The DOI matches its Crossref record; 42 of the 46 references it cites were found in a registry or an index.
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“their combined research revealed that these natural products remodeled their target proteins, a group of proteins named the immunophilins, recruiting novel interacting proteins to form entirely new ternary complexes (liu et al. 1991;Brown et al. 1994;Sabatini et al. 1994).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as Liu et al. 1991
In the citing paper
“Another example of an MG is Cyclosporin A, which forms a binary complex with cyclophilin able to bind and inhibit calcineurin.80,81”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [80]
Citations
Cites
Burnette, W. N. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90281-5 · Cited by 8,432
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-citationCyclophilin 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-citationPeptidyl-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
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
Klee, C. B., & VANAMAN, T. C. (1982) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60470-2 · Cited by 778
Research works printed but not linked: 1
- Klee, 1988, Calcineurin, Vol. 61, 149
Cited by
Sorted by citations
Items 201–300 of 1,027
Immunosuppressant FK506 promotes neurite outgrowth in cultures of PC12 cells and sensory ganglia.
Lyons, W. E., George, E. B., Dawson, T. M., Steiner, J. P., & Snyder, S. H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3191 · Cited by 286
Tacrolimus ointment for the treatment of atopic dermatitis in adult patients: Part I, efficacy
Hanifin, J. M., LING, M. R., Langley, R. G. B., Breneman, D., & Rafal, E. S. (2001) · Journal of the American Academy of Dermatology · doi:10.1067/mjd.2001.109810 · Cited by 285
Amelioration of Experimental Autoimmune Encephalomyelitis in Lewis Rats by FTY720 Treatment
Fujino, M., Funeshima, N., Kitazawa, Y., Kimura, H., Amemiya, H., Suzuki, S., & Li, X. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.045658 · Cited by 279
Cameron, A. M., Steiner, J. P., Sabatini, D. M., Kaplin, A. I., Walensky, L. D., & Snyder, S. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1784 · Cited by 279
Cyclophilin A regulates HIV‐1 infectivity, as demonstrated by gene targeting in human T cells
Braaten, D. C., & Luban, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1300 · Cited by 275
Belshaw, P. J., Ho, S. N., Crabtree, G. R., & Schreiber, S. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4604 · Cited by 278
Self-citationHuai, Q., Kim, H.-Y., Liu, Y., Zhao, Y., Mondragon, A., Liu, J. O., & Ke, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192206699 · Cited by 278
Self-citationBram, R. J., Hung, D. T., Martin, P. K., Schreiber, S. L., & Crabtree, G. R. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4760 · Cited by 275
Self-citationRegulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A
Brazin, K. N., Mallis, R. J., Fulton, D. B., & Andreotti, A. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042529199 · Cited by 275
Walsh, C. T., Zydowsky, L. D., & McKeon, F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42176-x · Cited by 274
Goul, C., Peruzzo, R., & Zoncu, R. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00641-8 · Cited by 280
S3 – Guidelines on the treatment of psoriasis vulgaris (English version). Update
Nast, A., Boehncke, W., Mrowietz, U., Ockenfels, H. M., Philipp, S., Reich, K., Rosenbach, T., Sammain, A., Schlaeger, M., Sebastian, M., et al. (2012) · JDDG Journal der Deutschen Dermatologischen Gesellschaft · doi:10.1111/j.1610-0387.2012.07919.x · Cited by 272
Effects of Serine/Threonine Protein Phosphatases on Ion Channels in Excitable Membranes
Herzig, S., & Neumann, J. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.1.173 · Cited by 272
Nakamura, T., Liu, Y., Hirata, D., Namba, H., Harada, S., Hirokawa, T., & Miyakawa, T. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06090.x · Cited by 270
CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A
