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Volumn 280, Issue 19, 2013, Pages 4739-4760

Viewing serine/threonine protein phosphatases through the eyes of drug designers

Author keywords

drug design; high throughput assay; serine threonine protein phosphatase; small molecule inhibitors; structure guided drug discovery

Indexed keywords

CALCINEURIN INHIBITOR; CYCLOSPORIN A; FOSTRIECIN; GUANABENZ; OKADAIC ACID; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOPROTEIN PHOSPHATASE 5; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROTEIN PHOSPHATASE 1 INHIBITOR; PROTEIN WIP1; RABEPRAZOLE; SALUBRINAL; SANGUINARINE; SERINE PROTEIN PHOSPHATASE; TACROLIMUS; THREONINE PROTEIN PHOSPHATASE; TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84884595522     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12481     Document Type: Review
Times cited : (62)

References (155)
  • 1
    • 26844571282 scopus 로고    scopus 로고
    • Multisite protein phosphorylation makes a good threshold but can be a poor switch
    • Gunawardena J, (2005) Multisite protein phosphorylation makes a good threshold but can be a poor switch. Proc Natl Acad Sci U S A 102, 14617-14622.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14617-14622
    • Gunawardena, J.1
  • 3
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T, (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80, 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 5
    • 84872502581 scopus 로고    scopus 로고
    • Challenges and opportunities in the development of protein phosphatase-directed therapeutics
    • De Munter S, Kohn M, &, Bollen M, (2013) Challenges and opportunities in the development of protein phosphatase-directed therapeutics. ACS Chem Biol 8, 36-45.
    • (2013) ACS Chem Biol , vol.8 , pp. 36-45
    • De Munter, S.1    Kohn, M.2    Bollen, M.3
  • 6
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • Cohen P, (2002) Protein kinases-the major drug targets of the twenty-first century? Nat Rev Drug Discov 1, 309-315.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 309-315
    • Cohen, P.1
  • 7
    • 22144456041 scopus 로고    scopus 로고
    • The promise of molecular targeted therapies: Protein kinase inhibitors in the treatment of cutaneous malignancies
    • Kondapalli L, Soltani K, &, Lacouture ME, (2005) The promise of molecular targeted therapies: protein kinase inhibitors in the treatment of cutaneous malignancies. J Am Acad Dermatol 53, 291-302.
    • (2005) J Am Acad Dermatol , vol.53 , pp. 291-302
    • Kondapalli, L.1    Soltani, K.2    Lacouture, M.E.3
  • 8
    • 63449112585 scopus 로고    scopus 로고
    • Therapeutic protein kinase inhibitors
    • Grant SK, (2009) Therapeutic protein kinase inhibitors. Cell Mol Life Sci 66, 1163-1177.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1163-1177
    • Grant, S.K.1
  • 9
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, &, Mann M, (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 10
    • 0026661583 scopus 로고
    • Signal integration at the level of protein kinases, protein phosphatases and their substrates
    • Cohen P, (1992) Signal integration at the level of protein kinases, protein phosphatases and their substrates. Trends Biochem Sci 17, 408-413.
    • (1992) Trends Biochem Sci , vol.17 , pp. 408-413
    • Cohen, P.1
  • 11
    • 0028359957 scopus 로고
    • Protein phosphatase 2A - A 'menage a trois'
    • Mayer-Jaekel RE, &, Hemmings BA, (1994) Protein phosphatase 2A-a 'menage a trois'. Trends Cell Biol 4, 287-291.
    • (1994) Trends Cell Biol , vol.4 , pp. 287-291
    • Mayer-Jaekel, R.E.1    Hemmings, B.A.2
  • 12
    • 79960726254 scopus 로고    scopus 로고
    • Phosphatases: Providing safe passage through mitotic exit
    • Wurzenberger C, &, Gerlich DW, (2011) Phosphatases: providing safe passage through mitotic exit. Nat Rev Mol Cell Biol 12, 469-482.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 469-482
    • Wurzenberger, C.1    Gerlich, D.W.2
  • 13
    • 84857215562 scopus 로고    scopus 로고
    • Phosphatases driving mitosis: Pushing the gas and lifting the brakes
    • Johnson ES, &, Kornbluth S, (2012) Phosphatases driving mitosis: pushing the gas and lifting the brakes. Prog Mol Biol Transl Sci 106, 327-341.
    • (2012) Prog Mol Biol Transl Sci , vol.106 , pp. 327-341
    • Johnson, E.S.1    Kornbluth, S.2
  • 14
    • 85027928854 scopus 로고    scopus 로고
    • Protein phosphatases and their regulation in the control of mitosis
    • Mochida S, &, Hunt T, (2012) Protein phosphatases and their regulation in the control of mitosis. EMBO Rep 13, 197-203.
    • (2012) EMBO Rep , vol.13 , pp. 197-203
    • Mochida, S.1    Hunt, T.2
  • 15
    • 0346728803 scopus 로고    scopus 로고
    • Functional diversity of protein phosphatase-1, a cellular economizer and reset button
    • Ceulemans H, &, Bollen M, (2004) Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol Rev 84, 1-39.
    • (2004) Physiol Rev , vol.84 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 16
    • 4143117908 scopus 로고    scopus 로고
    • Structure and mechanism of RNA polymerase II CTD phosphatases
    • Kamenski T, Heilmeier S, Meinhart A, &, Cramer P, (2004) Structure and mechanism of RNA polymerase II CTD phosphatases. Mol Cell 15, 399-407.
    • (2004) Mol Cell , vol.15 , pp. 399-407
    • Kamenski, T.1    Heilmeier, S.2    Meinhart, A.3    Cramer, P.4
  • 17
    • 15044348175 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatases: Life, death, and sleeping
    • Gallego M, &, Virshup DM, (2005) Protein serine/threonine phosphatases: life, death, and sleeping. Curr Opin Cell Biol 17, 197-202.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 197-202
    • Gallego, M.1    Virshup, D.M.2
  • 19
    • 84855881402 scopus 로고    scopus 로고
    • Exploiting the cancer genome: Strategies for the discovery and clinical development of targeted molecular therapeutics
    • Yap TA, &, Workman P, (2012) Exploiting the cancer genome: strategies for the discovery and clinical development of targeted molecular therapeutics. Annu Rev Pharmacol Toxicol 52, 549-573.
