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

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

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

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1016/0092-8674(91)90124-h

Cites

42 of 42 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

“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

Sorted by citations

Items 901–1,000 of 1,027

Rabbit FKBP59-heat shock protein binding immunophillin (HBI) is a calmodulin binding protein
Massol, N., Lebeau, M., Renoir, J., Faber, L. E., & Baulieu, É.-É. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90448-t · Cited by 79
Identifying New Substrates and Functions for an Old Enzyme: CalcineurinPreprint
Roy, J., & Cyert, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a035436 · Cited by 81
Epidemiologic and clinical characteristics of heart transplant recipients during the 2019 coronavirus outbreak in Wuhan, China: A descriptive survey report
Ren, Z., Hu, R., Wang, Z., Zhang, M., Ruan, Y., Wu, Z., Wu, H., Hu, X.-P., Hu, Z., Ren, W., et al. (2020) · The Journal of Heart and Lung Transplantation · doi:10.1016/j.healun.2020.03.008 · Cited by 78
Profiling humoral autoimmune repertoire of dilated cardiomyopathy (DCM) patients and development of a disease‐associated protein chip
Horn, S., Lueking, A., Murphy, D. B., Staudt, A., Gutjahr, C., Schulte, K., König, A. A., Landsberger, M., Lehrach, H., Felix, S. B., et al. (2006) · PROTEOMICS · doi:10.1002/pmic.200401293 · Cited by 77
Nerve Allotransplantation as it Pertains to Composite Tissue Transplantation
Moore, A. M., Ray, W. Z., Chenard, K. E., Tung, T. H. H., & Mackinnon, S. E. (2009) · Hand · doi:10.1007/s11552-009-9183-x · Cited by 78
N‐Methylierung von Peptiden und Proteinen: ein wichtiges Element für die Regulation biologischer Funktionen
Chatterjee, J., Rechenmacher, F., & Kessler, H. (2012) · Angewandte Chemie · doi:10.1002/ange.201205674 · Cited by 78
Loss of Apm1, the μ1 Subunit of the Clathrin-Associated Adaptor-Protein-1 Complex, Causes Distinct Phenotypes and Synthetic Lethality with Calcineurin Deletion in Fission Yeast
Kita, A., Sugiura, R., Shoji, H., He, Y., Deng, L., Lü, Y., Sio, S. O., Takegawa, K., Sakaue, M., Shuntoh, H., et al. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0659 · Cited by 78
Peptidyl‐prolyl isomerase inhibitors
Wang, X. J., & Etzkorn, F. A. (2005) · Biopolymers · doi:10.1002/bip.20240 · Cited by 78
Neuroimaging findings in patients on immunosuppressive therapy: experience with tacrolimus toxicity.
Appignani, B. A., Bhadelia, R. A., Blacklow, S. C., Wang, A., Roland, S. F., & Freeman, R. B. (1996) · American Journal of Roentgenology · doi:10.2214/ajr.166.3.8623651 · Cited by 78
Cyclosporin A inhibits Ca2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells.
Groblewski, G. E., Wagner, A. C. C., & Williams, J. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36580-8 · Cited by 78
A Chemical Biology View of Bioactive Small Molecules and a Binder‐Based Approach to Connect Biology to Precision Medicines
Schreiber, S. L. (2018) · Israel Journal of Chemistry · doi:10.1002/ijch.201800113 · Cited by 78
Self-citation
The immunophilin FKBP12: a molecular guardian of the TGF-beta family type I receptors
Wang, T. (2004) · Frontiers in bioscience · doi:10.2741/1095 · Cited by 77
Calcineurin dephosphorylates glycogen synthase kinase‐3 beta at serine‐9 in neuroblast‐derived cells
Kim, Y., Lee, Y., Seo, M., Kim, S., Lee, J., Youn, H., Kim, Y. S., & Juhnn, Y. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06318.x · Cited by 80
Control of the phosphorylation of the astrocyte marker glial fibrillary acidic protein (GFAP) in the immature rat hippocampus by glutamate and calcium ions: possible key factor in astrocytic plasticity
Rodnight, R., Gonçalves, C. A., Wofchuk, S. T., & Leal, R. B. (1997) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x1997000300005 · Cited by 77
Affinity-based target identification for bioactive small molecules
Kawatani, M., & Osada, H. (2013) · MedChemComm · doi:10.1039/c3md00276d · Cited by 78
A general strategy for producing conditional alleles of Src-like tyrosine kinases.
