메뉴 건너뛰기




Volumn 7, Issue , 2009, Pages

Novel inhibitors of the calcineurin/NFATc hub - Alternatives to CsA and FK506?

Author keywords

[No Author keywords available]

Indexed keywords


EID: 72849149270     PISSN: 1478811X     EISSN: None     Source Type: Journal    
DOI: 10.1186/1478-811X-7-25     Document Type: Review
Times cited : (94)

References (198)
  • 1
    • 0017890599 scopus 로고
    • Purification of cyclic 3',5'-nucleotide phosphodiesterase inhibitory protein by affinity chromatography on activator protein coupled to Sepharose
    • Purification of cyclic 3',5'-nucleotide phosphodiesterase inhibitory protein by affinity chromatography on activator protein coupled to Sepharose. CB Klee MH Krinks, Biochemistry 1978 17 120 126
    • (1978) Biochemistry , vol.17 , pp. 120-126
    • Klee, C.B.1    Krinks, M.H.2
  • 2
    • 0036234543 scopus 로고    scopus 로고
    • NFAT signaling: Choreographing the social lives of cells
    • NFAT signaling: choreographing the social lives of cells. GR Crabtree EN Olson, Cell 2002 109 Suppl 67 79
    • (2002) Cell , vol.109 , Issue.SUPPL , pp. 1967-79
    • Crabtree, G.R.1    Olson, E.N.2
  • 3
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. CB Klee H Ren X Wang, J Biol Chem 1998 273 13367 13370
    • (1998) J Biol Chem , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 4
    • 0242606161 scopus 로고    scopus 로고
    • Endogenous protein inhibitors of calcineurin
    • Endogenous protein inhibitors of calcineurin. JO Liu, Biochem Biophys Res Commun 2003 311 1103 1109
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 1103-1109
    • Liu, J.O.1
  • 5
    • 61849085112 scopus 로고    scopus 로고
    • Calmodulin-dependent phosphatase, kinases, and transcriptional corepressors involved in T-cell activation
    • Calmodulin-dependent phosphatase, kinases, and transcriptional corepressors involved in T-cell activation. JO Liu, Immunol Rev 2009 228 184 198
    • (2009) Immunol Rev , vol.228 , pp. 184-198
    • Liu, J.O.1
  • 6
    • 0032941253 scopus 로고    scopus 로고
    • Potential role of calcineurin for brain ischemia and traumatic injury
    • Potential role of calcineurin for brain ischemia and traumatic injury. M Morioka J Hamada Y Ushio E Miyamoto, Prog Neurobiol 1999 58 1 30
    • (1999) Prog Neurobiol , vol.58 , pp. 1-30
    • Morioka, M.1    Hamada, J.2    Ushio, Y.3    Miyamoto, E.4
  • 7
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Transcription factors of the NFAT family: regulation and function. A Rao C Luo PG Hogan, Annu Rev Immunol 1997 15 707 747
    • (1997) Annu Rev Immunol , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 9
    • 0141483523 scopus 로고    scopus 로고
    • Transcriptional regulation by calcium, calcineurin, and NFAT
    • Transcriptional regulation by calcium, calcineurin, and NFAT. PG Hogan L Chen J Nardone A Rao, Genes Dev 2003 17 2205 2232
    • (2003) Genes Dev , vol.17 , pp. 2205-2232
    • Hogan, P.G.1    Chen, L.2    Nardone, J.3    Rao, A.4
  • 10
    • 20644466433 scopus 로고    scopus 로고
    • NFAT proteins: Key regulators of T-cell development and function
    • NFAT proteins: key regulators of T-cell development and function. F Macian, Nat Rev Immunol 2005 5 472 484
    • (2005) Nat Rev Immunol , vol.5 , pp. 472-484
    • MacIan, F.1
  • 12
    • 0030962605 scopus 로고    scopus 로고
    • The downstream consequences of calcineurin inhibition
    • The downstream consequences of calcineurin inhibition. TD Batiuk PF Halloran, Transplant Proc 1997 29 1239 1240
    • (1997) Transplant Proc , vol.29 , pp. 1239-1240
    • Batiuk, T.D.1    Halloran, P.F.2
  • 13
    • 0035967887 scopus 로고    scopus 로고
    • Signals transduced by Ca(2+)/calcineurin and NFATc3/c4 pattern the developing vasculature
    • Signals transduced by Ca(2+)/calcineurin and NFATc3/c4 pattern the developing vasculature. IA Graef F Chen L Chen A Kuo GR Crabtree, Cell 2001 105 863 875
    • (2001) Cell , vol.105 , pp. 863-875
    • Graef, I.A.1    Chen, F.2    Chen, L.3    Kuo, A.4    Crabtree, G.R.5
  • 20
    • 0033561538 scopus 로고    scopus 로고
    • Two independent calcineurin-binding regions in the N-terminal domain of murine NF-ATx1 recruit calcineurin to murine NF-ATx1
    • Two independent calcineurin-binding regions in the N-terminal domain of murine NF-ATx1 recruit calcineurin to murine NF-ATx1. J Liu ES Masuda L Tsuruta N Arai K Arai, J Immunol 1999 162 4755 4761
    • (1999) J Immunol , vol.162 , pp. 4755-4761
    • Liu, J.1    Masuda, E.S.2    Tsuruta, L.3    Arai, N.4    Arai, K.5
  • 21
    • 0032039075 scopus 로고    scopus 로고
    • Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT
    • Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT. J Aramburu F Garcia-Cozar A Raghavan H Okamura A Rao PG Hogan, Mol Cell 1998 1 627 637
    • (1998) Mol Cell , vol.1 , pp. 627-637
    • Aramburu, J.1    Garcia-Cozar, F.2    Raghavan, A.3    Okamura, H.4    Rao, A.5    Hogan, P.G.6
  • 25
    • 34248666084 scopus 로고    scopus 로고
    • Structure of calcineurin in complex with PVIVIT peptide: Portrait of a low-affinity signalling interaction
    • Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. H Li L Zhang A Rao SC Harrison PG Hogan, J Mol Biol 2007 369 1296 1306
    • (2007) J Mol Biol , vol.369 , pp. 1296-1306
    • Li, H.1    Zhang, L.2    Rao, A.3    Harrison, S.C.4    Hogan, P.G.5
  • 26
    • 33947241214 scopus 로고    scopus 로고
    • A conserved docking site modulates substrate affinity for calcineurin, signaling output, and in vivo function
    • A conserved docking site modulates substrate affinity for calcineurin, signaling output, and in vivo function. J Roy H Li PG Hogan MS Cyert, Mol Cell 2007 25 889 901
    • (2007) Mol Cell , vol.25 , pp. 889-901
    • Roy, J.1    Li, H.2    Hogan, P.G.3    Cyert, M.S.4
  • 28
    • 0030682419 scopus 로고    scopus 로고
    • The calcium/calmodulin-dependent protein phosphatase calcineurin is the major Elk-1 phosphatase
    • The calcium/calmodulin-dependent protein phosphatase calcineurin is the major Elk-1 phosphatase. T Sugimoto S Stewart KL Guan, J Biol Chem 1997 272 29415 29418
    • (1997) J Biol Chem , vol.272 , pp. 29415-29418
    • Sugimoto, T.1    Stewart, S.2    Guan, K.L.3
  • 29
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Calcium oscillations increase the efficiency and specificity of gene expression. RE Dolmetsch K Xu RS Lewis, Nature 1998 392 933 936
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 30
    • 0037400609 scopus 로고    scopus 로고
    • Calcineurin activates NF-kappaB in skeletal muscle C2C12 cells
    • Calcineurin activates NF-kappaB in skeletal muscle C2C12 cells. H Alzuherri KC Chang, Cell Signal 2003 15 471 478
    • (2003) Cell Signal , vol.15 , pp. 471-478
    • Alzuherri, H.1    Chang, K.C.2
  • 31
    • 34250635494 scopus 로고    scopus 로고
    • NF-kappaB activation by depolarization of skeletal muscle cells depends on ryanodine and IP3 receptor-mediated calcium signals
    • NF-kappaB activation by depolarization of skeletal muscle cells depends on ryanodine and IP3 receptor-mediated calcium signals. JA Valdes J Hidalgo JL Galaz N Puentes M Silva E Jaimovich MA Carrasco, Am J Physiol Cell Physiol 2007 292 1960 1970