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 549-573
    • Yap, T.A.1    Workman, P.2
  • 20
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi Y, (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139, 468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 21
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution
    • Das AK, Helps NR, Cohen PT, &, Barford D, (1996) Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. EMBO J 15, 6798-6809.
    • (1996) EMBO J , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 22
    • 27744481299 scopus 로고    scopus 로고
    • Chemical inhibition of Wip1 phosphatase contributes to suppression of tumorigenesis
    • Belova GI, Demidov ON, Fornace AJ Jr, &, Bulavin DV, (2005) Chemical inhibition of Wip1 phosphatase contributes to suppression of tumorigenesis. Cancer Biol Ther 4, 1154-1158.
    • (2005) Cancer Biol Ther , vol.4 , pp. 1154-1158
    • Belova, G.I.1    Demidov, O.N.2    Fornace, Jr.A.J.3    Bulavin, D.V.4
  • 23
    • 33750703180 scopus 로고    scopus 로고
    • Development of a substrate-based cyclic phosphopeptide inhibitor of protein phosphatase 2Cdelta, Wip1
    • Yamaguchi H, Durell SR, Feng H, Bai Y, Anderson CW, &, Appella E, (2006) Development of a substrate-based cyclic phosphopeptide inhibitor of protein phosphatase 2Cdelta, Wip1. Biochemistry 45, 13193-13202.
    • (2006) Biochemistry , vol.45 , pp. 13193-13202
    • Yamaguchi, H.1    Durell, S.R.2    Feng, H.3    Bai, Y.4    Anderson, C.W.5    Appella, E.6
  • 24
    • 70349312573 scopus 로고    scopus 로고
    • Structure-activity relationship studies of fostriecin, cytostatin, and key analogs, with PP1, PP2A, PP5, and (beta12-beta13)-chimeras (PP1/PP2A and PP5/PP2A), provide further insight into the inhibitory actions of fostriecin family inhibitors
    • Swingle MR, Amable L, Lawhorn BG, Buck SB, Burke CP, Ratti P, Fischer KL, Boger DL, &, Honkanen RE, (2009) Structure-activity relationship studies of fostriecin, cytostatin, and key analogs, with PP1, PP2A, PP5, and (beta12-beta13)-chimeras (PP1/PP2A and PP5/PP2A), provide further insight into the inhibitory actions of fostriecin family inhibitors. J Pharmacol Exp Ther 331, 45-53.
    • (2009) J Pharmacol Exp Ther , vol.331 , pp. 45-53
    • Swingle, M.R.1    Amable, L.2    Lawhorn, B.G.3    Buck, S.B.4    Burke, C.P.5    Ratti, P.6    Fischer, K.L.7    Boger, D.L.8    Honkanen, R.E.9
  • 25
    • 84872783533 scopus 로고    scopus 로고
    • Small molecule tools for functional interrogation of protein tyrosine phosphatases
    • He R, Zeng LF, He Y, Zhang S, &, Zhang ZY, (2012) Small molecule tools for functional interrogation of protein tyrosine phosphatases. FEBS J 280, 731-750.
    • (2012) FEBS J , vol.280 , pp. 731-750
    • He, R.1    Zeng, L.F.2    He, Y.3    Zhang, S.4    Zhang, Z.Y.5
  • 26
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: Evolution of a catalytic scaffold
    • Allen KN, &, Dunaway-Mariano D, (2004) Phosphoryl group transfer: evolution of a catalytic scaffold. Trends Biochem Sci 29, 495-503.
    • (2004) Trends Biochem Sci , vol.29 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 27
    • 77951587359 scopus 로고    scopus 로고
    • Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1
    • Zhang M, Liu J, Kim Y, Dixon JE, Pfaff SL, Gill GN, Noel JP, &, Zhang Y, (2010) Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1. Protein Sci 19, 974-986.
    • (2010) Protein Sci , vol.19 , pp. 974-986
    • Zhang, M.1    Liu, J.2    Kim, Y.3    Dixon, J.E.4    Pfaff, S.L.5    Gill, G.N.6    Noel, J.P.7    Zhang, Y.8
  • 28
    • 44149124228 scopus 로고    scopus 로고
    • Cracking the RNA polymerase II CTD code
    • Egloff S, &, Murphy S, (2008) Cracking the RNA polymerase II CTD code. Trends Genet 24, 280-288.
    • (2008) Trends Genet , vol.24 , pp. 280-288
    • Egloff, S.1    Murphy, S.2
  • 30
    • 27844572915 scopus 로고    scopus 로고
    • Different strategies for carboxyl-terminal domain (CTD) recognition by serine 5-specific CTD phosphatases
    • Hausmann S, Koiwa H, Krishnamurthy S, Hampsey M, &, Shuman S, (2005) Different strategies for carboxyl-terminal domain (CTD) recognition by serine 5-specific CTD phosphatases. J Biol Chem 280, 37681-37688.
    • (2005) J Biol Chem , vol.280 , pp. 37681-37688
    • Hausmann, S.1    Koiwa, H.2    Krishnamurthy, S.3    Hampsey, M.4    Shuman, S.5
  • 31
    • 12844250536 scopus 로고    scopus 로고
    • Small CTD phosphatases function in silencing neuronal gene expression
    • Yeo M, Lee SK, Lee B, Ruiz EC, Pfaff SL, &, Gill GN, (2005) Small CTD phosphatases function in silencing neuronal gene expression. Science 307, 596-600.
    • (2005) Science , vol.307 , pp. 596-600
    • Yeo, M.1    Lee, S.K.2    Lee, B.3    Ruiz, E.C.4    Pfaff, S.L.5    Gill, G.N.6
  • 32
    • 34147157651 scopus 로고    scopus 로고
    • The microRNA miR-124 antagonizes the anti-neural REST/SCP1 pathway during embryonic CNS development
    • Visvanathan J, Lee S, Lee B, Lee JW, &, Lee SK, (2007) The microRNA miR-124 antagonizes the anti-neural REST/SCP1 pathway during embryonic CNS development. Genes Dev 21, 744-749.
