. A., Kneitz, B., Lohoff, M. D., Schimpl, A., Franza, B. R., & Serfling, E. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07191.x · Cited by 195
Physiologic importance of protein phosphatase inhibitors
Shenolikar, S. (1998) · Frontiers in bioscience · doi:10.2741/a336 · Cited by 194
Calcineurin: Structure, function, and inhibition
Hemenway, C. S., & Heitman, J. (1999) · Cell Biochemistry and Biophysics · doi:10.1007/bf02737887 · Cited by 227
Calcineurin mediates alpha-adrenergic stimulation of Na+,K(+)-ATPase activity in renal tubule cells.
Aperia, A., Ibarra, F. R., Svensson, L. B., Klee, C., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7394 · Cited by 191
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200
Natural products as immunosuppressive agents
Mann, J. (2001) · Natural Product Reports · doi:10.1039/b001720p · Cited by 192
NFAT signaling and the invention of vertebrates
Wu, H., Peisley, A., Graef, I. A., & Crabtree, G. R. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.04.006 · Cited by 196
Calcineurin mediates inhibition by FK506 and cyclosporin of recovery from α-factor arrest in yeast
Poor, F., Parent, S. A., Morin, N. R., Dahl, A., Ramadan, N., Chrebet, G. L., Bostian, K. A., & NIELSEN, J. B. K. (1992) · Nature · doi:10.1038/360682a0 · Cited by 192
Quantitative proteomics approach for identifying protein–drug interactions in complex mixtures using protein stability measurements
West, G. M., Tucker, C. L., Xu, T., Park, S. K., Han, X., Yates, J. R., & Fitzgerald, M. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000148107 · Cited by 189
Efficient Delivery of Cyclic Peptides into Mammalian Cells with Short Sequence Motifs
Qian, Z., Liu, T., Liu, Y., Briesewitz, R., Barrios, A. M., Jhiang, S. M., & Pei, D. (2012) · ACS Chemical Biology · doi:10.1021/cb3005275 · Cited by 191
Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
Connern, C. P., & Halestrap, A. P. (1992) · Biochemical Journal · doi:10.1042/bj2840381 · Cited by 191
FK506 and the role of immunophilins in nerve regeneration
Gold, B. G. (1997) · Molecular Neurobiology · doi:10.1007/bf02740664 · Cited by 191
Inhibition of Neutrophil Chemokinesis on Vitronectin by Inhibitors of Calcineurin
Hendey, B., Klee, C. B., & Maxfield, F. R. (1992) · Science · doi:10.1126/science.1384129 · Cited by 191
Natively Disordered Proteins
Daughdrill, G. W., Pielak, G. J., Uversky, V. N., Cortese, M. S., & Dunker, A. K. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch41 · Cited by 196
T cell activation induces a noncoding RNA transcript sensitive to inhibition by immunosuppressant drugs and encoded by the proto-oncogene, BIC
Haasch, D. L., Chen, Y., Reilly, R. M., Chiou, X. G., Koterski, S., Smith, M. L., Kroeger, P., McWeeny, K., Halbert, D. N., Mollison, K. W., et al. (2002) · Cellular Immunology · doi:10.1016/s0008-8749(02)00506-3 · Cited by 189
IN VIVO EXPRESSION OF TRANSFORMING GROWTH FACTOR-??1 IN HUMANS
Shin, G., Khanna, A. K., Ding, R., Sharma, V. K., Lagman, M., Li, B., & Suthanthiran, M. (1998) · Transplantation · doi:10.1097/00007890-199802150-00003 · Cited by 190
Immunophilins and nervous system
Snyder, S. H., & Sabatini, D. M. (1995) · Nature Medicine · doi:10.1038/nm0195-32 · Cited by 186
Defective T cell development and function in calcineurin Aβ-deficient mice
Bueno, O. F., Brandt, E. B., Rothenberg, M. E., & Molkentin, J. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152665399 · Cited by 188
Mitochondrial dysfunction in the pathogenesis of Ullrich congenital muscular dystrophy and prospective therapy with cyclosporins
Angelin, A., Tiepolo, T., Sabatelli, P., Grumati, P., Bergamin, N., Golfieri, C., Mattioli, E., Gualandi, F., Ferlini, A., Merlini, L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610270104 · Cited by 189
The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)
Ratajczak, T., Carrello, A., Mark, P. J., Warner, B., Simpson, R. J., Moritz, R. L., & House, A. K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38636-3 · Cited by 187
Calcineurin Is Essential for Candida albicans Survival in Serum and Virulence
Blankenship, J. R., Wormley, F. L., Boyce, M. K., Schell, W. A., Filler, S. G., Perfect, J. R., & Heitman, J. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.3.422-430.2003 · Cited by 186
Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein
Silverstein, A. M., Galigniana, M. D., Kanelakis, K. C., Radanyi, C., Renoir, J.-M., & Pratt, W. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.36980 · Cited by 186
Comparison of acute rapamycin nephrotoxicity with cyclosporine and FK506
Andoh, T. F., Burdmann, E. A., Fransechini, N., Houghton, D. C., & Wm, B. (1996) · Kidney International · doi:10.1038/ki.1996.417 · Cited by 186