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 31960-1970
    • Valdes, J.A.1    Hidalgo, J.2    Galaz, J.L.3    Puentes, N.4    Silva, M.5    Jaimovich, E.6    Carrasco, M.A.7
  • 32
    • 56149115514 scopus 로고    scopus 로고
    • Elevating calcium in Th2 cells activates multiple pathways to induce IL-4 transcription and mRNA stabilization
    • Elevating calcium in Th2 cells activates multiple pathways to induce IL-4 transcription and mRNA stabilization. L Guo JF Urban J Zhu WE Paul, J Immunol 2008 181 3984 3993
    • (2008) J Immunol , vol.181 , pp. 3984-3993
    • Guo, L.1    Urban, J.F.2    Zhu, J.3    Paul, W.E.4
  • 33
    • 59649116320 scopus 로고    scopus 로고
    • Interaction between TAK1-TAB1-TAB2 and RCAN1-calcineurin defines a signalling nodal control point
    • Interaction between TAK1-TAB1-TAB2 and RCAN1-calcineurin defines a signalling nodal control point. Q Liu JC Busby JD Molkentin, Nat Cell Biol 2009 11 154 161
    • (2009) Nat Cell Biol , vol.11 , pp. 154-161
    • Liu, Q.1    Busby, J.C.2    Molkentin, J.D.3
  • 34
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway
    • The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. J Ninomiya-Tsuji K Kishimoto A Hiyama J Inoue Z Cao K Matsumoto, Nature 1999 398 252 256
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5    Matsumoto, K.6
  • 36
    • 33751522625 scopus 로고    scopus 로고
    • Controlling the generation and function of human CD8+ memory T cells in vitro with immunosuppressants
    • Controlling the generation and function of human CD8+ memory T cells in vitro with immunosuppressants. DL Jones SH Sacks W Wong, Transplantation 2006 82 1352 1361
    • (2006) Transplantation , vol.82 , pp. 1352-1361
    • Jones, D.L.1    Sacks, S.H.2    Wong, W.3
  • 37
    • 24644461627 scopus 로고    scopus 로고
    • Immunosuppressive agents in solid organ transplantation: Mechanisms of action and therapeutic efficacy
    • Immunosuppressive agents in solid organ transplantation: Mechanisms of action and therapeutic efficacy. AL Taylor CJ Watson JA Bradley, Crit Rev Oncol Hematol 2005 56 23 46
    • (2005) Crit Rev Oncol Hematol , vol.56 , pp. 23-46
    • Taylor, A.L.1    Watson, C.J.2    Bradley, J.A.3
  • 38
    • 63149097158 scopus 로고    scopus 로고
    • Topical calcineurin inhibitors in atopic dermatitis: A systematic review and meta-analysis
    • Topical calcineurin inhibitors in atopic dermatitis: a systematic review and meta-analysis. MM El-Batawy MA Bosseila HM Mashaly VS Hafez, J Dermatol Sci 2009 54 76 87
    • (2009) J Dermatol Sci , vol.54 , pp. 76-87
    • El-Batawy, M.M.1    Bosseila, M.A.2    Mashaly, H.M.3    Hafez, V.S.4
  • 39
    • 70349858128 scopus 로고    scopus 로고
    • Low-dose cyclosporine A therapy increases the regulatory T cell population in patients with atopic dermatitis
    • Low-dose cyclosporine A therapy increases the regulatory T cell population in patients with atopic dermatitis. C Brandt V Pavlovic A Radbruch M Worm R Baumgrass, Allergy 2009 64 1588 1596
    • (2009) Allergy , vol.64 , pp. 1588-1596
    • Brandt, C.1    Pavlovic, V.2    Radbruch, A.3    Worm, M.4    Baumgrass, R.5
  • 40
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Calcineurin: form and function. F Rusnak P Mertz, Physiol Rev 2000 80 1483 1521
    • (2000) Physiol Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 41
    • 0035103066 scopus 로고    scopus 로고
    • Molecular genetic analysis of the calcineurin signaling pathways
    • Molecular genetic analysis of the calcineurin signaling pathways. R Sugiura SO Sio H Shuntoh T Kuno, Cell Mol Life Sci 2001 58 278 288
    • (2001) Cell Mol Life Sci , vol.58 , pp. 278-288
    • Sugiura, R.1    Sio, S.O.2    Shuntoh, H.3    Kuno, T.4
  • 42
    • 0017157814 scopus 로고
    • Biological effects of cyclosporin A: A new antilymphocytic agent
    • Biological effects of cyclosporin A: a new antilymphocytic agent. JF Borel C Feurer HU Gubler H Stahelin, Agents Actions 1976 6 468 475
    • (1976) Agents Actions , vol.6 , pp. 468-475
    • Borel, J.F.1    Feurer, C.2    Gubler, H.U.3    Stahelin, H.4
  • 45
    • 0023245677 scopus 로고
    • FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics
    • FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics. T Kino H Hatanaka M Hashimoto M Nishiyama T Goto M Okuhara M Kohsaka H Aoki H Imanaka, J Antibiot (Tokyo) 1987 40 1249 1255
    • (1987) J Antibiot (Tokyo) , vol.40 , pp. 1249-1255
    • Kino, T.1    Hatanaka, H.2    Hashimoto, M.3    Nishiyama, M.4    Goto, T.5    Okuhara, M.6    Kohsaka, M.7    Aoki, H.8    Imanaka, H.9
  • 48
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • The mechanism of action of cyclosporin A and FK506. SL Schreiber GR Crabtree, Immunol Today 1992 13 136 142
    • (1992) Immunol Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 49
    • 33846059755 scopus 로고    scopus 로고
    • Immunophilins: For the love of proteins
    • Immunophilins: for the love of proteins. S Barik, Cell Mol Life Sci 2006 63 2889 2900
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2889-2900
    • Barik, S.1
  • 50
    • 57149093203 scopus 로고    scopus 로고
    • FKBP family proteins: Immunophilins with versatile biological functions
    • FKBP family proteins: immunophilins with versatile biological functions. CB Kang Y Hong S Dhe-Paganon HS Yoon, Neurosignals 2008 16 318 325
    • (2008) Neurosignals , vol.16 , pp. 318-325
    • Kang, C.B.1    Hong, Y.2    Dhe-Paganon, S.3    Yoon, H.S.4
  • 53
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Q Huai HY Kim Y Liu Y Zhao A Mondragon JO Liu H Ke, Proc Natl Acad Sci USA 2002 99 12037 12042
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12037-12042
    • Huai, Q.1    Kim, H.Y.2    Liu, Y.3    Zhao, Y.4    Mondragon, A.5    Liu, J.O.6    Ke, H.7
  • 54
    • 0037108767 scopus 로고    scopus 로고
    • Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin
    • Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. L Jin SC Harrison, Proc Natl Acad Sci USA 2002 99 13522 13526
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13522-13526
    • Jin, L.1    Harrison, S.C.2
  • 56
    • 0142226935 scopus 로고    scopus 로고
    • Mechanism for the paradoxical inhibition and stimulation of calcineurin by the immunosuppresive drug tacrolimus (FK506)
    • Mechanism for the paradoxical inhibition and stimulation of calcineurin by the immunosuppresive drug tacrolimus (FK506). M Yin RS Ochs, Arch Biochem Biophys 2003 419 207 213
    • (2003) Arch Biochem Biophys , vol.419 , pp. 207-213
    • Yin, M.1    Ochs, R.S.2
  • 58
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. JJ Siekierka SH Hung M Poe CS Lin NH Sigal, Nature 1989 341 755 757
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 59
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. MW Harding A Galat DE Uehling SL Schreiber, Nature 1989 341 758 760
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 60
    • 0031842613 scopus 로고    scopus 로고