Pushkarsky, T., Zybarth, G., Dubrovsky, L., Yurchenko, V., Tang, H., Guo, H., Toole, B. P., Sherry, B. A., & Bukrinsky, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111583198 · Cited by 270
Kaul, A., Stauffer, S., Berger, C., Pertel, T., Schmitt, J., Kallis, S., Zayas, M., Lohmann, V., Luban, J., & Bartenschlager, R. F. W. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000546 · Cited by 267
Prolyl Isomerases: Role in Protein Folding
Schmid, F. X., Mayr, L. M., Mücke, M., & Schönbrunner, E. R. (1993) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60563-x · Cited by 267
Physiologic Functions of Cyclophilin D and the Mitochondrial Permeability Transition Pore
Elrod, J. W., & Molkentin, J. D. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-0321 · Cited by 275
Superoxide dismutase protects calcineurin from inactivation
Wang, X., Culotta, V., & Klee, C. B. (1996) · Nature · doi:10.1038/383434a0 · Cited by 266
Okonkwo, D. O., & Povlishock, J. T. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199904000-00010 · Cited by 263
Multispecific drugs herald a new era of biopharmaceutical innovation
Deshaies, R. J. (2020) · Nature · doi:10.1038/s41586-020-2168-1 · Cited by 270
Calcineurin Controls Growth, Morphology, and Pathogenicity in Aspergillus fumigatus
Steinbach, W. J., Cramer, R. A., Perfect, B. Z., Asfaw, Y. G., Sauer, T. C., Najvar, L. K., Kirkpatrick, W. R., Patterson, T. F., Benjamin, D. K., Heitman, J., et al. (2006) · Eukaryotic Cell · doi:10.1128/ec.00139-06 · Cited by 264
Kowalski, R. J., Post, D. R., Schneider, M. C., Britz, J. A., Thomas, J. N., Deierhoi, M. H., Lobashevsky, A. L., Redfield, R. R., Schweitzer, E. J., Heredia, A., et al. (2003) · Clinical Transplantation · doi:10.1034/j.1399-0012.2003.00013.x · Cited by 261
Cianciotto, N. P., & Fields, B. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.11.5188 · Cited by 261
Dimeric ligands define a role for transcriptional activation domains in reinitiation
Ho, S. N., Biggar, S. R., Spencer, D. M., Schreiber, S. L., & Crabtree, G. R. (1996) · Nature · doi:10.1038/382822a0 · Cited by 261
Self-citationChemical remodeling of a cellular chaperone to target the active state of mutant KRAS
Schulze, C. J., Seamon, K. J., Zhao, Y., Yang, Y. C., Cregg, J., Kim, D., Tomlinson, A., Choy, T. J., Wang, Z., Sang, B., et al. (2023) · Science · doi:10.1126/science.adg9652 · Cited by 264
Potent Synergism of the Combination of Fluconazole and Cyclosporine in Candida albicans
Marchetti, O., Moreillon, P., Glauser, M. P., Bille, J., & Sanglard, D. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.9.2373-2381.2000 · Cited by 252
Cyclosporin A, FK506 and rapamycin: more than just immunosuppression
Kunz, J., & Hall, M. N. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90069-y · Cited by 258
Coordinate and cooperative roles for NF-AT and AP-1 in the regulation of the murine IL-4 gene
Rooney, J. W., Hoey, T. C., & Glimcher, L. H. (1995) · Immunity · doi:10.1016/1074-7613(95)90028-4 · Cited by 255
Sinars, C. R., Cheung-Flynn, J., Rimerman, R. A., Scammell, J. G., Smith, D. F., & Clardy, J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0231020100 · Cited by 254
Selective Binding of FKBP12.6 by the Cardiac Ryanodine Receptor
Timerman, A. P., Onoue, H., Xin, H.-B., Barg, S., Copello, J. A., Wiederrecht, G., & Fleischer, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20385 · Cited by 254
Regeneration in the metazoans: why does it happen?
Alvarado, A. S. (2000) · BioEssays · doi:10.1002/(sici)1521-1878(200006)22:6 · Cited by 342
Rapamycins: Antifungal, antitumor, antiproliferative, and immunosuppressive macrolides
Morris, R. E. (1992) · Transplantation Reviews · doi:10.1016/s0955-470x(10)80014-x · Cited by 253
Inhibition of Eukaryotic Translation Initiation by the Marine Natural Product Pateamine A
Low, W., Dang, Y., Schneider‐Poetsch, T., Shi, Z., Choi, N. S., Merrick, W. C., Romo, D., & Liu, J. O. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.008 · Cited by 252
Self-citationCalcineurin functions in Ca(2+)-activated cell death in mammalian cells.