Multiple closely-linked NFAT/octamer and HMG I(Y) binding sites are part of the interleukin-4 promoter
Chuvpilo, S. A., Schomberg, C., Gerwig, R., Heinfling, A., Reeves, R., Grummt, F., & ling, E. S. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.24.5694 · Cited by 186
Cyclosporin A and FK506: molecular mechanisms of immunosuppression and probes for transplantation biology
Bierer, B. E., Holländer, G. A., Fruman, D., & Burakoff, S. J. (1993) · Current Opinion in Immunology · doi:10.1016/0952-7915(93)90135-f · Cited by 184
Understanding and controlling the cell cycle with natural products
Hung, D. T., Jamison, T. F., & Schreiber, S. L. (1996) · Chemistry & Biology · doi:10.1016/s1074-5521(96)90129-5 · Cited by 183
Self-citation
Inhibition of human immunodeficiency virus type 1 replication by SDZ NIM 811, a nonimmunosuppressive cyclosporine analog
Rosenwirth, B., Billich, A., DATEMA, R., Donatsch, P., Hammerschmid, F., Harrison, R. K., HIESTAND, P. C., Jaksche, H., Mayer, P. E., & Peichl, P. (1994) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.38.8.1763 · Cited by 184
Regulation of Membrane‐Type Matrix Metalloproteinase‐1 Expression by Growth Factors and Phorbol 12‐Myristate 13‐Acetate
Lohi, J., Lehti, K., Westermarck, J. K., Kähäri, V., & Keski‐Oja, J. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0239u.x · Cited by 185
Immunophilins in the Nervous System
Snyder, S. H., Lai, M. M.-S., & Burnett, P. E. (1998) · Neuron · doi:10.1016/s0896-6273(00)80538-3 · Cited by 181
Lymphocyte calcium signaling from membrane to nucleus
Gallo, E. M., Canté-Barrett, K., & Crabtree, G. R. (2005) · Nature Immunology · doi:10.1038/ni1295 · Cited by 188
Effects of Rapamycin on Ryanodine Receptor/Ca 2+ -Release Channels From Cardiac Muscle
Kaftan, E. J., Marks, A. R., & Ehrlich, B. E. (1996) · Circulation Research · doi:10.1161/01.res.78.6.990 · Cited by 182
The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane.
Wieland, J., Nitsche, A. M., Strayle, J., Steiner, H., & Rudolph, H. K. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00059.x · Cited by 183
Enhancement of Cytokine Production and AP-1 Transcriptional Activity in T Cells by Thalidomide-Related Immunomodulatory Drugs
Schafer, P. H., Gandhi, A. K., Loveland, M. A., Chen, R. S., Man, H., Schnetkamp, P. P. M., Wolbring, G., Govinda, S., Corral, L. G., Payvandi, F., et al. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.048496 · Cited by 182
The development and therapeutic potential of protein kinase inhibitors.
Cohen, P. R. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80067-2 · Cited by 178
Ammonia induces the mitochondrial permeability transition in primary cultures of rat astrocytes
Bai, G., Rao, K. V. R., Murthy, C. R. K., Panickar, K. S., Jayakumar, A. R., & Norenberg, M. D. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10056 · Cited by 182
Immunosuppression after traumatic or ischemic CNS damage: It is neuroprotective and illuminates the role of microglial cells
Hailer, N. P. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.12.001 · Cited by 181
Visualizing biologically active small molecules in cells using click chemistry
Cañeque, T., Müller, S., & Rodriguez, R. (2018) · Nature Reviews Chemistry · doi:10.1038/s41570-018-0030-x · Cited by 185
Mitochondrial Targeted Cyclophilin D Protects Cells from Cell Death by Peptidyl Prolyl Isomerization
Lin, D.-T., & Lechleiter, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112035200 · Cited by 181
Cyclophilin D in mitochondrial pathophysiology
Giorgio, V., Soriano, M. E., Basso, E., Bisetto, E., Lippe, G., Forte, M. A., & Bernardi, P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.006 · Cited by 179
Dealing with the family: CD147 interactions with cyclophilins
Yurchenko, V., Constant, S. L., & Bukrinsky, M. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02316.x · Cited by 180
Comparative Dose-Dependence Study of FK506 and Cyclosporin A on the Rate of Axonal Regeneration in the Rat Sciatic Nerve
Wang, M.-S., Zeleny-Pooley, M., & Gold, B. G. (1997) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)36886-7 · Cited by 180
The peripheral nerve allograft: A comprehensive review of regeneration and neuroimmunology
Evans, P. J., Midha, R., & Mackinnon, S. E. (1994) · Progress in Neurobiology · doi:10.1016/0301-0082(94)90001-9 · Cited by 180
Nucleocytoplasmic Shuttling Factors Including Ran and CRM1 Mediate Nuclear Export of NFAT In Vitro
Kehlenbach, R. H., Dickmanns, A., & Gerace, L. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.863 · Cited by 180
Rapamycin-induced inhibition of p34cdc2 kinase activation is associated with G1/S-phase growth arrest in T lymphocytes.