    • (2007) Genes Dev , vol.21 , pp. 744-749
    • Visvanathan, J.1    Lee, S.2    Lee, B.3    Lee, J.W.4    Lee, S.K.5
  • 33
    • 84872601985 scopus 로고    scopus 로고
    • Direct conversion of fibroblasts to neurons by reprogramming PTB-regulated microRNA circuits
    • Xue Y, Ouyang K, Huang J, Zhou Y, Ouyang H, Li H, Wang G, Wu Q, Wei C, Bi Y, et al,. (2013) Direct conversion of fibroblasts to neurons by reprogramming PTB-regulated microRNA circuits. Cell 152, 82-96.
    • (2013) Cell , vol.152 , pp. 82-96
    • Xue, Y.1    Ouyang, K.2    Huang, J.3    Zhou, Y.4    Ouyang, H.5    Li, H.6    Wang, G.7    Wu, Q.8    Wei, C.9    Bi, Y.10
  • 34
    • 0035893314 scopus 로고    scopus 로고
    • Opposing effects of Ctk1 kinase and Fcp1 phosphatase at ser 2 of the RNA polymerase II C-terminal domain
    • Cho EJ, Kobor MS, Kim M, Greenblatt J, &, Buratowski S, (2001) Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain. Genes Dev 15, 3319-3329.
    • (2001) Genes Dev , vol.15 , pp. 3319-3329
    • Cho, E.J.1    Kobor, M.S.2    Kim, M.3    Greenblatt, J.4    Buratowski, S.5
  • 35
    • 0037077302 scopus 로고    scopus 로고
    • Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5
    • Hausmann S, &, Shuman S, (2002) Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5. J Biol Chem 277, 21213-21220.
    • (2002) J Biol Chem , vol.277 , pp. 21213-21220
    • Hausmann, S.1    Shuman, S.2
  • 36
    • 0038168110 scopus 로고    scopus 로고
    • A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5
    • Yeo M, Lin PS, Dahmus ME, &, Gill GN, (2003) A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J Biol Chem 278, 26078-26085.
    • (2003) J Biol Chem , vol.278 , pp. 26078-26085
    • Yeo, M.1    Lin, P.S.2    Dahmus, M.E.3    Gill, G.N.4
  • 37
    • 55949110622 scopus 로고    scopus 로고
    • The structure of Fcp1, an essential RNA polymerase II CTD phosphatase
    • Ghosh A, Shuman S, &, Lima CD, (2008) The structure of Fcp1, an essential RNA polymerase II CTD phosphatase. Mol Cell 32, 478-490.
    • (2008) Mol Cell , vol.32 , pp. 478-490
    • Ghosh, A.1    Shuman, S.2    Lima, C.D.3
  • 39
    • 79952172160 scopus 로고    scopus 로고
    • Bio-molecular architects: A scaffold provided by the C-terminal domain of eukaryotic RNA polymerase II
    • doi: 10.3402/nano.v1i0.5502.
    • Zhang M, Gill GN, &, Zhang Y, (2010) Bio-molecular architects: a scaffold provided by the C-terminal domain of eukaryotic RNA polymerase II. Nano Rev 1, doi: 10.3402/nano.v1i0.5502.
    • (2010) Nano Rev , vol.1
    • Zhang, M.1    Gill, G.N.2    Zhang, Y.3
  • 40
    • 79957519203 scopus 로고    scopus 로고
    • Selective inactivation of a human neuronal silencing phosphatase by a small molecule inhibitor
    • Zhang M, Cho EJ, Burstein G, Siegel D, &, Zhang Y, (2011) Selective inactivation of a human neuronal silencing phosphatase by a small molecule inhibitor. ACS Chem Biol 6, 511-519.
    • (2011) ACS Chem Biol , vol.6 , pp. 511-519
    • Zhang, M.1    Cho, E.J.2    Burstein, G.3    Siegel, D.4    Zhang, Y.5
  • 41
    • 33845970267 scopus 로고    scopus 로고
    • Dephosphorylation of the linker regions of Smad1 and Smad2/3 by small C-terminal domain phosphatases has distinct outcomes for bone morphogenetic protein and transforming growth factor-beta pathways
    • Sapkota G, Knockaert M, Alarcon C, Montalvo E, Brivanlou AH, &, Massague J, (2006) Dephosphorylation of the linker regions of Smad1 and Smad2/3 by small C-terminal domain phosphatases has distinct outcomes for bone morphogenetic protein and transforming growth factor-beta pathways. J Biol Chem 281, 40412-40419.
    • (2006) J Biol Chem , vol.281 , pp. 40412-40419
    • Sapkota, G.1    Knockaert, M.2    Alarcon, C.3    Montalvo, E.4    Brivanlou, A.H.5    Massague, J.6
  • 43
    • 4344560876 scopus 로고    scopus 로고
    • The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair
    • Lu X, Bocangel D, Nannenga B, Yamaguchi H, Appella E, &, Donehower LA, (2004) The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair. Mol Cell 15, 621-634.
    • (2004) Mol Cell , vol.15 , pp. 621-634
    • Lu, X.1    Bocangel, D.2    Nannenga, B.3    Yamaguchi, H.4    Appella, E.5    Donehower, L.A.6
  • 47
    • 84856741945 scopus 로고    scopus 로고
    • Pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP): A new player in cell signaling
    • Warfel NA, &, Newton AC, (2012) Pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP): a new player in cell signaling. J Biol Chem 287, 3610-3616.