    • Mechanism responsible for T-cell antigen receptor- and CD28- or interleukin 1 (IL-1) receptor-initiated regulation of IL-2 gene expression by NF-kappaB
    • Mechanism responsible for T-cell antigen receptor- and CD28- or interleukin 1 (IL-1) receptor-initiated regulation of IL-2 gene expression by NF-kappaB. K Kalli C Huntoon M Bell DJ McKean, Mol Cell Biol 1998 18 3140 3148
    • (1998) Mol Cell Biol , vol.18 , pp. 3140-3148
    • Kalli, K.1    Huntoon, C.2    Bell, M.3    McKean, D.J.4
  • 61
    • 0032748411 scopus 로고    scopus 로고
    • Erythromycin inhibits transcriptional activation of NF-kappaB, but not NFAT, through calcineurin-independent signaling in T cells
    • Erythromycin inhibits transcriptional activation of NF-kappaB, but not NFAT, through calcineurin-independent signaling in T cells. Y Aoki PN Kao, Antimicrob Agents Chemother 1999 43 2678 2684
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 2678-2684
    • Aoki, Y.1    Kao, P.N.2
  • 62
    • 0028973059 scopus 로고
    • Regulation of IkB alpha phosphorylation by PKC- and Ca(2+)-dependent signal transduction pathways
    • Regulation of IkB alpha phosphorylation by PKC- and Ca(2+)-dependent signal transduction pathways. NM Steffan GD Bren B Frantz MJ Tocci EA O'Neill CV Paya, J Immunol 1995 155 4685 4691
    • (1995) J Immunol , vol.155 , pp. 4685-4691
    • Steffan, N.M.1    Bren, G.D.2    Frantz, B.3    Tocci, M.J.4    O'Neill, E.A.5    Paya, C.V.6
  • 63
    • 17844366894 scopus 로고    scopus 로고
    • The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization-induced CREB transcriptional activity at the coactivator level
    • The immunosuppressive drugs cyclosporin A and tacrolimus inhibit membrane depolarization-induced CREB transcriptional activity at the coactivator level. E Oetjen KM Thoms Y Laufer D Pape R Blume P Li W Knepel, Br J Pharmacol 2005 144 982 993
    • (2005) Br J Pharmacol , vol.144 , pp. 982-993
    • Oetjen, E.1    Thoms, K.M.2    Laufer, Y.3    Pape, D.4    Blume, R.5    Li, P.6    Knepel, W.7
  • 64
    • 0030879083 scopus 로고    scopus 로고
    • Cyclosporin A interferes with the inducible degradation of NF-kappa B inhibitors, but not with the processing of p105/NF-kappa B1 in T cells
    • Cyclosporin A interferes with the inducible degradation of NF-kappa B inhibitors, but not with the processing of p105/NF-kappa B1 in T cells. R Marienfeld M Neumann S Chuvpilo C Escher B Kneitz A Avots A Schimpl E Serfling, Eur J Immunol 1997 27 1601 1609
    • (1997) Eur J Immunol , vol.27 , pp. 1601-1609
    • Marienfeld, R.1    Neumann, M.2    Chuvpilo, S.3    Escher, C.4    Kneitz, B.5    Avots, A.6    Schimpl, A.7    Serfling, E.8
  • 65
    • 0030805604 scopus 로고    scopus 로고
    • Cyclosporine A is an uncompetitive inhibitor of proteasome activity and prevents NF-κB activation
    • DOI 10.1016/S0014-5793(97)00930-7, PII S0014579397009307
    • Cyclosporine A is an uncompetitive inhibitor of proteasome activity and prevents NF-kappaB activation. S Meyer NG Kohler A Joly, FEBS Lett 1997 413 354 358 (Pubitemid 27353299)
    • (1997) FEBS Letters , vol.413 , Issue.2 , pp. 354-358
    • Meyer, S.1    Kohler, N.G.2    Joly, A.3
  • 66
    • 10644278692 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent spot assay for donor-reactive interferon-gamma-producing cells identifies T-cell presensitization and correlates with graft function at 6 and 12 months in renal-transplant recipients
    • Enzyme-linked immunosorbent spot assay for donor-reactive interferon-gamma-producing cells identifies T-cell presensitization and correlates with graft function at 6 and 12 months in renal-transplant recipients. P Nickel F Presber G Bold D Biti C Schonemann SG Tullius HD Volk P Reinke, Transplantation 2004 78 1640 1646
    • (2004) Transplantation , vol.78 , pp. 1640-1646
    • Nickel, P.1    Presber, F.2    Bold, G.3    Biti, D.4    Schonemann, C.5    Tullius, S.G.6    Volk, H.D.7    Reinke, P.8
  • 68
    • 0033698581 scopus 로고    scopus 로고
    • Manipulating immune responses with immunosuppressive agents that target NFAT
    • Manipulating immune responses with immunosuppressive agents that target NFAT. A Kiani A Rao J Aramburu, Immunity 2000 12 359 372
    • (2000) Immunity , vol.12 , pp. 359-372
    • Kiani, A.1    Rao, A.2    Aramburu, J.3
  • 69
    • 4544238963 scopus 로고    scopus 로고
    • Branches on the alpha-C atom of cyclosporin A residue 3 result in direct calcineurin inhibition and rapid cyclophilin 18 binding
    • Branches on the alpha-C atom of cyclosporin A residue 3 result in direct calcineurin inhibition and rapid cyclophilin 18 binding. Y Zhang R Baumgrass M Schutkowski G Fischer, Chembiochem 2004 5 1006 1009
    • (2004) Chembiochem , vol.5 , pp. 1006-1009
    • Zhang, Y.1    Baumgrass, R.2    Schutkowski, M.3    Fischer, G.4
  • 72
    • 0027336029 scopus 로고
    • Immunosuppressive activity of [MeBm2t]1-, D-diaminobutyryl-8-, and D-diaminopropyl-8-cyclosporin analogues correlates with inhibition of calcineurin phosphatase activity
    • Immunosuppressive activity of [MeBm2t]1-, D-diaminobutyryl-8-, and D-diaminopropyl-8-cyclosporin analogues correlates with inhibition of calcineurin phosphatase activity. PA Nelson Y Akselband A Kawamura M Su RD Tung DH Rich V Kishore SL Rosborough MT DeCenzo DJ Livingston, et al. J Immunol 1993 150 2139 2147
    • (1993) J Immunol , vol.150 , pp. 2139-2147
    • Nelson, P.A.1    Akselband, Y.2    Kawamura, A.3    Su, M.4    Tung, R.D.5    Rich, D.H.6    Kishore, V.7    Rosborough, S.L.8    Decenzo, M.T.9    Livingston, D.J.10
  • 73
    • 1642494718 scopus 로고    scopus 로고
    • Substitution in position 3 of cyclosporin A abolishes the cyclophilin-mediated gain-of-function mechanism but not immunosuppression
    • Substitution in position 3 of cyclosporin A abolishes the cyclophilin-mediated gain-of-function mechanism but not immunosuppression. R Baumgrass Y Zhang F Erdmann A Thiel M Weiwad A Radbruch G Fischer, J Biol Chem 2004 279 2470 2479
    • (2004) J Biol Chem , vol.279 , pp. 2470-2479
    • Baumgrass, R.1    Zhang, Y.2    Erdmann, F.3    Thiel, A.4    Weiwad, M.5    Radbruch, A.6    Fischer, G.7
  • 74
    • 0025240645 scopus 로고
    • Synthesis, conformation, and immunosuppressive activities of three analogues of cyclosporin A modified in the 1-position
    • Synthesis, conformation, and immunosuppressive activities of three analogues of cyclosporin A modified in the 1-position. JD Aebi DT Deyo CQ Sun D Guillaume B Dunlap DH Rich, J Med Chem 1990 33 999 1009 (Pubitemid 20085905)
    • (1990) Journal of Medicinal Chemistry , vol.33 , Issue.3 , pp. 999-1009
    • Aebi, J.D.1    Deyo, D.T.2    Sun, C.Q.3    Guillaume, D.4    Dunlap, B.5    Rich, D.H.6
  • 76
    • 23944441184 scopus 로고    scopus 로고
    • The novel calcineurin inhibitor ISA247: A more potent immunosuppressant than cyclosporine in vitro
    • The novel calcineurin inhibitor ISA247: a more potent immunosuppressant than cyclosporine in vitro. T Birsan C Dambrin DG Freitag RW Yatscoff RE Morris, Transpl Int 2005 17 767 771
    • (2005) Transpl Int , vol.17 , pp. 767-771
    • Birsan, T.1    Dambrin, C.2    Freitag, D.G.3    Yatscoff, R.W.4    Morris, R.E.5