Spencer, D. M., Graef, I. A., Austin, D. J., Schreiber, S. L., & Crabtree, G. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9805 · Cited by 77
Self-citation
Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs
Lam, E., Martin, M. M., & Wiederrecht, G. (1995) · Gene · doi:10.1016/0378-1119(95)00216-s · Cited by 77
Neuroprotection by cyclosporin A following transient brain ischemia correlates with the inhibition of the early efflux of cytochrome C to cytoplasm
Domańska‐Janik, K., Bużańska, L., Dłużniewska, J., Kozłowska, H., Sarnowska, A., & Zabłocka, B. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2003.11.006 · Cited by 77
Immunophilin Ligands and GDNF Enhance Neurite Branching or Elongation from Developing Dopamine Neurons in Culture
Costantini, L. C., & Ole Isacson, A. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7417 · Cited by 77
Mitochondrial Dysfunction and Defective Autophagy in the Pathogenesis of Collagen VI Muscular DystrophiesPreprint
Bernardi, P., & Bonaldo, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011387 · Cited by 78
Autoimmune/inflammatory syndrome induced by adjuvants—ASIA—related to biomaterials: analysis of 45 cases and comprehensive review of the literature
Alijotas‐Reig, J., Esteve‐Valverde, E., Gil-Aliberas, N., & Garcia-Gimenez, V. (2017) · Immunologic Research · doi:10.1007/s12026-017-8980-5 · Cited by 76
Advancing targeted protein degradation for metabolic diseases therapy
Zhou, Q., Xiao, H., Yang, F., Wang, Y., Li, P., & Zheng, Z. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106627 · Cited by 77
Differential effects of the immunosuppressive agents cyclosporin A, tacrolimus and sirolimus on drug transport by multidrug resistance proteins
Pawarode, A., Shukla, S., Minderman, H., Fricke, S. M., Pinder, E., O’Loughlin, K. L., Ambudkar, S. V., & Baer, M. R. (2006) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-006-0357-8 · Cited by 76
Molecular characterization of a plant FKBP12 that does not mediate action of FK506 and rapamycin
Xu, Q., Liang, S., Kudla, J., & Sheng, L. (1998) · The Plant Journal · doi:10.1046/j.1365-313x.1998.00232.x · Cited by 76
Structure and expression of two isoforms of the murine calmodulin-dependent protein phosphatase regulatory subunit (calcineurin B)
Ueki, K., Muramatsu, T., & Kincaid, R. L. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81527-x · Cited by 76
Light-regulated, tissue-specific immunophilins in a higher plant.