    • (2012) J Biol Chem , vol.287 , pp. 3610-3616
    • Warfel, N.A.1    Newton, A.C.2
  • 48
    • 43049128122 scopus 로고    scopus 로고
    • The type 2C phosphatase Wip1: An oncogenic regulator of tumor suppressor and DNA damage response pathways
    • Lu X, Nguyen TA, Moon SH, Darlington Y, Sommer M, &, Donehower LA, (2008) The type 2C phosphatase Wip1: an oncogenic regulator of tumor suppressor and DNA damage response pathways. Cancer Metastasis Rev 27, 123-135.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 123-135
    • Lu, X.1    Nguyen, T.A.2    Moon, S.H.3    Darlington, Y.4    Sommer, M.5    Donehower, L.A.6
  • 54
    • 75949097839 scopus 로고    scopus 로고
    • WIP1 phosphatase at the crossroads of cancer and aging
    • Le Guezennec X, &, Bulavin DV, (2010) WIP1 phosphatase at the crossroads of cancer and aging. Trends Biochem Sci 35, 109-114.
    • (2010) Trends Biochem Sci , vol.35 , pp. 109-114
    • Le Guezennec, X.1    Bulavin, D.V.2
  • 55
    • 1842483852 scopus 로고    scopus 로고
    • Inactivation of the Wip1 phosphatase inhibits mammary tumorigenesis through p38 MAPK-mediated activation of the p16(Ink4a)-p19(Arf) pathway
    • Bulavin DV, Phillips C, Nannenga B, Timofeev O, Donehower LA, Anderson CW, Appella E, &, Fornace AJ Jr, (2004) Inactivation of the Wip1 phosphatase inhibits mammary tumorigenesis through p38 MAPK-mediated activation of the p16(Ink4a)-p19(Arf) pathway. Nat Genet 36, 343-350.
    • (2004) Nat Genet , vol.36 , pp. 343-350
    • Bulavin, D.V.1    Phillips, C.2    Nannenga, B.3    Timofeev, O.4    Donehower, L.A.5    Anderson, C.W.6    Appella, E.7    Fornace, Jr.A.J.8
  • 56
    • 35148893194 scopus 로고    scopus 로고
    • The Wip1 phosphatase acts as a gatekeeper in the p53-Mdm2 autoregulatory loop
    • Lu X, Ma O, Nguyen TA, Jones SN, Oren M, &, Donehower LA, (2007) The Wip1 phosphatase acts as a gatekeeper in the p53-Mdm2 autoregulatory loop. Cancer Cell 12, 342-354.
    • (2007) Cancer Cell , vol.12 , pp. 342-354
    • Lu, X.1    Ma, O.2    Nguyen, T.A.3    Jones, S.N.4    Oren, M.5    Donehower, L.A.6
  • 57
    • 0034383398 scopus 로고    scopus 로고
    • P53-inducible wip1 phosphatase mediates a negative feedback regulation of p38 MAPK-p53 signaling in response to UV radiation
    • Takekawa M, Adachi M, Nakahata A, Nakayama I, Itoh F, Tsukuda H, Taya Y, &, Imai K, (2000) p53-inducible wip1 phosphatase mediates a negative feedback regulation of p38 MAPK-p53 signaling in response to UV radiation. EMBO J 19, 6517-6526.
    • (2000) EMBO J , vol.19 , pp. 6517-6526
    • Takekawa, M.1    Adachi, M.2    Nakahata, A.3    Nakayama, I.4    Itoh, F.5    Tsukuda, H.6    Taya, Y.7    Imai, K.8
  • 58
    • 21344451886 scopus 로고    scopus 로고
    • The benzo[c]phenanthridine alkaloid, sanguinarine, is a selective, cell-active inhibitor of mitogen-activated protein kinase phosphatase-1
    • Vogt A, Tamewitz A, Skoko J, Sikorski RP, Giuliano KA, &, Lazo JS, (2005) The benzo[c]phenanthridine alkaloid, sanguinarine, is a selective, cell-active inhibitor of mitogen-activated protein kinase phosphatase-1. J Biol Chem 280, 19078-19086.
    • (2005) J Biol Chem , vol.280 , pp. 19078-19086
    • Vogt, A.1    Tamewitz, A.2    Skoko, J.3    Sikorski, R.P.4    Giuliano, K.A.5    Lazo, J.S.6
  • 60
    • 84872825786 scopus 로고    scopus 로고
    • Suppression of survival signalling pathways by the phosphatase PHLPP
    • O'Neill AK, Niederst MJ, &, Newton AC, (2013) Suppression of survival signalling pathways by the phosphatase PHLPP. FEBS J 280, 572-583.
    • (2013) FEBS J , vol.280 , pp. 572-583
    • O'Neill, A.K.1    Niederst, M.J.2    Newton, A.C.3
  • 61
    • 77957930200 scopus 로고    scopus 로고
    • Discovery of small molecule inhibitors of the PH domain leucine-rich repeat protein phosphatase (PHLPP) by chemical and virtual screening
    • Sierecki E, Sinko W, McCammon JA, &, Newton AC, (2010) Discovery of small molecule inhibitors of the PH domain leucine-rich repeat protein phosphatase (PHLPP) by chemical and virtual screening. J Med Chem 53, 6899-6911.
    • (2010) J Med Chem , vol.53 , pp. 6899-6911
    • Sierecki, E.1    Sinko, W.2    McCammon, J.A.3    Newton, A.C.4
  • 62
    • 77950159448 scopus 로고    scopus 로고
    • Sanguinarine as a potent and specific inhibitor of protein phosphatase 2C in vitro and induces apoptosis via phosphorylation of p38 in HL60 cells
    • Aburai N, Yoshida M, Ohnishi M, &, Kimura K, (2010) Sanguinarine as a potent and specific inhibitor of protein phosphatase 2C in vitro and induces apoptosis via phosphorylation of p38 in HL60 cells. Biosci Biotechnol Biochem 74, 548-552.
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 548-552
    • Aburai, N.1    Yoshida, M.2    Ohnishi, M.3    Kimura, K.4
  • 63
    • 0042231985 scopus 로고    scopus 로고
    • A comparison of phosphonothioic acids with phosphonic acids as phosphatase inhibitors
    • Swierczek K, Pandey AS, Peters JW, &, Hengge AC, (2003) A comparison of phosphonothioic acids with phosphonic acids as phosphatase inhibitors. J Med Chem 46, 3703-3708.