  • 78
    • 51249124874 scopus 로고    scopus 로고
    • Voclosporin (ISA247) for plaque psoriasis
    • author reply 889
    • Voclosporin (ISA247) for plaque psoriasis. P Naidoo V Rambiritch, Lancet 2008 372 888 889 author reply 889
    • (2008) Lancet , vol.372 , pp. 888-889
    • Naidoo, P.1    Rambiritch, V.2
  • 80
    • 0035900877 scopus 로고    scopus 로고
    • The neuroprotective actions of FK506 binding protein ligands: Neuronal survival is triggered by de novo RNA synthesis, but is independent of inhibition of JNK and calcineurin
    • The neuroprotective actions of FK506 binding protein ligands: neuronal survival is triggered by de novo RNA synthesis, but is independent of inhibition of JNK and calcineurin. A Klettner R Baumgrass Y Zhang G Fischer E Burger T Herdegen K Mielke, Brain Res Mol Brain Res 2001 97 21 31
    • (2001) Brain Res Mol Brain Res , vol.97 , pp. 21-31
    • Klettner, A.1    Baumgrass, R.2    Zhang, Y.3    Fischer, G.4    Burger, E.5    Herdegen, T.6    Mielke, K.7
  • 85
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands. SL Schreiber, Science 1991 251 283 287
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 87
    • 65549140711 scopus 로고    scopus 로고
    • Minimizing the risk of posttransplant malignancy
    • Minimizing the risk of posttransplant malignancy. JM Campistol, Transplantation 2009 87 19 22
    • (2009) Transplantation , vol.87 , pp. 1919-22
    • Campistol, J.M.1
  • 88
    • 0028863679 scopus 로고
    • 4-(Fluoromethyl)phenyl phosphate acts as a mechanism-based inhibitor of calcineurin
    • 4-(Fluoromethyl)phenyl phosphate acts as a mechanism-based inhibitor of calcineurin. TL Born JK Myers TS Widlanski F Rusnak, J Biol Chem 1995 270 25651 25655
    • (1995) J Biol Chem , vol.270 , pp. 25651-25655
    • Born, T.L.1    Myers, J.K.2    Widlanski, T.S.3    Rusnak, F.4
  • 89
    • 0031781898 scopus 로고    scopus 로고
    • Inhibition of calcineurin by the tyrphostin class of tyrosine kinase inhibitors
    • Inhibition of calcineurin by the tyrphostin class of tyrosine kinase inhibitors. BL Martin, Biochem Pharmacol 1998 56 483 488
    • (1998) Biochem Pharmacol , vol.56 , pp. 483-488
    • Martin, B.L.1
  • 91
    • 45549105319 scopus 로고    scopus 로고
    • Use of protein phosphatase inhibitors
    • Use of protein phosphatase inhibitors. DC Weiser S Shenolikar, Curr Protoc Protein Sci 2003 Chapter 13 Unit 13 10
    • (2003) Curr Protoc Protein Sci , vol.13 , Issue.UNIT 13 , pp. 10
    • Weiser, D.C.1    Shenolikar, S.2
  • 92
    • 0030825493 scopus 로고    scopus 로고
    • Class II pyrethroids: Noninhibitors calcineurin
    • Class II pyrethroids: noninhibitors calcineurin. A Enz E Pombo-Villar, Biochem Pharmacol 1997 54 321 323
    • (1997) Biochem Pharmacol , vol.54 , pp. 321-323
    • Enz, A.1    Pombo-Villar, E.2
  • 95
    • 67349201766 scopus 로고    scopus 로고
    • Studies on the interactions of kaempferol to calcineurin by spectroscopic methods and docking
    • Studies on the interactions of kaempferol to calcineurin by spectroscopic methods and docking. H Lei Y Qi ZG Jia WL Lin Q Wei, Biochim Biophys Acta 2009 1794 1269 1275
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1269-1275
    • Lei, H.1    Qi, Y.2    Jia, Z.G.3    Lin, W.L.4    Wei, Q.5
  • 96
    • 66549084491 scopus 로고    scopus 로고
    • Inhibitory effects of flavonoids on TNF-alpha-induced IL-8 gene expression in HEK 293 cells
    • Inhibitory effects of flavonoids on TNF-alpha-induced IL-8 gene expression in HEK 293 cells. S Lee YJ Kim S Kwon Y Lee SY Choi J Park HJ Kwon, BMB Rep 2009 42 265 270
    • (2009) BMB Rep , vol.42 , pp. 265-270
    • Lee, S.1    Kim, Y.J.2    Kwon, S.3    Lee, Y.4    Choi, S.Y.5    Park, J.6    Kwon, H.J.7
  • 97
    • 1642538958 scopus 로고    scopus 로고
    • Barbiturates directly inhibit the calmodulin/calcineurin complex: A novel mechanism of inhibition of nuclear factor of activated T cells
    • Barbiturates directly inhibit the calmodulin/calcineurin complex: a novel mechanism of inhibition of nuclear factor of activated T cells. M Humar SE Pischke T Loop A Hoetzel R Schmidt C Klaas HL Pahl KK Geiger BH Pannen, Mol Pharmacol 2004 65 350 361
    • (2004) Mol Pharmacol , vol.65 , pp. 350-361
    • Humar, M.1    Pischke, S.E.2    Loop, T.3    Hoetzel, A.4    Schmidt, R.5    Klaas, C.6    Pahl, H.L.7    Geiger, K.K.8    Pannen, B.H.9
  • 98
    • 36348954510 scopus 로고    scopus 로고
    • Repression of T-cell function by thionamides is mediated by inhibition of the activator protein-1/nuclear factor of activated T-cells pathway and is associated with a common structure
    • Repression of T-cell function by thionamides is mediated by inhibition of the activator protein-1/nuclear factor of activated T-cells pathway and is associated with a common structure. M Humar H Dohrmann P Stein N Andriopoulos U Goebel B Heimrich M Roesslein R Schmidt CI Schwer A Hoetzel, et al. Mol Pharmacol 2007 72 1647 1656
    • (2007) Mol Pharmacol , vol.72 , pp. 1647-1656
    • Humar, M.1    Dohrmann, H.2    Stein, P.3    Andriopoulos, N.4    Goebel, U.5    Heimrich, B.6    Roesslein, M.7    Schmidt, R.8    Schwer, C.I.9    Hoetzel, A.10
  • 100
    • 0040437952 scopus 로고    scopus 로고
    • The effects of anesthesia with thiopental on T lymphocyte responses to antigen and mitogens in vivo and in vitro
    • The effects of anesthesia with thiopental on T lymphocyte responses to antigen and mitogens in vivo and in vitro. C Correa-Sales CE Tosta LV Rizzo, Int J Immunopharmacol 1997 19 117 128
    • (1997) Int J Immunopharmacol , vol.19 , pp. 117-128
    • Correa-Sales, C.1    Tosta, C.E.2    Rizzo, L.V.3
  • 101
    • 0041624233 scopus 로고    scopus 로고
    • Structure-based design of a highly selective catalytic site-directed inhibitor of Ser/Thr protein phosphatase 2B (calcineurin)
    • Structure-based design of a highly selective catalytic site-directed inhibitor of Ser/Thr protein phosphatase 2B (calcineurin). Y Baba N Hirukawa N Tanohira M Sodeoka, J Am Chem Soc 2003 125 9740 9749
    • (2003) J Am Chem Soc , vol.125 , pp. 9740-9749
    • Baba, Y.1    Hirukawa, N.2    Tanohira, N.3    Sodeoka, M.4
  • 102
    • 22844451947 scopus 로고    scopus 로고
    • Optically active cantharidin analogues possessing selective inhibitory activity on Ser/Thr protein phosphatase 2B (calcineurin): Implications for the binding mode
    • Optically active cantharidin analogues possessing selective inhibitory activity on Ser/Thr protein phosphatase 2B (calcineurin): implications for the binding mode. Y Baba N Hirukawa M Sodeoka, Bioorg Med Chem 2005 13 5164 5170
    • (2005) Bioorg Med Chem , vol.13 , pp. 5164-5170
    • Baba, Y.1    Hirukawa, N.2    Sodeoka, M.3
  • 103
    • 33845975586 scopus 로고    scopus 로고
    • Gossypol inhibits calcineurin phosphatase activity at multiple sites
    • Gossypol inhibits calcineurin phosphatase activity at multiple sites. NJ Carruthers MK Dowd PM Stemmer, Eur J Pharmacol 2007 555 106 114
    • (2007) Eur J Pharmacol , vol.555 , pp. 106-114
    • Carruthers, N.J.1    Dowd, M.K.2    Stemmer, P.M.3
  • 104
    • 66749177977 scopus 로고    scopus 로고