Luan, S., Albers, M. W., & Schreiber, S. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.984 · Cited by 76
Self-citation
Proximity and orientation underlie signaling by the non‐receptor tyrosine kinase ZAP70
Graef, I. A., Holsinger, L. J., Diver, S., Schreiber, S. L., & Crabtree, G. R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5618 · Cited by 76
Self-citation
Peptidyl-Prolyl Isomerase FKBP52 Controls Chemotropic Guidance of Neuronal Growth Cones via Regulation of TRPC1 Channel Opening
Shim, S., Yuan, J. P., Kim, J. Y., Zeng, W., Huang, G. N., Milshteyn, A., Kern, D., Muallem, S., Ming, G., & Worley, P. F. (2009) · Neuron · doi:10.1016/j.neuron.2009.09.025 · Cited by 75
Overexpression of Vascular Endothelial Growth Factor and the Development of Post-Transplantation Cancer
Basu, A., Contreras, A. G., Datta, D. B., Flynn, E. A., Zeng, L., Cohen, H. T., Briscoe, D. M., & Pal, S. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6603 · Cited by 76
Prolyl Isomerases
Schmid, F. X. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)59008-7 · Cited by 76
Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity
Zhao, Y., Chen, Y. Q., Schutkowski, M., Fischer, G., & Ke, H. (1997) · Structure · doi:10.1016/s0969-2126(97)00172-x · Cited by 76
Calcineurin regulates slow myosin, but not fast myosin or metabolic enzymes, during fast‐to‐slow transformation in rabbit skeletal muscle cell culture
Meißner, J. D., Gros, G., Scheibe, R. J., Scholz, M., & Kubis, H. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.0215b.x · Cited by 76
Truncation Releases Olfactory Receptors from the Endoplasmic Reticulum of Heterologous Cells
Gimelbrant, A. A., Stoss, T. D., Landers, T. M., & McClintock, T. S. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722301.x · Cited by 76
Rapamycin (sirolimus) inhibits proliferating cell nuclear antigen expression and blocks cell cycle in the G1 phase in human keratinocyte stem cells.
Javier, A.-A., Bata‐Csörgõ, Z., Ellis, C. N., Kang, S., Voorhees, J. J., & Cooper, K. D. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119382 · Cited by 76
An inhibitor for calcineurin, FK506, blocks induction of long-term depression in rat visual cortex
Torii, N., Kamishita, T., Otsu, Y., & Tsumoto, T. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(94)11210-a · Cited by 75
The immunosuppressant FK506 increases GAP-43 mRNA levels in axotomized sensory neurons
Gold, B. G., Yew, J. Y., & Zeleny-Pooley, M. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00960-9 · Cited by 76
Ca2+-dependent Cell Signaling through Calmodulin-activated Protein Phosphatase and Protein Kinases Minireview Series
Stull, J. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r000030200 · Cited by 76
Three Amino Acid Residues Determine Selective Binding of FK506-binding Protein 12.6 to the Cardiac Ryanodine Receptor
Xin, H.-B., Rogers, K., Qi, Y., Kanematsu, T., & Fleischer, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15315 · Cited by 76
Protein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator
Travis, S. M., Berger, H. A., & Welsh, M. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.11055 · Cited by 76
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR
Meadows, R. P., Nettesheim, D. G., Xu, R. X., Olejniczak, E. T., Petros, A. M., Holzman, T. F., Severin, J. M., Gubbins, E. J., Smith, H., & Fesik, S. W. (1993) · Biochemistry · doi:10.1021/bi00054a004 · Cited by 76
Chemical Biology Strategies for Posttranslational Control of Protein Function
Rakhit, R., Navarro, R., & Wandless, T. J. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.08.011 · Cited by 75
FK506 binding proteins: Cellular regulators of intracellular Ca2+ signalling
MacMillan, D. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.12.029 · Cited by 73
Declining Intracellular T-Lymphocyte Concentration of Cyclosporine A Precedes Acute Rejection in Kidney Transplant Recipients
Falck, P., Åsberg, A., Guldseth, H., Bremer, S., Akhlaghi, F., Reubsaet, L., Pfeffer, P. F., Hartmann, A., & Midtvedt, K. (2008) · Transplantation · doi:10.1097/tp.0b013e31815feede · Cited by 75