    • (2003) J Med Chem , vol.46 , pp. 3703-3708
    • Swierczek, K.1    Pandey, A.S.2    Peters, J.W.3    Hengge, A.C.4
  • 64
    • 74549175937 scopus 로고    scopus 로고
    • The cross-sectional and longitudinal association of the BODE index with quality of life in patients with chronic obstructive pulmonary disease
    • Lin YX, Xu WN, Liang LR, Pang BS, Nie XH, Zhang J, Wang H, Liu YX, Wang DQ, Xu ZY, et al,. (2009) The cross-sectional and longitudinal association of the BODE index with quality of life in patients with chronic obstructive pulmonary disease. Chin Med J (Engl) 122, 2939-2944.
    • (2009) Chin Med J (Engl) , vol.122 , pp. 2939-2944
    • Lin, Y.X.1    Xu, W.N.2    Liang, L.R.3    Pang, B.S.4    Nie, X.H.5    Zhang, J.6    Wang, H.7    Liu, Y.X.8    Wang, D.Q.9    Xu, Z.Y.10
  • 65
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg J, Huang HB, Kwon YG, Greengard P, Nairn AC, &, Kuriyan J, (1995) Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 66
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff MP, Cohen PT, Reinemer P, &, Barford D, (1995) Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol 254, 942-959.
    • (1995) J Mol Biol , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.2    Reinemer, P.3    Barford, D.4
  • 68
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • Bialojan C, &, Takai A, (1988) Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics. Biochem J 256, 283-290.
    • (1988) Biochem J , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 69
    • 0025333146 scopus 로고
    • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants
    • MacKintosh C, Beattie KA, Klumpp S, Cohen P, &, Codd GA, (1990) Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Lett 264, 187-192.
    • (1990) FEBS Lett , vol.264 , pp. 187-192
    • Mackintosh, C.1    Beattie, K.A.2    Klumpp, S.3    Cohen, P.4    Codd, G.A.5
  • 71
    • 34447275978 scopus 로고    scopus 로고
    • Small-molecule inhibitors of ser/thr protein phosphatases: Specificity, use and common forms of abuse
    • Swingle M, Ni L, &, Honkanen RE, (2007) Small-molecule inhibitors of ser/thr protein phosphatases: specificity, use and common forms of abuse. Methods Mol Biol 365, 23-38.
    • (2007) Methods Mol Biol , vol.365 , pp. 23-38
    • Swingle, M.1    Ni, L.2    Honkanen, R.E.3
  • 74
    • 0030065764 scopus 로고    scopus 로고
    • Tyrosine-272 is involved in the inhibition of protein phosphatase-1 by multiple toxins
    • Zhang L, Zhang Z, Long F, &, Lee EY, (1996) Tyrosine-272 is involved in the inhibition of protein phosphatase-1 by multiple toxins. Biochemistry 35, 1606-1611.
    • (1996) Biochemistry , vol.35 , pp. 1606-1611
    • Zhang, L.1    Zhang, Z.2    Long, F.3    Lee, E.Y.4
  • 78
    • 0030344872 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the interaction of motuporin and microcystins with type-1 and type-2A protein phosphatases
    • Craig M, Luu HA, McCready TL, Williams D, Andersen RJ, &, Holmes CF, (1996) Molecular mechanisms underlying the interaction of motuporin and microcystins with type-1 and type-2A protein phosphatases. Biochem Cell Biol 74, 569-578.
    • (1996) Biochem Cell Biol , vol.74 , pp. 569-578
    • Craig, M.1    Luu, H.A.2    McCready, T.L.3    Williams, D.4    Andersen, R.J.5    Holmes, C.F.6
  • 79
    • 0029088182 scopus 로고
    • The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1
    • MacKintosh RW, Dalby KN, Campbell DG, Cohen PT, Cohen P, &, MacKintosh C, (1995) The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1. FEBS Lett 371, 236-240.
    • (1995) FEBS Lett , vol.371 , pp. 236-240
    • Mackintosh, R.W.1    Dalby, K.N.2    Campbell, D.G.3    Cohen, P.T.4    Cohen, P.5    Mackintosh, C.6
  • 80
    • 0027761070 scopus 로고
    • Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1
    • Zhang Z, Zhao S, Deans-Zirattu S, Bai G, &, Lee EY, (1993) Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1. Mol Cell Biochem 127-128, 113-119.
    • (1993) Mol Cell Biochem , vol.127-128 , pp. 113-119
    • Zhang, Z.1    Zhao, S.2    Deans-Zirattu, S.3    Bai, G.4    Lee, E.Y.5
  • 81
    • 0036111253 scopus 로고    scopus 로고
    • Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1
    • Kita A, Matsunaga S, Takai A, Kataiwa H, Wakimoto T, Fusetani N, Isobe M, &, Miki K, (2002) Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1. Structure 10, 715-724.
    • (2002) Structure , vol.10 , pp. 715-724
    • Kita, A.1    Matsunaga, S.2    Takai, A.3    Kataiwa, H.4    Wakimoto, T.5    Fusetani, N.6    Isobe, M.7    Miki, K.8
  • 82
    • 30344447686 scopus 로고    scopus 로고
    • Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: Elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins
    • Maynes JT, Luu HA, Cherney MM, Andersen RJ, Williams D, Holmes CF, &, James MN, (2006) Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins. J Mol Biol 356, 111-120.
    • (2006) J Mol Biol , vol.356 , pp. 111-120
    • Maynes, J.T.1    Luu, H.A.2    Cherney, M.M.3    Andersen, R.J.4    Williams, D.5    Holmes, C.F.6    James, M.N.7
  • 83
    • 57749209868 scopus 로고    scopus 로고
    • Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: A novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
    • Kelker MS, Page R, &, Peti W, (2009) Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors. J Mol Biol 385, 11-21.
    • (2009) J Mol Biol , vol.385 , pp. 11-21
    • Kelker, M.S.1    Page, R.2    Peti, W.3
  • 85
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells JA, &, McClendon CL, (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 87
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 - Targeted in many directions
    • Cohen PT, (2002) Protein phosphatase 1-targeted in many directions. J Cell Sci 115, 241-256.