Morice, W. G., Brunn, G. J., Wiederrecht, G., Siekierka, J. J., & Abraham, R. T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53755-8 · Cited by 180
Germinal center responses to SARS-CoV-2 mRNA vaccines in healthy and immunocompromised individuals
(2022) · doi:10.1016/j.cell.2022.01.027 · Cited by 179
A Magnaporthe grisea Cyclophilin Acts as a Virulence Determinant during Plant Infection
Viaud, M., Balhadère, P. V., & Talbot, N. J. (2002) · The Plant Cell · doi:10.1105/tpc.010389 · Cited by 177
Calcineurin regulatory subunit is essential for virulence and mediates interactions with FKBP12–FK506 in Cryptococcus neoformans
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
Microbial Peptidyl-Prolyl cis / trans Isomerases (PPIases): Virulence Factors and Potential Alternative Drug Targets
Ünal, C., & Steinert, M. (2014) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00015-14 · Cited by 174
Systematic Review and Metaanalysis of the Efficacy of FK506 in Experimental Stroke
Macleod, M. R., O’Collins, T., Horky, L. L., Howells, D. W., & Donnan, G. A. (2005) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600064 · Cited by 176
Antifungal drug resistance evoked via RNAi-dependent epimutations
Calo, S., Shertz-Wall, C., Lee, S. C., Bastidas, R. J., Nicolás, F. E., Granek, J. A., Mieczkowski, P., Torres-Martínez, S., Ruiz-Vázquez, R. M., Cardenas, M. E., et al. (2014) · Nature · doi:10.1038/nature13575 · Cited by 175
FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition
Baughman, G., Wiederrecht, G. J., Campbell, N. F., Martin, M. M., & Bourgeois, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4395 · Cited by 173
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
Selective inhibition of calcineurin-NFAT signaling by blocking protein–protein interaction with small organic molecules
Roehrl, M. H. A., Kang, S., Aramburu, J., Wagner, G., Rao, A., & Hogan, P. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401835101 · Cited by 177
Targeting Protein Serine/Threonine Phosphatases for Drug Development
McConnell, J. L., & Wadzinski, B. E. (2009) · Molecular Pharmacology · doi:10.1124/mol.108.053140 · Cited by 175
Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporin A analog with activity against human immunodeficiency virus (HIV) type 1: interference with HIV protein-cyclophilin A interactions
Billich, A., Hammerschmid, F., Peichl, P., Wenger, R., Zenke, G., Quesniaux, V., & Rosenwirth, B. (1995) · Journal of Virology · doi:10.1128/jvi.69.4.2451-2461.1995 · Cited by 170
Interaction of calcineurin with a domain of the transcription factor NFAT1 that controls nuclear import.
Luo, C. H., Shaw, K. T. Y., Raghavan, A., Aramburu, J. F., Garcia-Cozar, F. J., Perrino, B. A., Hogan, P. G., & Rao, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.17.8907 · Cited by 175
Targeting virulence: A new paradigm for antifungals
Gauwerky, K. J., Borelli, C., & Körting, H. C. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2008.11.013 · Cited by 174
Inflammatory bowel disease biomarkers
Liu, D., Saikam, V., Skrada, K. A., Merlin, D., & Iyer, S. S. (2022) · Medicinal Research Reviews · doi:10.1002/med.21893 · Cited by 183
Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.