    • The immunosuppressive effect of gossypol in mice is mediated by inhibition of lymphocyte proliferation and by induction of cell apoptosis
    • The immunosuppressive effect of gossypol in mice is mediated by inhibition of lymphocyte proliferation and by induction of cell apoptosis. WB Xu LH Xu HS Lu DY Ou-Yang HJ Shi JF Di XH He, Acta Pharmacol Sin 2009 30 597 604
    • (2009) Acta Pharmacol Sin , vol.30 , pp. 597-604
    • Xu, W.B.1    Xu, L.H.2    Lu, H.S.3    Ou-Yang, D.Y.4    Shi, H.J.5    Di, J.F.6    He, X.H.7
  • 105
    • 11144296876 scopus 로고    scopus 로고
    • The calcineurin inhibitor gossypol impairs growth, cell signalling and development in Dictyostelium discoideum
    • The calcineurin inhibitor gossypol impairs growth, cell signalling and development in Dictyostelium discoideum. B Weissenmayer K Boeckeler A Lahrz R Mutzel, FEMS Microbiol Lett 2005 242 19 25
    • (2005) FEMS Microbiol Lett , vol.242 , pp. 19-25
    • Weissenmayer, B.1    Boeckeler, K.2    Lahrz, A.3    Mutzel, R.4
  • 106
  • 107
    • 0030812936 scopus 로고    scopus 로고
    • Gossypol modification of Ala-1 of secreted phospholipase A2: A probe for the kinetic effects of sulfate glycoconjugates
    • Gossypol modification of Ala-1 of secreted phospholipase A2: a probe for the kinetic effects of sulfate glycoconjugates. BZ Yu J Rogers G Ranadive S Baker DC Wilton R Apitz-Castro MK Jain, Biochemistry 1997 36 12400 12411
    • (1997) Biochemistry , vol.36 , pp. 12400-12411
    • Yu, B.Z.1    Rogers, J.2    Ranadive, G.3    Baker, S.4    Wilton, D.C.5    Apitz-Castro, R.6    Jain, M.K.7
  • 108
    • 0024580574 scopus 로고
    • Modulation of 4'-(9-acridinylamino)methanesulfon-m-anisidide-induced, topoisomerase II-mediated DNA cleavage by gossypol
    • Modulation of 4'-(9-acridinylamino)methanesulfon-m-anisidide-induced, topoisomerase II-mediated DNA cleavage by gossypol. RC Adlakha CL Ashorn D Chan LA Zwelling, Cancer Res 1989 49 2052 2058
    • (1989) Cancer Res , vol.49 , pp. 2052-2058
    • Adlakha, R.C.1    Ashorn, C.L.2    Chan, D.3    Zwelling, L.A.4
  • 109
    • 0032549595 scopus 로고    scopus 로고
    • P53 transactivation of the HIV-1 long terminal repeat is blocked by PD 14 a calcineurin-inhibitor with anti-HIV properties
    • p53 transactivation of the HIV-1 long terminal repeat is blocked by PD 14 a calcineurin-inhibitor with anti-HIV properties. A Gualberto G Marquez M Carballo GL Youngblood SW Hunt 3rd AS Baldwin F Sobrino, J Biol Chem 1998 273 12 7088 7093
    • (1998) J Biol Chem , vol.273 , Issue.12 , pp. 7088-7093
    • Gualberto, A.1    Marquez, G.2    Carballo, M.3    Youngblood, G.L.4    Baldwin, A.S.5    Sobrino, F.6
  • 111
    • 66149096223 scopus 로고    scopus 로고
    • Inhibiting the calcineurin-NFAT (nuclear factor of activated T cells) signaling pathway with a regulator of calcineurin-derived peptide without affecting general calcineurin phosphatase activity
    • Inhibiting the calcineurin-NFAT (nuclear factor of activated T cells) signaling pathway with a regulator of calcineurin-derived peptide without affecting general calcineurin phosphatase activity. MC Mulero A Aubareda M Orzaez J Messeguer E Serrano-Candelas S Martinez-Hoyer A Messeguer E Perez-Paya M Perez-Riba, J Biol Chem 2009 284 9394 9401
    • (2009) J Biol Chem , vol.284 , pp. 9394-9401
    • Mulero, M.C.1    Aubareda, A.2    Orzaez, M.3    Messeguer, J.4    Serrano-Candelas, E.5    Martinez-Hoyer, S.6    Messeguer, A.7    Perez-Paya, E.8    Perez-Riba, M.9
  • 114
    • 2442714017 scopus 로고    scopus 로고
    • Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules
    • Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules. MH Roehrl S Kang J Aramburu G Wagner A Rao PG Hogan, Proc Natl Acad Sci USA 2004 101 7554 7559
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7554-7559
    • Roehrl, M.H.1    Kang, S.2    Aramburu, J.3    Wagner, G.4    Rao, A.5    Hogan, P.G.6
  • 115
    • 27844549820 scopus 로고    scopus 로고
    • Inhibition of the calcineurin-NFAT interaction by small organic molecules reflects binding at an allosteric site
    • Inhibition of the calcineurin-NFAT interaction by small organic molecules reflects binding at an allosteric site. S Kang H Li A Rao PG Hogan, J Biol Chem 2005 280 37698 37706
    • (2005) J Biol Chem , vol.280 , pp. 37698-37706
    • Kang, S.1    Li, H.2    Rao, A.3    Hogan, P.G.4
  • 119
    • 0037407834 scopus 로고    scopus 로고
    • A pyrazole derivative, YM-58483 potently inhibits store-operated sustained Ca2+ influx and IL-2 production in T lymphocytes
    • A pyrazole derivative, YM-58483 potently inhibits store-operated sustained Ca2+ influx and IL-2 production in T lymphocytes. J Ishikawa K Ohga T Yoshino R Takezawa A Ichikawa H Kubota T Yamada, J Immunol 2003 170 9 4441 4449
    • (2003) J Immunol , vol.170 , Issue.9 , pp. 4441-4449
    • Ishikawa, J.1    Ohga, K.2    Yoshino, T.3    Takezawa, R.4    Ichikawa, A.5    Kubota, H.6    Yamada, T.7
  • 120
    • 1842582607 scopus 로고    scopus 로고
    • Potent inhibition of Ca2+ release-activated Ca2+ channels and T-lymphocyte activation by the pyrazole derivative BTP2
    • Potent inhibition of Ca2+ release-activated Ca2+ channels and T-lymphocyte activation by the pyrazole derivative BTP2. C Zitt B Strauss EC Schwarz N Spaeth G Rast A Hatzelmann M Hoth, J Biol Chem 2004 279 12427 12437
    • (2004) J Biol Chem , vol.279 , pp. 12427-12437
    • Zitt, C.1    Strauss, B.2    Schwarz, E.C.3    Spaeth, N.4    Rast, G.5    Hatzelmann, A.6    Hoth, M.7
  • 121
    • 33645105461 scopus 로고    scopus 로고
    • A pyrazole derivative potently inhibits lymphocyte Ca2+ influx and cytokine production by facilitating transient receptor potential melastatin 4 channel activity
    • A pyrazole derivative potently inhibits lymphocyte Ca2+ influx and cytokine production by facilitating transient receptor potential melastatin 4 channel activity. R Takezawa H Cheng A Beck J Ishikawa P Launay H Kubota JP Kinet A Fleig T Yamada R Penner, Mol Pharmacol 2006 69 1413 1420
    • (2006) Mol Pharmacol , vol.69 , pp. 1413-1420
    • Takezawa, R.1    Cheng, H.2    Beck, A.3    Ishikawa, J.4    Launay, P.5    Kubota, H.6    Kinet, J.P.7    Fleig, A.8    Yamada, T.9    Penner, R.10
  • 122
    • 33847406960 scopus 로고    scopus 로고
    • YM-58483 a selective CRAC channel inhibitor, prevents antigen-induced airway eosinophilia and late phase asthmatic responses via Th2 cytokine inhibition in animal models
    • YM-58483 a selective CRAC channel inhibitor, prevents antigen-induced airway eosinophilia and late phase asthmatic responses via Th2 cytokine inhibition in animal models. T Yoshino J Ishikawa K Ohga T Morokata R Takezawa H Morio Y Okada K Honda T Yamada, Eur J Pharmacol 2007 560 2-3 225 233
    • (2007) Eur J Pharmacol , vol.560 , Issue.2-3 , pp. 225-233
    • Yoshino, T.1    Ishikawa, J.2    Ohga, K.3    Morokata, T.4    Takezawa, R.5    Morio, H.6    Okada, Y.7    Honda, K.8    Yamada, T.9
  • 123
    • 55249104159 scopus 로고    scopus 로고
    • Characterization of YM-58483/BTP2, a novel store-operated Ca2+ entry blocker, on T cell-mediated immune responses in vivo