    • (2002) J Cell Sci , vol.115 , pp. 241-256
    • Cohen, P.T.1
  • 88
    • 84872773091 scopus 로고    scopus 로고
    • Structural basis for protein phosphatase 1 regulation and specificity
    • Peti W, Nairn AC, &, Page R, (2013) Structural basis for protein phosphatase 1 regulation and specificity. FEBS J 280, 596-611.
    • (2013) FEBS J , vol.280 , pp. 596-611
    • Peti, W.1    Nairn, A.C.2    Page, R.3
  • 89
    • 84872786662 scopus 로고    scopus 로고
    • PP1 and PP2A phosphatases - Cooperating partners in modulating retinoblastoma protein activation
    • Kolupaeva V, &, Janssens V, (2013) PP1 and PP2A phosphatases-cooperating partners in modulating retinoblastoma protein activation. FEBS J 280, 627-643.
    • (2013) FEBS J , vol.280 , pp. 627-643
    • Kolupaeva, V.1    Janssens, V.2
  • 90
    • 77955279255 scopus 로고    scopus 로고
    • The extended PP1 toolkit: Designed to create specificity
    • Bollen M, Peti W, Ragusa MJ, &, Beullens M, (2010) The extended PP1 toolkit: designed to create specificity. Trends Biochem Sci 35, 450-458.
    • (2010) Trends Biochem Sci , vol.35 , pp. 450-458
    • Bollen, M.1    Peti, W.2    Ragusa, M.J.3    Beullens, M.4
  • 91
    • 84866679293 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 1 by intrinsically disordered proteins
    • Choy MS, Page R, &, Peti W, (2012) Regulation of protein phosphatase 1 by intrinsically disordered proteins. Biochem Soc Trans 40, 969-974.
    • (2012) Biochem Soc Trans , vol.40 , pp. 969-974
    • Choy, M.S.1    Page, R.2    Peti, W.3
  • 92
    • 3042547846 scopus 로고    scopus 로고
    • Structural basis of protein phosphatase 1 regulation
    • Terrak M, Kerff F, Langsetmo K, Tao T, &, Dominguez R, (2004) Structural basis of protein phosphatase 1 regulation. Nature 429, 780-784.
    • (2004) Nature , vol.429 , pp. 780-784
    • Terrak, M.1    Kerff, F.2    Langsetmo, K.3    Tao, T.4    Dominguez, R.5
  • 94
    • 77950519767 scopus 로고    scopus 로고
    • Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
    • Ragusa MJ, Dancheck B, Critton DA, Nairn AC, Page R, &, Peti W, (2010) Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nat Struct Mol Biol 17, 459-464.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 459-464
    • Ragusa, M.J.1    Dancheck, B.2    Critton, D.A.3    Nairn, A.C.4    Page, R.5    Peti, W.6
  • 96
    • 79951659237 scopus 로고    scopus 로고
    • Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex
    • Dancheck B, Ragusa MJ, Allaire M, Nairn AC, Page R, &, Peti W, (2011) Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex. Biochemistry 50, 1238-1246.
    • (2011) Biochemistry , vol.50 , pp. 1238-1246
    • Dancheck, B.1    Ragusa, M.J.2    Allaire, M.3    Nairn, A.C.4    Page, R.5    Peti, W.6
  • 98
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff MP, Johnson DF, Moorhead G, Cohen PT, Cohen P, &, Barford D, (1997) Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J 16, 1876-1887.
    • (1997) EMBO J , vol.16 , pp. 1876-1887
    • Egloff, M.P.1    Johnson, D.F.2    Moorhead, G.3    Cohen, P.T.4    Cohen, P.5    Barford, D.6
  • 99
    • 39149114105 scopus 로고    scopus 로고
    • Activation of protein phosphatase 1 by a small molecule designed to bind to the enzyme's regulatory site
    • Tappan E, &, Chamberlin AR, (2008) Activation of protein phosphatase 1 by a small molecule designed to bind to the enzyme's regulatory site. Chem Biol 15, 167-174.
    • (2008) Chem Biol , vol.15 , pp. 167-174
    • Tappan, E.1    Chamberlin, A.R.2
  • 102
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler P, Harding HP, Ron D, &, Bertolotti A, (2011) Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 332, 91-94.
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 103
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V, &, Goris J, (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353, 417-439.
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 104
    • 84857133852 scopus 로고    scopus 로고
    • The role and therapeutic potential of Ser/Thr phosphatase PP2A in apoptotic signalling networks in human cancer cells
    • Janssens V, &, Rebollo A, (2012) The role and therapeutic potential of Ser/Thr phosphatase PP2A in apoptotic signalling networks in human cancer cells. Curr Mol Med 12, 268-287.
    • (2012) Curr Mol Med , vol.12 , pp. 268-287
    • Janssens, V.1    Rebollo, A.2
  • 105
    • 78650407231 scopus 로고    scopus 로고
    • Identification of PP2A complexes and pathways involved in cell transformation
    • Sablina AA, Hector M, Colpaert N, &, Hahn WC, (2010) Identification of PP2A complexes and pathways involved in cell transformation. Cancer Res 70, 10474-10484.
    • (2010) Cancer Res , vol.70 , pp. 10474-10484
    • Sablina, A.A.1    Hector, M.2    Colpaert, N.3    Hahn, W.C.4
  • 108
    • 0035804217 scopus 로고    scopus 로고
    • Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the A alpha subunit gene
    • Ruediger R, Pham HT, &, Walter G, (2001) Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the A alpha subunit gene. Oncogene 20, 10-15.
    • (2001) Oncogene , vol.20 , pp. 10-15
    • Ruediger, R.1    Pham, H.T.2    Walter, G.3
  • 109
    • 79957910918 scopus 로고    scopus 로고
    • Targeting SET/I(2)PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy
    • Switzer CH, Cheng RY, Vitek TM, Christensen DJ, Wink DA, &, Vitek MP, (2011) Targeting SET/I(2)PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy. Oncogene 30, 2504-2513.