Zhuo, S., Clemens, J. C., Hakes, D. J., Barford, D., & Dixon, J. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46769-x · Cited by 174
Studies on the Mechanism of Resistance to Rapamycin in Human Cancer Cells
Hosoi, H., Dilling, M. B., Liu, L. N., Danks, M. K., Shikata, T., Sekulic, A., Abraham, R. T., Lawrence, J. C., & Houghton, P. J. (1998) · Molecular Pharmacology · doi:10.1124/mol.54.5.815 · Cited by 173
Calcineurin Target CrzA Regulates Conidial Germination, Hyphal Growth, and Pathogenesis of Aspergillus fumigatus
Cramer, R. A., Perfect, B. Z., Pinchai, N., Park, S., Perlin, D. S., Asfaw, Y. G., Heitman, J., Perfect, J. R., & Steinbach, W. J. (2008) · Eukaryotic Cell · doi:10.1128/ec.00086-08 · Cited by 172
The Genome of Tolypocladium inflatum: Evolution, Organization, and Expression of the Cyclosporin Biosynthetic Gene Cluster
Bushley, K. E., Raja, R., Jaiswal, P., Cumbie, J. S., Nonogaki, M., Boyd, A. E., Quandt, C. A., Knaus, B. J., Elser, J. L., Miller, D., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003496 · Cited by 171
Calcineurin Plays Key Roles in the Dimorphic Transition and Virulence of the Human Pathogenic Zygomycete Mucor circinelloides
Lee, S. C., Li, A., Calo, S., & Heitman, J. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003625 · Cited by 175
Solution‐Phase Combinatorial Libraries: Modulating Cellular Signaling by Targeting Protein–Protein or Protein–DNA Interactions
Boger, D. L., Desharnais, J., & Capps, K. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200300574 · Cited by 172
Identification and characterization of a highly conserved calcineurin binding protein, CBP1/calcipressin, in Cryptococcus neoformans
Görlach, J. M., Fox, D. S., Cutler, N. S., Cox, G. M., Perfect, J. R., & Heitman, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.14.3618 · Cited by 172
Cyclosporine A and adverse effects on organs: histochemical studies
Rezzani, R. (2004) · Progress in Histochemistry and Cytochemistry · doi:10.1016/j.proghi.2004.04.001 · Cited by 170
NFATc3, a Lymphoid-specific NFATc Family Member That Is Calcium-regulated and Exhibits Distinct DNA Binding Specificity
Ho, S. N., Thomas, D. J., Timmerman, L., Li, X., Francke, U., & Crabtree, G. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.19898 · Cited by 167
Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B
Hanoulle, X., Badillo, A., Wieruszeski, J., Verdegem, D., Landrieu, I., Bartenschlager, R. F. W., Pénin, F., & Lippens, G. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809244200 · Cited by 168
The mitochondrial permeability transition in neurologic disease
Norenberg, M. D., & RAO, K. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.02.008 · Cited by 168
The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease
Fries, G. R., Gassen, N. C., & Rein, T. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122614 · Cited by 170
The NFAT-Related Protein NFATL1 (TonEBP/NFAT5) Is Induced Upon T Cell Activation in a Calcineurin-Dependent Manner
Trama, J. P., Lu, Q., Hawley, R. G., & Ho, S. N. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.9.4884 · Cited by 170

Authors: Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L.
Affiliations: Harvard University (US)
Howard Hughes Medical Institute (US)
ORCID: Weissman, Irving
Schreiber, Stuart L.
Venue: Cell
Publisher: Elsevier BV
Published: 1991-08
Volume: 66
Issue: 4
Pages: 807-815
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(91)90124-h
OpenAlex: W1984754431
Cited by: 4,116
References: 46
Citations by year: 2026: 61 · 2025: 90 · 2024: 68 · 2023: 104 · 2022: 78 · 2021: 84 · 2020: 96 · 2019: 77 · 2018: 76 · 2017: 74 · 2016: 95 · 2015: 101 · 2014: 106 · 2013: 111 · 2012: 115
FWCI: 63.40
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: American Cancer Society
Damon Runyon Cancer Research Foundation
National Institutes of Health (5p01gm040660-02)
National Cancer Institute (T32CA009302)
National Institute of General Medical Sciences (GM-40660, GM38627)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Keywords: calcineurin, cyclophilin, cyclosporine, FKBP, FK506, immunophilins, immunosuppressants, T cell receptor signaling, IgE receptor signaling
MeSH terms: Amino Acid Isomerases, Amino Acid Sequence, Animals, Anti-Bacterial Agents, Base Sequence, Calmodulin, Calmodulin-Binding Proteins, Carrier Proteins, Cations, Divalent, Cloning, Molecular, Cyclosporins, Humans, Immunosuppressive Agents, Molecular Sequence Data, Molecular Weight, Oligonucleotides, Oligopeptides, Phosphoprotein Phosphatases, Polyenes, Protein Binding, Tacrolimus, Peptidylprolyl Isomerase, Calcineurin, Sirolimus, Tacrolimus Binding Proteins, Macromolecular Substances, Mice, In Vitro Techniques

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Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

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