    • Characterization of YM-58483/BTP2, a novel store-operated Ca2+ entry blocker, on T cell-mediated immune responses in vivo. K Ohga R Takezawa Y Arakida Y Shimizu J Ishikawa, Int Immunopharmacol 2008 8 1787 1792
    • (2008) Int Immunopharmacol , vol.8 , pp. 1787-1792
    • Ohga, K.1    Takezawa, R.2    Arakida, Y.3    Shimizu, Y.4    Ishikawa, J.5
  • 124
    • 33947660516 scopus 로고    scopus 로고
    • Potent inhibition of store-operated Ca2+ influx and superoxide production in HL60 cells and polymorphonuclear neutrophils by the pyrazole derivative BTP2
    • Potent inhibition of store-operated Ca2+ influx and superoxide production in HL60 cells and polymorphonuclear neutrophils by the pyrazole derivative BTP2. N Steinckwich JP Frippiat MJ Stasia M Erard R Boxio C Tankosic I Doignon O Nusse, J Leukoc Biol 2007 81 1054 1064
    • (2007) J Leukoc Biol , vol.81 , pp. 1054-1064
    • Steinckwich, N.1    Frippiat, J.P.2    Stasia, M.J.3    Erard, M.4    Boxio, R.5    Tankosic, C.6    Doignon, I.7    Nusse, O.8
  • 127
    • 34447529504 scopus 로고    scopus 로고
    • Nuclear translocation of calcineurin Abeta but not calcineurin Aalpha by platelet-derived growth factor in rat aortic smooth muscle
    • Nuclear translocation of calcineurin Abeta but not calcineurin Aalpha by platelet-derived growth factor in rat aortic smooth muscle. RI Jabr AJ Wilson MH Riddervold AH Jenkins BA Perrino LH Clapp, Am J Physiol Cell Physiol 2007 292 2213 2225
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 32213-2225
    • Jabr, R.I.1    Wilson, A.J.2    Riddervold, M.H.3    Jenkins, A.H.4    Perrino, B.A.5    Clapp, L.H.6
  • 131
    • 24744469860 scopus 로고    scopus 로고
    • Conversion of acetaminophen to the bioactive N-acylphenolamine AM404 via fatty acid amide hydrolase-dependent arachidonic acid conjugation in the nervous system
    • Conversion of acetaminophen to the bioactive N-acylphenolamine AM404 via fatty acid amide hydrolase-dependent arachidonic acid conjugation in the nervous system. ED Hogestatt BA Jonsson A Ermund DA Andersson H Bjork JP Alexander BF Cravatt AI Basbaum PM Zygmunt, J Biol Chem 2005 280 31405 31412
    • (2005) J Biol Chem , vol.280 , pp. 31405-31412
    • Hogestatt, E.D.1    Jonsson, B.A.2    Ermund, A.3    Andersson, D.A.4    Bjork, H.5    Alexander, J.P.6    Cravatt, B.F.7    Basbaum, A.I.8    Zygmunt, P.M.9
  • 134
    • 65449131213 scopus 로고    scopus 로고
    • The new salicylate derivative UR-1505 modulates the Th2/humoral response in a dextran sodium sulphate model of colitis that resembles ulcerative colitis
    • The new salicylate derivative UR-1505 modulates the Th2/humoral response in a dextran sodium sulphate model of colitis that resembles ulcerative colitis. E Bailon J Roman I Ramis P Michelena D Balsa M Merlos A Zarzuelo J Galvez M Comalada, J Pharmacol Sci 2009 109 315 318
    • (2009) J Pharmacol Sci , vol.109 , pp. 315-318
    • Bailon, E.1    Roman, J.2    Ramis, I.3    Michelena, P.4    Balsa, D.5    Merlos, M.6    Zarzuelo, A.7    Galvez, J.8    Comalada, M.9
  • 137
    • 0026632557 scopus 로고
    • FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin
    • FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. SJ O'Keefe J Tamura RL Kincaid MJ Tocci EA O'Neill, Nature 1992 357 692 694
    • (1992) Nature , vol.357 , pp. 692-694
    • O'Keefe, S.J.1    Tamura, J.2    Kincaid, R.L.3    Tocci, M.J.4    O'Neill, E.A.5
  • 139
    • 64049109504 scopus 로고    scopus 로고
    • Anti-inflammatory effects of 5-HT receptor antagonist, tropisetron on experimental colitis in rats
    • Anti-inflammatory effects of 5-HT receptor antagonist, tropisetron on experimental colitis in rats. K Mousavizadeh R Rahimian G Fakhfouri FS Aslani P Ghafourifar, Eur J Clin Invest 2009 39 375 383
    • (2009) Eur J Clin Invest , vol.39 , pp. 375-383
    • Mousavizadeh, K.1    Rahimian, R.2    Fakhfouri, G.3    Aslani, F.S.4    Ghafourifar, P.5
  • 140
  • 143
    • 0029863033 scopus 로고    scopus 로고
    • Calcineurin protein phosphatase activity in peripheral blood lymphocytes
    • Calcineurin protein phosphatase activity in peripheral blood lymphocytes. F Rusnak AH Beressi A Haddy A Tefferi, Bone Marrow Transplant 1996 17 309 313
    • (1996) Bone Marrow Transplant , vol.17 , pp. 309-313
    • Rusnak, F.1    Beressi, A.H.2    Haddy, A.3    Tefferi, A.4
  • 144
    • 0028904145 scopus 로고
    • Calmodulin, a junction between two independent immunosuppressive pathways in Jurkat T cells
    • Calmodulin, a junction between two independent immunosuppressive pathways in Jurkat T cells. C Aussel JP Breittmayer C Pelassy A Bernard, J Biol Chem 1995 270 8032 8036
    • (1995) J Biol Chem , vol.270 , pp. 8032-8036
    • Aussel, C.1    Breittmayer, J.P.2    Pelassy, C.3    Bernard, A.4
  • 145
    • 73349127476 scopus 로고    scopus 로고
    • Oral administration of 1, 4-aryl-2-mercaptoimidazole (KRM-III) inhibits T cell proliferation and reduces clinical severity in murine experimental autoimmune encephalomyelitis model
    • Oral administration of 1, 4-aryl-2-mercaptoimidazole (KRM-III) inhibits T cell proliferation and reduces clinical severity in murine experimental autoimmune encephalomyelitis model. EJ Jung M Hur YL Kim GH Lee J Kim I Kim M Lee HK Han MS Kim S Hwang, et al. J Pharmacol Exp Ther 2009
    • (2009) J Pharmacol Exp Ther
    • Jung, E.J.1    Hur, M.2    Kim, Y.L.3    Lee, G.H.4    Kim, J.5    Kim, I.6    Lee, M.7    Han, H.K.8    Kim, M.S.9    Hwang, S.10
  • 146
    • 1342280967 scopus 로고    scopus 로고
    • Caffeic acid phenethyl ester inhibits T-cell activation by targeting both nuclear factor of activated T-cells and NF-kappaB transcription factors
    • Caffeic acid phenethyl ester inhibits T-cell activation by targeting both nuclear factor of activated T-cells and NF-kappaB transcription factors. N Marquez R Sancho A Macho MA Calzado BL Fiebich E Munoz, J Pharmacol Exp Ther 2004 308 993 1001
    • (2004) J Pharmacol Exp Ther , vol.308 , pp. 993-1001
    • Marquez, N.1    Sancho, R.2    MacHo, A.3    Calzado, M.A.4    Fiebich, B.L.5    Munoz, E.6
  • 147
    • 0041655892 scopus 로고    scopus 로고
    • Propolis and some of its constituents down-regulate DNA synthesis and inflammatory cytokine production but induce TGF-beta1 production of human immune cells
    • Propolis and some of its constituents down-regulate DNA synthesis and inflammatory cytokine production but induce TGF-beta1 production of human immune cells. S Ansorge D Reinhold U Lendeckel, Z Naturforsch [C] 2003 58 580 589
    • (2003) Z Naturforsch [C] , vol.58 , pp. 580-589
    • Ansorge, S.1    Reinhold, D.2    Lendeckel, U.3
  • 148
    • 0029810902 scopus 로고    scopus 로고
    • Caffeic acid phenethyl ester is a potent and specific inhibitor of activation of nuclear transcription factor NF-kappa B
    • Caffeic acid phenethyl ester is a potent and specific inhibitor of activation of nuclear transcription factor NF-kappa B. K Natarajan S Singh TR Burke Jr D Grunberger BB Aggarwal, Proc Natl Acad Sci USA 1996 93 9090 9095
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9090-9095