    • (2011) Oncogene , vol.30 , pp. 2504-2513
    • Switzer, C.H.1    Cheng, R.Y.2    Vitek, T.M.3    Christensen, D.J.4    Wink, D.A.5    Vitek, M.P.6
  • 110
    • 0026693436 scopus 로고
    • Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3′ half to different genes: Characterization of the set gene
    • von Lindern M, van Baal S, Wiegant J, Raap A, Hagemeijer A, &, Grosveld G, (1992) Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3′ half to different genes: characterization of the set gene. Mol Cell Biol 12, 3346-3355.
    • (1992) Mol Cell Biol , vol.12 , pp. 3346-3355
    • Von Lindern, M.1    Van Baal, S.2    Wiegant, J.3    Raap, A.4    Hagemeijer, A.5    Grosveld, G.6
  • 111
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li M, Makkinje A, &, Damuni Z, (1996) The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J Biol Chem 271, 11059-11062.
    • (1996) J Biol Chem , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 113
  • 115
    • 78650366525 scopus 로고    scopus 로고
    • Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis
    • Mochida S, Maslen SL, Skehel M, &, Hunt T, (2010) Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis. Science 330, 1670-1673.
    • (2010) Science , vol.330 , pp. 1670-1673
    • Mochida, S.1    Maslen, S.L.2    Skehel, M.3    Hunt, T.4
  • 117
    • 0030720062 scopus 로고    scopus 로고
    • Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A
    • Walsh AH, Cheng A, &, Honkanen RE, (1997) Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. FEBS Lett 416, 230-234.
    • (1997) FEBS Lett , vol.416 , pp. 230-234
    • Walsh, A.H.1    Cheng, A.2    Honkanen, R.E.3
  • 119
    • 20444424775 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase inhibitors with anti-tumor activity
    • Honkanen RE, (2005) Serine/threonine protein phosphatase inhibitors with anti-tumor activity. Handbk Exp Pharm 167, 295-317.
    • (2005) Handbk Exp Pharm , vol.167 , pp. 295-317
    • Honkanen, R.E.1
  • 123
    • 1642559254 scopus 로고    scopus 로고
    • Microcystin-LR and okadaic acid-induced cellular effects: A dualistic response
    • Gehringer MM, (2004) Microcystin-LR and okadaic acid-induced cellular effects: a dualistic response. FEBS Lett 557, 1-8.
    • (2004) FEBS Lett , vol.557 , pp. 1-8
    • Gehringer, M.M.1
  • 124
    • 0035072467 scopus 로고    scopus 로고
    • Preliminary evidence for in vivo tumour initiation by oral administration of extracts of the blue-green alga Cylindrospermopsis raciborskii containing the toxin cylindrospermopsin
    • Falconer IR, &, Humpage AR, (2001) Preliminary evidence for in vivo tumour initiation by oral administration of extracts of the blue-green alga Cylindrospermopsis raciborskii containing the toxin cylindrospermopsin. Environ Toxicol 16, 192-195.
    • (2001) Environ Toxicol , vol.16 , pp. 192-195
    • Falconer, I.R.1    Humpage, A.R.2
  • 125
    • 0027499590 scopus 로고
    • Hyperphosphorylation of cytokeratins by okadaic acid class tumor promoters in primary human keratinocytes
    • Yatsunami J, Komori A, Ohta T, Suganuma M, Yuspa SH, &, Fujiki H, (1993) Hyperphosphorylation of cytokeratins by okadaic acid class tumor promoters in primary human keratinocytes. Cancer Res 53, 992-996.
    • (1993) Cancer Res , vol.53 , pp. 992-996
    • Yatsunami, J.1    Komori, A.2    Ohta, T.3    Suganuma, M.4    Yuspa, S.H.5    Fujiki, H.6
  • 126
    • 0035178875 scopus 로고    scopus 로고
    • The toxic responses induced by okadaic acid involve processing of multiple caspase isoforms
    • Rossini GP, Sgarbi N, &, Malaguti C, (2001) The toxic responses induced by okadaic acid involve processing of multiple caspase isoforms. Toxicon 39, 763-770.
    • (2001) Toxicon , vol.39 , pp. 763-770
    • Rossini, G.P.1    Sgarbi, N.2    Malaguti, C.3
  • 127
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak F, &, Mertz P, (2000) Calcineurin: form and function. Physiol Rev 80, 1483-1521.
    • (2000) Physiol Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 128
    • 0017157814 scopus 로고
    • Biological effects of cyclosporin A: A new antilymphocytic agent
    • Borel JF, Feurer C, Gubler HU, &, Stahelin H, (1976) Biological effects of cyclosporin A: a new antilymphocytic agent. Agents Actions 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
  • 129
    • 0023245677 scopus 로고
    • FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics
    • Kino T, Hatanaka H, Hashimoto M, Nishiyama M, Goto T, Okuhara M, Kohsaka M, Aoki H, &, Imanaka H, (1987) FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics. J Antibiot (Tokyo) 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
  • 132
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, &, Ke H, (2002) Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci U S A 99, 12037-12042.
    • (2002) Proc Natl Acad Sci U S A , 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
  • 133
    • 0037108767 scopus 로고    scopus 로고
    • Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin
    • Jin L, &, Harrison SC, (2002) Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci U S A 99, 13522-13526.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13522-13526
    • Jin, L.1    Harrison, S.C.2
  • 135
    • 0028245317 scopus 로고
    • NF-AT-AP-1 and Rel-bZIP: Hybrid vigor and binding under the influence
    • Nolan GP, (1994) NF-AT-AP-1 and Rel-bZIP: hybrid vigor and binding under the influence. Cell 77, 795-798.
    • (1994) Cell , vol.77 , pp. 795-798
    • Nolan, G.P.1
  • 137
    • 0142197612 scopus 로고    scopus 로고
    • Regulation of IL4 gene expression by T cells and therapeutic perspectives
    • Li-Weber M, &, Krammer PH, (2003) Regulation of IL4 gene expression by T cells and therapeutic perspectives. Nat Rev Immunol 3, 534-543.