Shibasaki, F., & McKeon, F. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.3.735 · Cited by 252
Tau protein phosphatases in Alzheimer's disease: The leading role of PP2A
Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., & Terro, F. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.008 · Cited by 265
Immunophilins in protein folding and immunosuppression 1
Fruman, D. A., Burakoff, S. J., & Bierer, B. E. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.6.7513288 · Cited by 249
Nghiem, P., Pearson, G., & Langley, R. G. B. (2002) · Journal of the American Academy of Dermatology · doi:10.1067/mjd.2002.120942 · Cited by 249
Immunosuppressants implicate protein phosphatase regulation of K+ channels in guard cells.
Luan, S., Li, W., Rusnak, F. M., Assmann, S. M., & Schreiber, S. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.6.2202 · Cited by 248
Self-citationGOTTSCHALK, A. R., Boise, L., Thompson, C. B., & Quintáns, J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7350 · Cited by 248
Gummert, J. F., Ikonen, T. S., & Morris, R. E. (1999) · Journal of the American Society of Nephrology · doi:10.1681/asn.v1061366 · Cited by 245
Current progress in antiviral strategies
Lou, Z., Sun, Y., & Rao, Z. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.11.006 · Cited by 246
Hirotani, H., Tuohy, N. A., Woo, J.-T., Stern, P. H., & Clipstone, N. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m213067200 · Cited by 248
Nadeau, K. C., Das, A., & Walsh, C. T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54100-4 · Cited by 245
Cabin 1, A Negative Regulator for Calcineurin Signaling in T Lymphocytes
Sun, L., Youn, H., Loh, C., Stolow, M. A., He, W.-W., & Liu, J. O. (1998) · Immunity · doi:10.1016/s1074-7613(00)80575-0 · Cited by 242
Self-citationSolution structure of the cyclosporin A/cyclophilin complex by NMR
Thériault, Y., Logan, T. M., Meadows, R., Yu, L. P., Olejniczak, E. T., Holzman, T. F., Simmer, R. L., & Fesik, S. W. (1993) · Nature · doi:10.1038/361088a0 · Cited by 242
Stathopoulos-Gerontides, A., Guo, J. J., & Cyert, M. S. (1999) · Genes & Development · doi:10.1101/gad.13.7.798 · Cited by 240
Immune response following traumatic spinal cord injury: Pathophysiology and therapies
Sterner, R. C., & Sterner, R. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1084101 · Cited by 258
Peptidylproline cis/trans isomerases
Gałat, A., & Metcalfe, S. M. (1995) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(94)00009-x · Cited by 240
Galigniana, M. D., Radanyi, C., Renoir, J.-M., Housley, P. R., & Pratt, W. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010809200 · Cited by 236
Zweifach, A., & Lewis, R. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14445 · Cited by 244
TOR Mutations Confer Rapamycin Resistance by Preventing Interaction with FKBP12-Rapamycin
Lorenz, M. C., & Heitman, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27531 · Cited by 236
Oligomerization activates c-Raf-1 through a Ras-dependent mechanism
Luo, Z., Tzivion, G., Belshaw, P. J., Vavvas, D. G., Marshall, M. S., & Avruch, J. (1996) · Nature · doi:10.1038/383181a0 · Cited by 238
Scleraxis and NFATc Regulate the Expression of the Pro-α1(I) Collagen Gene in Tendon Fibroblasts
Leéjard, V., Brideau, G., Blais, F., Ampornaramveth, R. S., Wagner, G., Roehrl, M. H. A., Noda, M., Duprez, D., Houillier, P., & Rossert, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610113200 · Cited by 239
Cyert, M., & Thorner, J. W. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.8.3460 · Cited by 236
Gold, B. G., Densmore, V. S., Shou, W., Matzuk, M. M., & Gordon, H. S. (1999) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)38260-6 · Cited by 236
Cyclophilin A Is a Proinflammatory Cytokine that Activates Endothelial Cells
Jin, Z., Lungu, A. O., Xie, L., Wang, M., Wong, C. N., & Berk, B. C. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000130664.51010.28 · Cited by 235