    • Natarajan, K.1    Singh, S.2    Grunberger, D.3    Aggarwal, B.B.4
  • 149
    • 0030686469 scopus 로고    scopus 로고
    • 3-(13-Hydroxytridecyl)-1-[13-(3-pyridyl)tridecyl]pyridinium chloride (YM-53792), a novel inhibitor of NF-AT activation
    • 3-(13-Hydroxytridecyl)-1-[13-(3-pyridyl)tridecyl]pyridinium chloride (YM-53792), a novel inhibitor of NF-AT activation. S Kuromitsu M Fukunaga AC Lennard Y Masuho S Nakada, Biochem Pharmacol 1997 54 999 1005
    • (1997) Biochem Pharmacol , vol.54 , pp. 999-1005
    • Kuromitsu, S.1    Fukunaga, M.2    Lennard, A.C.3    Masuho, Y.4    Nakada, S.5
  • 155
    • 16644372348 scopus 로고    scopus 로고
    • Quinolone alkaloids with inhibitory activity against nuclear factor of activated T cells from the fruits of Evodia rutaecarpa
    • Quinolone alkaloids with inhibitory activity against nuclear factor of activated T cells from the fruits of Evodia rutaecarpa. HZ Jin JH Lee D Lee HS Lee YS Hong YH Kim JJ Lee, Biol Pharm Bull 2004 27 926 928
    • (2004) Biol Pharm Bull , vol.27 , pp. 926-928
    • Jin, H.Z.1    Lee, J.H.2    Lee, D.3    Lee, H.S.4    Hong, Y.S.5    Kim, Y.H.6    Lee, J.J.7
  • 156
    • 29944437543 scopus 로고    scopus 로고
    • Phenolic constituents with inhibitory activity against NFAT transcription from Desmos chinensis
    • Phenolic constituents with inhibitory activity against NFAT transcription from Desmos chinensis. PV Kiem CV Minh HT Huong JJ Lee IS Lee YH Kim, Arch Pharm Res 2005 28 1345 1349
    • (2005) Arch Pharm Res , vol.28 , pp. 1345-1349
    • Kiem, P.V.1    Minh, C.V.2    Huong, H.T.3    Lee, J.J.4    Lee, I.S.5    Kim, Y.H.6
  • 157
    • 18744380076 scopus 로고    scopus 로고
    • New inhibitor against nuclear factor of activated T cells transcription from Ribes fasciculatum var. chinense
    • New inhibitor against nuclear factor of activated T cells transcription from Ribes fasciculatum var. chinense. NT Dat XF Cai Q Shen IS Lee YH Kim, Chem Pharm Bull (Tokyo) 2005 53 114 117
    • (2005) Chem Pharm Bull (Tokyo) , vol.53 , pp. 114-117
    • Dat, N.T.1    Cai, X.F.2    Shen, Q.3    Lee, I.S.4    Kim, Y.H.5
  • 158
  • 160
    • 4944246603 scopus 로고    scopus 로고
    • Diterpenoids with inhibitory activity against NFAT transcription factor from Acanthopanax koreanum
    • DOI 10.1002/ptr.1523
    • Diterpenoids with inhibitory activity against NFAT transcription factor from Acanthopanax koreanum. XF Cai IS Lee NT Dat G Shen YH Kim, Phytother Res 2004 18 677 680 (Pubitemid 39329722)
    • (2004) Phytotherapy Research , vol.18 , Issue.8 , pp. 677-680
    • Xing, F.C.1    Im, S.L.2    Nguyen, T.D.3    Shen, G.4    Young, H.K.5
  • 161
    • 8444246258 scopus 로고    scopus 로고
    • Oleanane triterpenoids with inhibitory activity against NFAT transcription factor from Liquidambar formosana
    • DOI 10.1248/bpb.27.426
    • Oleanane triterpenoids with inhibitory activity against NFAT transcription factor from Liquidambar formosana. NT Dat IS Lee XF Cai G Shen YH Kim, Biol Pharm Bull 2004 27 426 428 (Pubitemid 41685493)
    • (2004) Biological and Pharmaceutical Bulletin , vol.27 , Issue.3 , pp. 426-428
    • Dat, N.T.1    Lee, I.S.2    Cai, X.F.3    Shen, G.4    Kim, Y.H.5
  • 162
    • 0345505707 scopus 로고    scopus 로고
    • Lignans with inhibitory activity against NFAT transcription from Schisandra chinensis
    • Lignans with inhibitory activity against NFAT transcription from Schisandra chinensis. IS Lee HK Lee NT Dat MS Lee JW Kim DS Na YH Kim, Planta Med 2003 69 63 64
    • (2003) Planta Med , vol.69 , pp. 63-64
    • Lee, I.S.1    Lee, H.K.2    Dat, N.T.3    Lee, M.S.4    Kim, J.W.5    Na, D.S.6    Kim, Y.H.7
  • 163
    • 0030473711 scopus 로고    scopus 로고
    • Competitive inhibition of calcineurin phosphatase activity by its autoinhibitory domain
    • Competitive inhibition of calcineurin phosphatase activity by its autoinhibitory domain. JK Sagoo DA Fruman S Wesselborg CT Walsh BE Bierer, Biochem J 1996 320 Pt 3 879 884
    • (1996) Biochem J , vol.320 , Issue.PT 3 , pp. 879-884
    • Sagoo, J.K.1    Fruman, D.A.2    Wesselborg, S.3    Walsh, C.T.4    Bierer, B.E.5
  • 164
    • 0024991506 scopus 로고
    • Identification of an autoinhibitory domain in calcineurin
    • Identification of an autoinhibitory domain in calcineurin. Y Hashimoto BA Perrino TR Soderling, J Biol Chem 1990 265 1924 1927
    • (1990) J Biol Chem , vol.265 , pp. 1924-1927
    • Hashimoto, Y.1    Perrino, B.A.2    Soderling, T.R.3
  • 165
    • 0028855841 scopus 로고
    • Calcium regulation of calcineurin phosphatase activity by its B subunit and calmodulin. Role of the autoinhibitory domain
    • Calcium regulation of calcineurin phosphatase activity by its B subunit and calmodulin. Role of the autoinhibitory domain. BA Perrino LY Ng TR Soderling, J Biol Chem 1995 270 340 346
    • (1995) J Biol Chem , vol.270 , pp. 340-346
    • Perrino, B.A.1    Ng, L.Y.2    Soderling, T.R.3
  • 166
    • 0033485861 scopus 로고    scopus 로고
    • Regulation of calcineurin phosphatase activity by its autoinhibitory domain
    • Regulation of calcineurin phosphatase activity by its autoinhibitory domain. BA Perrino, Arch Biochem Biophys 1999 372 159 165
    • (1999) Arch Biochem Biophys , vol.372 , pp. 159-165
    • Perrino, B.A.1
  • 170
    • 0032849010 scopus 로고    scopus 로고
    • Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A
    • Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A. J Aramburu MB Yaffe C Lopez-Rodriguez LC Cantley PG Hogan A Rao, Science 1999 285 2129 2133
    • (1999) Science , vol.285 , pp. 2129-2133
    • Aramburu, J.1    Yaffe, M.B.2    Lopez-Rodriguez, C.3    Cantley, L.C.4    Hogan, P.G.5    Rao, A.6
  • 172
    • 0037073758 scopus 로고    scopus 로고
    • Mapping the protein phosphatase-2B anchoring site on AKAP79. Binding and inhibition of phosphatase activity are mediated by residues 315-360
    • Mapping the protein phosphatase-2B anchoring site on AKAP79. Binding and inhibition of phosphatase activity are mediated by residues 315-360. ML Dell'Acqua KL Dodge SJ Tavalin JD Scott, J Biol Chem 2002 277 48796 48802
    • (2002) J Biol Chem , vol.277 , pp. 48796-48802
    • Dell'Acqua, M.L.1    Dodge, K.L.2    Tavalin, S.J.3    Scott, J.D.4
  • 174
    • 0032101282 scopus 로고    scopus 로고
    • Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes
    • Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes. L Sun HD Youn C Loh M Stolow W He JO Liu, Immunity 1998 8 703 711
    • (1998) Immunity , vol.8 , pp. 703-711
    • Sun, L.1    Youn, H.D.2    Loh, C.3    Stolow, M.4    He, W.5    Liu, J.O.6
  • 175
    • 29144484163 scopus 로고    scopus 로고
    • Multiple roles of the DSCR1 (Adapt78 or RCAN1) gene and its protein product calcipressin 1 (or RCAN1) in disease
    • Multiple roles of the DSCR1 (Adapt78 or RCAN1) gene and its protein product calcipressin 1 (or RCAN1) in disease. CD Harris G Ermak KJ Davies, Cell Mol Life Sci 2005 62 2477 2486
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2477-2486
    • Harris, C.D.1    Ermak, G.2    Davies, K.J.3
  • 176
    • 24944484976 scopus 로고    scopus 로고