Cyclophilins and cyclophilin inhibitors in nidovirus replication
de Wilde, A. H., Pham, U., Posthuma, C. C., & Snijder, E. J. (2018) · Virology · doi:10.1016/j.virol.2018.06.011 · Cited by 76
Calcineurin/NFAT signaling in the β‐cell: From diabetes to new therapeutics
Heit, J. J. (2007) · BioEssays · doi:10.1002/bies.20644 · Cited by 74
Endorepellin Affects Angiogenesis by Antagonizing Diverse Vascular Endothelial Growth Factor Receptor 2 (VEGFR2)-evoked Signaling Pathways
Goyal, A. K., Poluzzi, C., Willis, C. D., Smythies, J., Shellard, A., Neill, T., & Iozzo, R. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401786 · Cited by 76
AtCyp59 is a multidomain cyclophilin from Arabidopsis thaliana that interacts with SR proteins and the C-terminal domain of the RNA polymerase II
Gullerová, M., Barta, A., & Lorković, Z. J. (2006) · RNA · doi:10.1261/rna.2226106 · Cited by 75
High-Throughput Screening of One-Bead-One-Compound Libraries: Identification of Cyclic Peptidyl Inhibitors against Calcineurin/NFAT Interaction
Liu, T., Qian, Z., Xiao, Q., & Pei, D. (2011) · ACS Combinatorial Science · doi:10.1021/co200101w · Cited by 75
Cyclosporine A-induced nitration of tyrosine 34 MnSOD in endothelial cells: role of mitochondrial superoxide
Redondo‐Horcajo, M., Romero, N., Martínez-Acedo, P., Martı́nez-Ruiz, A., Quijano, C., Lourenço, C. F., Movilla, N., Enrı́quez, J. A., Rodríguez‐Pascual, F., Rial, E., et al. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq028 · Cited by 77
Immunosuppressive effects of tacrolimus on macrophages ameliorate experimental colitis
Yoshino, T., Nakase, H., Honzawa, Y., Matsumura, K., Yamamoto, S., Takeda, Y., Ueno, S., Uza, N., Masuda, S., Inui, K., et al. (2010) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21318 · Cited by 75
Calcineurin Inhibitors Activate the Proto-Oncogene Ras and Promote Protumorigenic Signals in Renal Cancer Cells
Datta, D. B., Contreras, A. G., Basu, A., Dormond, O., Flynn, E. A., Briscoe, D. M., & Pal, S. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1404 · Cited by 78
Cross-Talk between Gs- and Gq-Coupled Pathways in Regulation of Interleukin-4 by A2B Adenosine Receptors in Human Mast Cells
Ryzhov, S. V., Goldstein, A. E., Biaggioni, I., & Feoktistov, I. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.022780 · Cited by 75
A Slow Conformational Switch in the BMAL1 Transactivation Domain Modulates Circadian Rhythms
Gustafson, C. L., Parsley, N. C., Asimgil, H., Lee, H., Ahlbach, C., Michael, A. K., Xu, H., Williams, O. L., Davis, T. L., Liu, A. C., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.011 · Cited by 72
Diverse structures, functions and uses of FK506 binding proteins
Bonner, J. M., & Boulianne, G. L. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.06.013 · Cited by 78
Identification of Soluble Protein Phosphatases That Dephosphorylate Voltage-sensitive Sodium Channels in Rat Brain
Chen, T.-C., Law, B. K., Kondratyuk, T. P., & Rossie, S. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7750 · Cited by 75
The Human Type 1 Inositol 1,4,5-Trisphosphate Receptor from T Lymphocytes
Harnick, D. J., Jayaraman, T., Ma, Y., Mulieri, P., Go, L. O., & Marks, A. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2833 · Cited by 74
Neuroprotective action of tacrolimus (FK506) in focal and global cerebral ischemia in rodents: dose dependency, therapeutic time window and long-term efficacy
Furuichi, Y., Katsuta, K., Maeda, M., Ueyama, N., Moriguchi, A., Matsuoka, N., Goto, T., & Yanagihara, T. (2003) · Brain Research · doi:10.1016/s0006-8993(02)04151-3 · Cited by 75
Ascomycin macrolactam derivative SDZ ASM 981 inhibits the release of granule-associated mediators and of newly synthesized cytokines in RBL 2H3 mast cells in an immunophilin-dependent manner
Hultsch, T., Müller, K. D., Meingassner, J. G., Grassberger, M. A., Schopf, R. E., & KNOP, J. (1998) · Archives of Dermatological Research · doi:10.1007/s004030050343 · Cited by 75