Tacrolimus ointment for the treatment of atopic dermatitis in adult patients: Part II, safety
Soter, N. A., Fleischer, A. B., WEBSTER, G. F., Monroe, E., & Lawrence, I. (2001) · Journal of the American Academy of Dermatology · doi:10.1067/mjd.2001.109817 · Cited by 234
Pellagatti, A., Jädersten, M., Forsblom, A., Cattan, H., Christensson, B., Emanuelsson, E. K., Merup, M., Nilsson, L., Samuelsson, J., Sander, B., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610477104 · Cited by 233
Calcineurin as a Multifunctional Regulator
Shibasaki, F., Hallin, U., & Uchino, H. (2002) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a003063 · Cited by 230
Yang, F., Robotham, J. M., Nelson, H. B., Irsigler, A., Kenworthy, R., & Tang, H. (2008) · Journal of Virology · doi:10.1128/jvi.02614-07 · Cited by 231
Pediatric liver transplantation
Spada, M., Riva, S., Maggiore, G., Cintorino, D., & Gridelli, B. G. (2009) · World Journal of Gastroenterology · doi:10.3748/wjg.15.648 · Cited by 231
Dittmar, M., Lee, J. S., Whig, K., Segrist, E., Li, M., Kamalia, B., Castellana, L., Ayyanathan, K., Cardenas‐Diaz, F. L., Morrisey, E. E., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108959 · Cited by 230
Cain, A Novel Physiologic Protein Inhibitor of Calcineurin
Lai, M. M.-S., Burnett, P. E., Wolosker, H., Blackshaw, S., & Snyder, S. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18325 · Cited by 225
Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A
Bosco, D. A., Eisenmesser, E. Z., Pochapsky, S. S., Sundquist, W. I., & Kern, D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082100499 · Cited by 226
NMR screening techniques in drug discovery and drug design
Stockman, B. J., & Dalvit, C. (2002) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(02)00049-3 · Cited by 229
The architecture of the interleukin-2 promoter: a reflection of T lymphocyte activation
Serfling, E., Avots, A., & Neumann, M. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(95)00112-t · Cited by 229
Host Control of HIV-1 Parasitism in T Cells by the Nuclear Factor of Activated T Cells
Kinoshita, S. M., Chen, B. K., Kaneshima, H., & Nolan, G. P. (1998) · Cell · doi:10.1016/s0092-8674(00)81630-x · Cited by 228
Medicinal Chemistry in the Golden Age of Biology: Lessons from Steroid and Peptide Research
Hirschmann, R. F. (1991) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199112781 · Cited by 227
Aggresome Formation and Neurodegenerative Diseases: Therapeutic Implications
Chin, L., Olzmann, J. A., & Li, L. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708783330692 · Cited by 233
Scheff, S. W., & Sullivan, P. G. (1999) · Journal of Neurotrauma · doi:10.1089/neu.1999.16.783 · Cited by 227
Rusting of the Lock and Key Model for Protein-Ligand Binding
Jorgensen, W. L. (1991) · Science · doi:10.1126/science.1719636 · Cited by 226
Target Cell Cyclophilin A Modulates Human Immunodeficiency Virus Type 1 Infectivity
Sokolskaja, E., Sayah, D. M., & Luban, J. (2004) · Journal of Virology · doi:10.1128/jvi.78.23.12800-12808.2004 · Cited by 218
Cell Signaling and Neuronal Death
Hara, M. R., & Snyder, S. H. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105311 · Cited by 228
RAPAMYCIN: CLINICAL RESULTS AND FUTURE OPPORTUNITIES1
Kahan, B. D., & Camardo, J. S. (2001) · Transplantation · doi:10.1097/00007890-200110150-00001 · Cited by 225
Zhu, C., Wang, X., Deinum, J., Huang, Z., Gao, J.-F., Modjtahedi, N., Neagu, M. R., Nilsson, M., Eriksson, P. S., Hagberg, H., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070193 · Cited by 224
Fischer, G. S., & Aumüller, T. (2003) · Springer eBooks · doi:10.1007/s10254-003-0011-3 · Cited by 225
Targeted protein degradation for cancer therapy
Hinterndorfer, M., Spiteri, V. A., Ciulli, A., & Winter, G. E. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00817-8 · Cited by 263
Signal Transduction Pathways in Apoptosis
McConkey, D. J., & Orrenius, S. (1996) · Stem Cells · doi:10.1002/stem.140619 · Cited by 223
Probing the Biology of Natural Products: Molecular Editing by Diverted Total Synthesis
Szpilman, A. M., & Carreira, E. M. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200904761 · Cited by 221
Colgan, J. D., Asmal, M., Neagu, M. R., Yu, B., Schneidkraut, J., Lee, Y., Sokolskaja, E., Andreotti, A. H., & Luban, J. (2004) · Immunity · doi:10.1016/j.immuni.2004.07.005 · Cited by 219
Pheromone Induces Programmed Cell Death in S. cerevisiae
Severin, F. F., & Hyman, A. A. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00776-5 · Cited by 219
Dumont, F. J., Staruch, M. J., Koprak, S. L., Siekierka, J. J., Lin, C. S., Harrison, R., Sewell, T., Kindt, V. M., Beattie, T. R., & Wyvratt, M. (1992) · The Journal of experimental medicine · doi:10.1084/jem.176.3.751 · Cited by 250
Chemoenzymatic and Template-Directed Synthesis of Bioactive Macrocyclic Peptides
Grünewald, J., & Marahiel, M. A. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.70.1.121-146.2006 · Cited by 218
Conceptual Evolution of Cell Signaling
Nair, A., Chauhan, P. S., Saha, B., & Kubatzky, K. F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133292 · Cited by 238
Butcher, S. P., Henshall, D. C., TERAMURA, Y., Iwasaki, K., & Sharkey, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-18-06939.1997 · Cited by 215
Kraus, P. R., Fox, D. S., Cox, G. M., & Heitman, J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03508.x · Cited by 217
Molecular Reactions of Protein PhosphatasesInsights from Structure and Chemistry
Jackson, M. D., & Denu, J. M. (2001) · Chemical Reviews · doi:10.1021/cr000247e · Cited by 217
Ermak, G., Morgan, T. E., & Davies, K. J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102829200 · Cited by 216
Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis
He, Z., Li, L., & Luan, S. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.031005 · Cited by 214
A Critical Review of Cyclosporine Therapy in Inflammatory Bowel Disease
Sandborn, W. J. (1995) · Inflammatory Bowel Diseases · doi:10.1002/ibd.3780010107 · Cited by 216
Paraptosis in the anti-cancer arsenal of natural products
Lee, D., Kim, I. Y., Saha, S., & Choi, K. S. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.01.003 · Cited by 216
Matsumoto, S., Friberg, H., Ferrand-Drake, M., & Wieloch, T. W. (1999) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199907000-00002 · Cited by 215
NFAT signaling in vertebrate development
Graef, I. A., Chen, F., & Crabtree, G. R. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00225-2 · Cited by 215
Mitochondrial Reactive Oxygen Species at the Heart of the Matter
Kornfeld, O. S., Hwang, S., Disatnik, M., Chen, C., Qvit, N., & Mochly‐Rosen, D. (2015) · Circulation Research · doi:10.1161/circresaha.116.305432 · Cited by 215
Nelson, M., & Chazin, W. (1998) · BioMetals · doi:10.1023/a:1009253808876 · Cited by 213
Cameron, A. M., Nucifora, F. C., Fung, E. T., Livingston, D. J., Aldape, R. A., Ross, C. A., & Snyder, S. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27582 · Cited by 212
Zhu, J., Wu, J., Frizell, E., Liu, S.-L., Bashey, R., Rubin, R., Norton, P., & Zern, M. (1999) · Gastroenterology · doi:10.1016/s0016-5085(99)70406-3 · Cited by 234
Current and emerging strategies for the prevention of graft-versus-host disease
Choi, S. W., & Reddy, P. R. (2014) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2014.102 · Cited by 216
Taglialatela, G., Hogan, D., Zhang, W.-R., & Dineley, K. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.12.034 · Cited by 217
Metadata
- 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)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1991-08
- Volume
- 66
- Issue
- 4
- Pages
- 807-815
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review