    • Identification of a peptide fragment of DSCR1 that competitively inhibits calcineurin activity in vitro and in vivo
    • Identification of a peptide fragment of DSCR1 that competitively inhibits calcineurin activity in vitro and in vivo. B Chan G Greenan F McKeon T Ellenberger, Proc Natl Acad Sci USA 2005 102 13075 13080
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13075-13080
    • Chan, B.1    Greenan, G.2    McKeon, F.3    Ellenberger, T.4
  • 177
    • 33744832043 scopus 로고    scopus 로고
    • Functional characterization of the calcipressin 1 motif that suppresses calcineurin-mediated NFAT-dependent cytokine gene expression in human T cells
    • Functional characterization of the calcipressin 1 motif that suppresses calcineurin-mediated NFAT-dependent cytokine gene expression in human T cells. A Aubareda MC Mulero M Perez-Riba, Cell Signal 2006 18 1430 1438
    • (2006) Cell Signal , vol.18 , pp. 1430-1438
    • Aubareda, A.1    Mulero, M.C.2    Perez-Riba, M.3
  • 179
    • 66349086505 scopus 로고    scopus 로고
    • Domain architecture of the regulators of calcineurin (RCANs) and identification of a divergent RCAN in yeast
    • Domain architecture of the regulators of calcineurin (RCANs) and identification of a divergent RCAN in yeast. S Mehta H Li PG Hogan KW Cunningham, Mol Cell Biol 2009 29 2777 2793
    • (2009) Mol Cell Biol , vol.29 , pp. 2777-2793
    • Mehta, S.1    Li, H.2    Hogan, P.G.3    Cunningham, K.W.4
  • 180
    • 0034691195 scopus 로고    scopus 로고
    • A second calcineurin binding site on the NFAT regulatory domain
    • A second calcineurin binding site on the NFAT regulatory domain. S Park M Uesugi GL Verdine, Proc Natl Acad Sci USA 2000 97 7130 7135
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7130-7135
    • Park, S.1    Uesugi, M.2    Verdine, G.L.3
  • 181
    • 0035451615 scopus 로고    scopus 로고
    • Inhibition of NFATx activation by an oligopeptide: Disrupting the interaction of NFATx with calcineurin
    • Inhibition of NFATx activation by an oligopeptide: disrupting the interaction of NFATx with calcineurin. J Liu K Arai N Arai, J Immunol 2001 167 2677 2687
    • (2001) J Immunol , vol.167 , pp. 2677-2687
    • Liu, J.1    Arai, K.2    Arai, N.3
  • 183
    • 0034234963 scopus 로고    scopus 로고
    • A conserved family of calcineurin regulators
    • A conserved family of calcineurin regulators. TJ Kingsbury KW Cunningham, Genes Dev 2000 14 1595 1604
    • (2000) Genes Dev , vol.14 , pp. 1595-1604
    • Kingsbury, T.J.1    Cunningham, K.W.2
  • 184
  • 186
    • 0042932364 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation. B Gebert W Fischer E Weiss R Hoffmann R Haas, Science 2003 301 1099 1102
    • (2003) Science , vol.301 , pp. 1099-1102
    • Gebert, B.1    Fischer, W.2    Weiss, E.3    Hoffmann, R.4    Haas, R.5
  • 187
    • 2442682964 scopus 로고    scopus 로고
    • Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion
    • Inhibition of primary human T cell proliferation by Helicobacter pylori vacuolating toxin (VacA) is independent of VacA effects on IL-2 secretion. MS Sundrud VJ Torres D Unutmaz TL Cover, Proc Natl Acad Sci USA 2004 101 7727 7732
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7727-7732
    • Sundrud, M.S.1    Torres, V.J.2    Unutmaz, D.3    Cover, T.L.4
  • 189
    • 0032563244 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of the cellular phosphatase calcineurin
    • A viral mechanism for inhibition of the cellular phosphatase calcineurin. JE Miskin CC Abrams LC Goatley LK Dixon, Science 1998 281 562 565
    • (1998) Science , vol.281 , pp. 562-565
    • Miskin, J.E.1    Abrams, C.C.2    Goatley, L.C.3    Dixon, L.K.4
  • 190
    • 42149193168 scopus 로고    scopus 로고
    • A238L inhibits NF-ATc2, NF-kappa B, and c-Jun activation through a novel mechanism involving protein kinase C-theta-mediated up-regulation of the amino-terminal transactivation domain of p300
    • A238L inhibits NF-ATc2, NF-kappa B, and c-Jun activation through a novel mechanism involving protein kinase C-theta-mediated up-regulation of the amino-terminal transactivation domain of p300. AG Granja ND Perkins Y Revilla, J Immunol 2008 180 2429 2442
    • (2008) J Immunol , vol.180 , pp. 2429-2442
    • Granja, A.G.1    Perkins, N.D.2    Revilla, Y.3
  • 191
    • 0034331937 scopus 로고    scopus 로고
    • Two distinct action mechanisms of immunophilin-ligand complexes for the blockade of T-cell activation
    • Two distinct action mechanisms of immunophilin-ligand complexes for the blockade of T-cell activation. S Matsuda F Shibasaki K Takehana H Mori E Nishida S Koyasu, EMBO Rep 2000 1 428 434
    • (2000) EMBO Rep , vol.1 , pp. 428-434
    • Matsuda, S.1    Shibasaki, F.2    Takehana, K.3    Mori, H.4    Nishida, E.5    Koyasu, S.6
  • 192
    • 11144229616 scopus 로고    scopus 로고
    • The viral protein A238L inhibits cyclooxygenase-2 expression through a nuclear factor of activated T cell-dependent transactivation pathway
    • The viral protein A238L inhibits cyclooxygenase-2 expression through a nuclear factor of activated T cell-dependent transactivation pathway. AG Granja ML Nogal C Hurtado V Vila AL Carrascosa ML Salas M Fresno Y Revilla, J Biol Chem 2004 279 53736 53746
    • (2004) J Biol Chem , vol.279 , pp. 53736-53746
    • Granja, A.G.1    Nogal, M.L.2    Hurtado, C.3    Vila, V.4    Carrascosa, A.L.5    Salas, M.L.6    Fresno, M.7    Revilla, Y.8
  • 193
    • 0033809260 scopus 로고    scopus 로고
    • African swine fever virus protein A238L interacts with the cellular phosphatase calcineurin via a binding domain similar to that of NFAT
    • African swine fever virus protein A238L interacts with the cellular phosphatase calcineurin via a binding domain similar to that of NFAT. JE Miskin CC Abrams LK Dixon, J Virol 2000 74 9412 9420
    • (2000) J Virol , vol.74 , pp. 9412-9420
    • Miskin, J.E.1    Abrams, C.C.2    Dixon, L.K.3
  • 195
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics. C Bialojan A Takai, Biochem J 1988 256 283 290
    • (1988) Biochem J , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 196
    • 0026503434 scopus 로고
    • Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A
    • Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A. DA Fruman CB Klee BE Bierer SJ Burakoff, Proc Natl Acad Sci USA 1992 89 3686 3690
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3686-3690
    • Fruman, D.A.1    Klee, C.B.2    Bierer, B.E.3    Burakoff, S.J.4
  • 197
    • 0030591689 scopus 로고    scopus 로고
    • Preparation and in vitro activities of naphthyl and indolyl ether derivatives of the FK-506 related immunosuppressive macrolide ascomycin
    • Preparation and in vitro activities of naphthyl and indolyl ether derivatives of the FK-506 related immunosuppressive macrolide ascomycin. PJ Sinclair F Wong MJ Staruch GJ Wiederrecht WH Parsons F Dumont M Wyvratt, Bioorg Med Chem Lett 1996 6 2193 2196
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 2193-2196
    • Sinclair, P.J.1    Wong, F.2    Staruch, M.J.3    Wiederrecht, G.J.4    Parsons, W.H.5    Dumont, F.6    Wyvratt, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.