Pharmacodynamic assessment of mycophenolic acid-induced immunosuppression by measuring IMP dehydrogenase activity
Langman, L. J., LeGatt, D. F., & Yatscoff, R. W. (1995) · Clinical Chemistry · doi:10.1093/clinchem/41.2.295 · Cited by 75
Polydatin – a new mitochondria protector for acute severe hemorrhagic shock treatment
Wang, X., Song, R., Chen, Y., Zhao, M. F., & Zhao, K. (2012) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2013.748033 · Cited by 74
Aberrant Signaling Pathways in T-Cell Acute Lymphoblastic Leukemia
Bongiovanni, D., Saccomani, V., & Piovan, E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091904 · Cited by 78
Gene expression is differently affected by pimecrolimus and betamethasone in lesional skin of atopic dermatitis
Jensen, J., Scherer, A., Wanke, C., Bräutigam, M., Bongiovanni, S., Letzkus, M., Staedtler, F., Kehren, J., Zuehlsdorf, M., Schwarz, T., et al. (2011) · Allergy · doi:10.1111/j.1398-9995.2011.02747.x · Cited by 74
Role of calcineurin in the regulation of human lung mast cell and basophil function by cyclosporine and FK506
Harrison, C. A., Bastan, R., Peirce, M. J., Munday, M. R., & Peachell, P. T. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707002 · Cited by 74
Activation of the β myosin heavy chain promoter by MEF‐2D, MyoD, p300, and the calcineurin/NFATc1 pathway
Meissner, J. D., Umeda, P. K., Chang, K., Gros, G., & Scheibe, R. J. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20916 · Cited by 74
Regulated expression of the Leishmania major surface virulence factor lipophosphoglycan using conditionally destabilized fusion proteins
da Silva, L. M., Owens, K. L., Murta, S. M. F., & Beverley, S. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901698106 · Cited by 71
DEFECTIVE INHIBITION OF PERIPHERAL CD8+ T CELL IL-2 PRODUCTION BY ANTI-CALCINEURIN DRUGS DURING ACUTE LIVER ALLOGRAFT REJECTION
Boleslawski, E., Conti, F., Sanquer, S., Podevin, P., Chouzenoux, S., Batteux, F., Houssin, D. P., Weill, B. J., & Calmus, Y. (2004) · Transplantation · doi:10.1097/01.tp.0000129914.75547.b3 · Cited by 74
NIM811, a cyclophilin inhibitor without immunosuppressive activity, is beneficial in collagen VI congenital muscular dystrophy models
Zulian, A., Rizzo, E., Schiavone, M., Palma, E., Tagliavini, F., Blaauw, B., Merlini, L., Maraldi, N. M., Sabatelli, P., Braghetta, P., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu254 · Cited by 75
Physiology of epithelial Ca2+ and Mg2+ transport
van de Graaf, S. F. J., Bindels, R. J. M., & Hoenderop, J. G. J. (2007) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2006_0607 · Cited by 73
Recombinant Human (rh)IL-4-Mediated Apoptosis and Recombinant Human IL-6-Mediated Protection of Recombinant Human Stem Cell Factor-Dependent Human Mast Cells Derived from Cord Blood Mononuclear Cell Progenitors
Oskeritzian, C. A., Wang, Z., Kochan, J. P., Grimes, M. M., Du, Z., Chang, H., Grant, S., & Schwartz, L. B. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.9.5105 · Cited by 74
Cyclosporine Treatment of Inflammatory Bowel Disease
Sandborn, W. J., & Tremaine, W. J. (1992) · Mayo Clinic Proceedings · doi:10.1016/s0025-6196(12)60930-6 · Cited by 74
Cyclosporin A Protects Against Angiotensin II–Induced End-Organ Damage in Double Transgenic Rats Harboring Human Renin and Angiotensinogen Genes
Mervaala, E. M. A., Müller, D. N., Park, J.-K., Dechend, R., Schmidt, F. H., Fiebeler, A., Bieringer, M., Breu, V., Ganten, D., Haller, H. G., et al. (2000) · Hypertension · doi:10.1161/01.hyp.35.1.360 · Cited by 74
The Regulation of CD95 Ligand Expression and Function in CTL
Li, J., Rosen, D., Ronen, D., Behrens, C. K., Krammer, P. H., Clark, W. R., & Berke, G. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.8.3943 · Cited by 74
Target identification of small molecules based on chemical biology approaches
Futamura, Y., Muroi, M., & Osada, H. (2013) · Molecular BioSystems · doi:10.1039/c2mb25468a · Cited by 73
SNF4435C and D, Novel Immunosuppressants Produced by a Strain of Streptomyces spectabilis. I. Taxonomy, Fermentation, Isolation and Biological Activities.