    • (2003) Nat Rev Immunol , vol.3 , pp. 534-543
    • Li-Weber, M.1    Krammer, P.H.2
  • 138
    • 0029886850 scopus 로고    scopus 로고
    • Cyclosporine and tacrolimus in clinical transplant: A comparative review
    • Jain AB, &, Fung JJ, (1996) Cyclosporine and tacrolimus in clinical transplant: a comparative review. Clin Immunother 5, 351-373.
    • (1996) Clin Immunother , vol.5 , pp. 351-373
    • Jain, A.B.1    Fung, J.J.2
  • 139
    • 0034078320 scopus 로고    scopus 로고
    • FK506, an immunosuppressant targeting calcineurin function
    • Dumont FJ, (2000) FK506, an immunosuppressant targeting calcineurin function. Curr Med Chem 7, 731-748.
    • (2000) Curr Med Chem , vol.7 , pp. 731-748
    • Dumont, F.J.1
  • 140
    • 2442714017 scopus 로고    scopus 로고
    • Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules
    • Roehrl MH, Kang S, Aramburu J, Wagner G, Rao A, &, Hogan PG, (2004) Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules. Proc Natl Acad Sci U S A 101, 7554-7559.
    • (2004) Proc Natl Acad Sci U S A , 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
  • 141
    • 66849115406 scopus 로고    scopus 로고
    • Targeting protein serine/threonine phosphatases for drug development
    • McConnell JL, &, Wadzinski BE, (2009) Targeting protein serine/threonine phosphatases for drug development. Mol Pharmacol 75, 1249-1261.
    • (2009) Mol Pharmacol , vol.75 , pp. 1249-1261
    • McConnell, J.L.1    Wadzinski, B.E.2
  • 142
    • 43049097815 scopus 로고    scopus 로고
    • The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer
    • Golden T, Swingle M, &, Honkanen RE, (2008) The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer. Cancer Metastasis Rev 27, 169-178.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 169-178
    • Golden, T.1    Swingle, M.2    Honkanen, R.E.3
  • 144
    • 65649140083 scopus 로고    scopus 로고
    • Protein phosphatase 5 regulates the function of 53BP1 after neocarzinostatin-induced DNA damage
    • Kang Y, Lee JH, Hoan NN, Sohn HM, Chang IY, &, You HJ, (2009) Protein phosphatase 5 regulates the function of 53BP1 after neocarzinostatin-induced DNA damage. J Biol Chem 284, 9845-9853.
    • (2009) J Biol Chem , vol.284 , pp. 9845-9853
    • Kang, Y.1    Lee, J.H.2    Hoan, N.N.3    Sohn, H.M.4    Chang, I.Y.5    You, H.J.6
  • 145
    • 0029751136 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant
    • Chen MS, Silverstein AM, Pratt WB, &, Chinkers M, (1996) The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant. J Biol Chem 271, 32315-32320.
    • (1996) J Biol Chem , vol.271 , pp. 32315-32320
    • Chen, M.S.1    Silverstein, A.M.2    Pratt, W.B.3    Chinkers, M.4
  • 146
    • 70350093431 scopus 로고    scopus 로고
    • C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins
    • Ramsey AJ, Russell LC, &, Chinkers M, (2009) C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins. Biochem J 423, 411-419.
    • (2009) Biochem J , vol.423 , pp. 411-419
    • Ramsey, A.J.1    Russell, L.C.2    Chinkers, M.3
  • 147
    • 33750076984 scopus 로고    scopus 로고
    • The alpha4 regulatory subunit exerts opposing allosteric effects on protein phosphatases PP6 and PP2A
    • Prickett TD, &, Brautigan DL, (2006) The alpha4 regulatory subunit exerts opposing allosteric effects on protein phosphatases PP6 and PP2A. J Biol Chem 281, 30503-30511.
    • (2006) J Biol Chem , vol.281 , pp. 30503-30511
    • Prickett, T.D.1    Brautigan, D.L.2
  • 148
    • 0031915128 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)
    • Huang X, &, Honkanen RE, (1998) Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC). J Biol Chem 273, 1462-1468.
    • (1998) J Biol Chem , vol.273 , pp. 1462-1468
    • Huang, X.1    Honkanen, R.E.2
  • 150
    • 0025732992 scopus 로고
    • A novel protein phosphatase inhibitor, tautomycin. Effect on smooth muscle
    • Hori M, Magae J, Han YG, Hartshorne DJ, &, Karaki H, (1991) A novel protein phosphatase inhibitor, tautomycin. Effect on smooth muscle. FEBS Lett 285, 145-148.
    • (1991) FEBS Lett , vol.285 , pp. 145-148
    • Hori, M.1    Magae, J.2    Han, Y.G.3    Hartshorne, D.J.4    Karaki, H.5
  • 151
    • 0028813436 scopus 로고
    • The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells
    • Fruman DA, Bierer BE, Benes JE, Burakoff SJ, Austen KF, &, Katz HR, (1995) The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells. J Immunol 154, 1846-1851.
    • (1995) J Immunol , vol.154 , pp. 1846-1851
    • Fruman, D.A.1    Bierer, B.E.2    Benes, J.E.3    Burakoff, S.J.4    Austen, K.F.5    Katz, H.R.6
  • 152
    • 0028175820 scopus 로고
    • 2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells
    • 2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells. J Biol Chem 269, 15111-15117.
    • (1994) J Biol Chem , vol.269 , pp. 15111-15117
    • Groblewski, G.E.1    Wagner, A.C.2    Williams, J.A.3
  • 155
    • 68549115381 scopus 로고    scopus 로고
    • Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin
    • Bertini I, Calderone V, Fragai M, Luchinat C, &, Talluri E, (2009) Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin. J Med Chem 52, 4838-4843.
    • (2009) J Med Chem , vol.52 , pp. 4838-4843
    • Bertini, I.1    Calderone, V.2    Fragai, M.3    Luchinat, C.4    Talluri, E.5


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