Kurosawa, K., Takahashi, K., & TSUDA, E. (2001) · The Journal of Antibiotics · doi:10.7164/antibiotics.54.541 · Cited by 73
Long‐term potentiation inhibition by low‐level N‐methyl‐ D ‐aspartate receptor activation involves calcineurin, nitric oxide, and p38 mitogen‐activated protein kinase
Izumi, Y., Tokuda, K., & Zorumski, C. F. (2007) · Hippocampus · doi:10.1002/hipo.20383 · Cited by 73
The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity
Kumar, R., Adams, B. D., Musiyenko, A., Shulyayeva, O., & Barik, S. (2005) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2005.02.007 · Cited by 73
Rotenone Induces Apoptosis via Activation of Bad in Human Dopaminergic SH-SY5Y Cells
Watabe, M., & Nakaki, T. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.071381 · Cited by 73
A Unified Total Synthesis of the Immunomodulators (−)-Rapamycin and (−)-27-Demethoxyrapamycin: Construction of the C(21−42) Perimeters
Smith, A. B., Condon, S. M., McCauley, J. A., Leazer, J. L., Leahy, J. W., & Maleczka, R. E. (1997) · Journal of the American Chemical Society · doi:10.1021/ja963066w · Cited by 73
Substrate specificities of catalytic fragments of protein tyrosine phosphatases (HPTPβ, LAR, and CD45) toward phosphotyrosylpeptide substrates and thiophosphotyrosylated peptides as inhibitors
Cho, H., Krishnaraj, R., Walsh, C. T., Itoh, M., Saito, H., Kitas, E. A., & Bannwarth, W. (1993) · Protein Science · doi:10.1002/pro.5560020611 · Cited by 73
Inhibition of human immunodeficiency virus replication by nonimmunosuppressive analogs of cyclosporin A.
Bartz, S. R., Hohenwalter, E., Hu, M. K., Rich, D. H., & Malkovský, M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5381 · Cited by 73
Discovery of RMC-5552, a Selective Bi-Steric Inhibitor of mTORC1, for the Treatment of mTORC1-Activated Tumors
Burnett, G. L., Yang, Y. C., Aggen, J. B., Pitzen, J., Gliedt, M. K., Semko, C. M., Marquez, A., Evans, J. W., Wang, G., Won, W. S., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01658 · Cited by 72
Blockade of NFAT Activation by the Second Calcineurin Binding Site
Martı́nez-Martı́nez, S., Rodrı́guez, A., López-Maderuelo, D., Ortega‐Pérez, I., Vázquez, J., & Redondo, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513885200 · Cited by 74
Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin
Pan, F., Sun, L., Kardian, D., Whartenby, K. A., Pardoll, D. M., & Liu, J. O. (2007) · Nature · doi:10.1038/nature05476 · Cited by 72
Self-citation
FHL2 Binds Calcineurin and Represses Pathological Cardiac Growth
Hojayev, B., Rothermel, B. A., Gillette, T. G., & Hill, J. A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.05948-11 · Cited by 72
Roles of Cyclophilins in Cancers and Other Organ Systems
Yao, Q. C., Li, M., Yang, H., Chai, H., Fisher, W. P., & Chen, C. (2005) · World Journal of Surgery · doi:10.1007/s00268-004-7812-7 · Cited by 72
Genetic and Genomic Approaches to Identify and Study the Targets of Bioactive Small Molecules
Zheng, X., Chan, T., & Zhou, H. H. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.08.011 · Cited by 74
The Peptidyl-Prolyl Isomerase Pin1 Regulates Granulocyte-Macrophage Colony-Stimulating Factor mRNA Stability in T Lymphocytes
Esnault, S. J., Shen, Z.-J., Whitesel, E., & Malter, J. S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.10.6999 · Cited by 72
The Role of Nitric Oxide in Neurodegeneration
Pérez-Molina, J. A., Jim�nez-Jim�nez, F. J., Ort??-Pareja, M., & Navarro, J. A. (1998) · Drugs & Aging · doi:10.2165/00002512-199812040-00001 · Cited by 71
FK506 binding protein 12 mediates sensitivity to both FK506 and rapamycin in murine mast cells
Fruman, D. A., Wood, M. A., Gjertson, C. K., Katz, H. R., Burakoff, S. J., & Bierer, B. E. (1995) · European Journal of Immunology · doi:10.1002/eji.1830250239 · Cited by 72
Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1
Lohse, D. L., Denu, J., & Dixon, J. (1995) · Structure · doi:10.1016/s0969-2126(01)00234-9 · Cited by 72
4-(Fluoromethyl)phenyl Phosphate Acts as a Mechanism-based Inhibitor of Calcineurin
Born, T. L., Myers, J. K., Widlanski, T. S., & Rusnak, F. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25651 · Cited by 72
Molecular nature and regulation of the mitochondrial permeability transition pore(s), drug target(s) in cardioprotection
Carraro, M., Carrer, A., Urbani, A., & Bernardi, P. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.05.014 · Cited by 71
Attenuation of microglial activation in a mouse model of Alzheimer’s disease via NFAT inhibition
Rojanathammanee, L., Floden, A. M., Manocha, G. D., & Combs, C. K. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0255-2 · Cited by 69
Rational Screening for Cooperativity in Small-Molecule Inducers of Protein–Protein Associations
Liu, S., Tong, B., Mason, J. W., Ostrem, J. M. L., Tutter, A. V., Hua, B. K., Tang, S. A., Bonazzi, S., Briner, K., Berst, F., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c08307 · Cited by 69
Self-citation
Discovery and Use of Small Molecules for Probing Biological Processes in Zebrafish
Peterson, R. T., & Fishman, M. C. (2004) · Methods in cell biology · doi:10.1016/s0091-679x(04)76026-4 · Cited by 70
Recent advances in the chemistry, biosynthesis and pharmacology of rapamycin analogs
Graziani, E. I. (2009) · Natural Product Reports · doi:10.1039/b804602f · Cited by 71
Cellular mechanisms of vascular injury mediated by calcineurin inhibitors
Lamas, S. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.00472.x · Cited by 71
Donor ABCB1 Variant Associates with Increased Risk for Kidney Allograft Failure
Moore, J., McKnight, A. J., Döhler, B., Simmonds, M. J., Courtney, A. E., Brand, O. J., Briggs, D., Ball, S. T., Cockwell, P., Patterson, C., et al. (2012) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012030260 · Cited by 71
Identification of a Calmodulin-Binding and Inhibitory Peptide Domain in the HIV-1 Transmembrane Glycoprotein
Miller, M. A., Mietzner, T. A., Cloyd, M. W., Robey, W. G., & Montelaro, R. C. (1993) · AIDS Research and Human Retroviruses · doi:10.1089/aid.1993.9.1057 · Cited by 71
Modulation of the Enzymatic Properties of Protein Phosphatase 2A Catalytic Subunit by the Recombinant 65‐kDa Regulatory Subunit PR65α
Turowski, P., Favre, B., Campbell, K. S., Lamb, N. J. C., & Hemmings, B. A. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00200.x · Cited by 71

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

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks