메뉴 건너뛰기




Volumn 96, Issue 3, 2012, Pages 296-304

Protein kinase inhibitors that inhibit induction of lytic program and replication of Epstein-Barr virus

Author keywords

EBV BGLF4 protein kinase; Epstein Barr virus (EBV); Protein kinase inhibitors (PKI); Signal transduction; Viral reactivation

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 [1 (3 AMIDINOTHIOPROPYL) 1H INDOL 3 YL] 3 (1 METHYL 1H INDOL 3 YL)MALEIMIDE; 2 MORPHOLINO 8 PHENYLCHROMONE; 3 (4 METHYLPHENYLSULFONYL) 2 PROPENENITRILE; 5 IODOTUBERCIDIN; ACICLOVIR; ENZYME INHIBITOR; EPIDERMAL GROWTH FACTOR RECEPTOR ASSOCIATED TYROSINE KINASE INHIBITOR; ERBSTATIN; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; GLYCOGEN SYNTHASE KINASE 3BETA; I KAPPA B; K 252A; KENPAULLONE; MIDOSTAURIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR ASSOCIATED TYROSINE KINASE INHIBITOR; PROTEIN KINASE C INHIBITOR; PROTEIN KINASE INHIBITOR; ROTTLERIN; STAUROSPORINE; UNCLASSIFIED DRUG; VIRUS PROTEIN; WORTMANNIN;

EID: 84869102865     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2012.09.021     Document Type: Article
Times cited : (33)

References (66)
  • 1
    • 0032506210 scopus 로고    scopus 로고
    • Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product
    • Adamson A.L., Kenney S.C. Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product. Virology 1998, 251:187-197.
    • (1998) Virology , vol.251 , pp. 187-197
    • Adamson, A.L.1    Kenney, S.C.2
  • 2
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro A., Wymann M.P. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem. J. 1993, 296(Pt. 2):297-301.
    • (1993) Biochem. J. , vol.296 , Issue.PART 2 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 3
    • 33646737238 scopus 로고    scopus 로고
    • Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1
    • Asai R., Kato A., Kato K., Kanamori-Koyama M., Sugimoto K., Sairenji T., Nishiyama Y., Kawaguchi Y. Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1. J. Virol. 2006, 80:5125-5134.
    • (2006) J. Virol. , vol.80 , pp. 5125-5134
    • Asai, R.1    Kato, A.2    Kato, K.3    Kanamori-Koyama, M.4    Sugimoto, K.5    Sairenji, T.6    Nishiyama, Y.7    Kawaguchi, Y.8
  • 4
    • 21844455259 scopus 로고    scopus 로고
    • N-Benzoylstaurosporine (PKC412) inhibits Akt kinase inducing apoptosis in multiple myeloma cells
    • Bahlis N.J., Miao Y., Koc O.N., Lee K., Boise L.H., Gerson S.L. N-Benzoylstaurosporine (PKC412) inhibits Akt kinase inducing apoptosis in multiple myeloma cells. Leuk. Lymphoma 2005, 46:899-908.
    • (2005) Leuk. Lymphoma , vol.46 , pp. 899-908
    • Bahlis, N.J.1    Miao, Y.2    Koc, O.N.3    Lee, K.4    Boise, L.H.5    Gerson, S.L.6
  • 9
    • 0034011617 scopus 로고    scopus 로고
    • A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro
    • Chen M.R., Chang S.J., Huang H., Chen J.Y. A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro. J. Virol. 2000, 74:3093-3104.
    • (2000) J. Virol. , vol.74 , pp. 3093-3104
    • Chen, M.R.1    Chang, S.J.2    Huang, H.3    Chen, J.Y.4
  • 10
    • 0032775345 scopus 로고    scopus 로고
    • K252a induces cell cycle arrest and apoptosis by inhibiting Cdc2 and Cdc25c
    • Chin L.S., Murray S.F., Doherty P.F., Singh S.K. K252a induces cell cycle arrest and apoptosis by inhibiting Cdc2 and Cdc25c. Cancer Invest. 1999, 17:391-395.
    • (1999) Cancer Invest. , vol.17 , pp. 391-395
    • Chin, L.S.1    Murray, S.F.2    Doherty, P.F.3    Singh, S.K.4
  • 11
    • 0025341653 scopus 로고
    • Activation of latent EBV via anti-IgG-triggered, second messenger pathways in the Burkitt's lymphoma cell line Akata
    • Daibata M., Humphreys R.E., Takada K., Sairenji T. Activation of latent EBV via anti-IgG-triggered, second messenger pathways in the Burkitt's lymphoma cell line Akata. J. Immunol. 1990, 144:4788-4793.
    • (1990) J. Immunol. , vol.144 , pp. 4788-4793
    • Daibata, M.1    Humphreys, R.E.2    Takada, K.3    Sairenji, T.4
  • 12
    • 0030751035 scopus 로고    scopus 로고
    • Purification and characterization of the protein kinase encoded by the UL13 gene of herpes simplex virus type 2
    • Daikoku T., Shibata S., Goshima F., Oshima S., Tsurumi T., Yamada H., Yamashita Y., Nishiyama Y. Purification and characterization of the protein kinase encoded by the UL13 gene of herpes simplex virus type 2. Virology 1997, 235:82-93.
    • (1997) Virology , vol.235 , pp. 82-93
    • Daikoku, T.1    Shibata, S.2    Goshima, F.3    Oshima, S.4    Tsurumi, T.5    Yamada, H.6    Yamashita, Y.7    Nishiyama, Y.8
  • 14
    • 0034974152 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BRLF1 induces the lytic form of viral replication through a mechanism involving phosphatidylinositol-3 kinase activation
    • Darr C.D., Mauser A., Kenney S. Epstein-Barr virus immediate-early protein BRLF1 induces the lytic form of viral replication through a mechanism involving phosphatidylinositol-3 kinase activation. J. Virol. 2001, 75:6135-6142.
    • (2001) J. Virol. , vol.75 , pp. 6135-6142
    • Darr, C.D.1    Mauser, A.2    Kenney, S.3
  • 15
    • 0025837283 scopus 로고
    • Induction of Epstein-Barr virus lytic cycle by tumor-promoting and non-tumor-promoting phorbol esters requires active protein kinase C
    • Davies A.H., Grand R.J., Evans F.J., Rickinson A.B. Induction of Epstein-Barr virus lytic cycle by tumor-promoting and non-tumor-promoting phorbol esters requires active protein kinase C. J. Virol. 1991, 65:6838-6844.
    • (1991) J. Virol. , vol.65 , pp. 6838-6844
    • Davies, A.H.1    Grand, R.J.2    Evans, F.J.3    Rickinson, A.B.4
  • 16
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 2000, 351:95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 18
    • 0035671576 scopus 로고    scopus 로고
    • Epstein-Barr viral load measurement as a marker of EBV-related disease
    • Fan H., Gulley M.L. Epstein-Barr viral load measurement as a marker of EBV-related disease. Mol. Diagn. 2001, 6:279-289.
    • (2001) Mol. Diagn. , vol.6 , pp. 279-289
    • Fan, H.1    Gulley, M.L.2
  • 20
    • 0034660443 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators
    • Feederle R., Kost M., Baumann M., Janz A., Drouet E., Hammerschmidt W., Delecluse H.J. The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J. 2000, 19:3080-3089.
    • (2000) EMBO J. , vol.19 , pp. 3080-3089
    • Feederle, R.1    Kost, M.2    Baumann, M.3    Janz, A.4    Drouet, E.5    Hammerschmidt, W.6    Delecluse, H.J.7
  • 22
    • 0035919638 scopus 로고    scopus 로고
    • 12-O-tetradecanoylphorbol-13-acetate induces Epstein-Barr virus reactivation via NF-kappaB and AP-1 as regulated by protein kinase C and mitogen-activated protein kinase
    • Gao X., Ikuta K., Tajima M., Sairenji T. 12-O-tetradecanoylphorbol-13-acetate induces Epstein-Barr virus reactivation via NF-kappaB and AP-1 as regulated by protein kinase C and mitogen-activated protein kinase. Virology 2001, 286:91-99.
    • (2001) Virology , vol.286 , pp. 91-99
    • Gao, X.1    Ikuta, K.2    Tajima, M.3    Sairenji, T.4
  • 23
    • 2142639417 scopus 로고    scopus 로고
    • Effects of maribavir and selected indolocarbazoles on Epstein-Barr virus protein kinase BGLF4 and on viral lytic replication
    • Gershburg E., Hong K., Pagano J.S. Effects of maribavir and selected indolocarbazoles on Epstein-Barr virus protein kinase BGLF4 and on viral lytic replication. Antimicrob. Agents Chemother. 2004, 48:1900-1903.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1900-1903
    • Gershburg, E.1    Hong, K.2    Pagano, J.S.3
  • 24
    • 0036143222 scopus 로고    scopus 로고
    • Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the l-riboside benzimidazole 1263W94
    • Gershburg E., Pagano J.S. Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the l-riboside benzimidazole 1263W94. J. Virol. 2002, 76:998-1003.
    • (2002) J. Virol. , vol.76 , pp. 998-1003
    • Gershburg, E.1    Pagano, J.S.2
  • 25
  • 26
    • 34248339596 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus
    • Gershburg E., Raffa S., Torrisi M.R., Pagano J.S. Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J. Virol. 2007, 81:5407-5412.
    • (2007) J. Virol. , vol.81 , pp. 5407-5412
    • Gershburg, E.1    Raffa, S.2    Torrisi, M.R.3    Pagano, J.S.4
  • 27
    • 77957902312 scopus 로고    scopus 로고
    • Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization
    • Gershburg S., Murphy L., Marschall M., Gershburg E. Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization. Biochem. J. 2010, 431:227-235.
    • (2010) Biochem. J. , vol.431 , pp. 227-235
    • Gershburg, S.1    Murphy, L.2    Marschall, M.3    Gershburg, E.4
  • 30
    • 0034070467 scopus 로고    scopus 로고
    • The staurosporine analog, Ro-31-8220, induces apoptosis independently of its ability to inhibit protein kinase C
    • Han Z., Pantazis P., Lange T.S., Wyche J.H., Hendrickson E.A. The staurosporine analog, Ro-31-8220, induces apoptosis independently of its ability to inhibit protein kinase C. Cell Death Differ. 2000, 7:521-530.
    • (2000) Cell Death Differ. , vol.7 , pp. 521-530
    • Han, Z.1    Pantazis, P.2    Lange, T.S.3    Wyche, J.H.4    Hendrickson, E.A.5
  • 31
    • 0031060542 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein is a protein kinase that autophosphorylates on serines and threonines
    • He Z., He Y.S., Kim Y., Chu L., Ohmstede C., Biron K.K., Coen D.M. The human cytomegalovirus UL97 protein is a protein kinase that autophosphorylates on serines and threonines. J. Virol. 1997, 71:405-411.
    • (1997) J. Virol. , vol.71 , pp. 405-411
    • He, Z.1    He, Y.S.2    Kim, Y.3    Chu, L.4    Ohmstede, C.5    Biron, K.K.6    Coen, D.M.7
  • 32
    • 0032705583 scopus 로고    scopus 로고
    • The protein kinase C inhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity
    • Hers I., Tavare J.M., Denton R.M. The protein kinase C inhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity. FEBS Lett. 1999, 460:433-436.
    • (1999) FEBS Lett. , vol.460 , pp. 433-436
    • Hers, I.1    Tavare, J.M.2    Denton, R.M.3
  • 33
    • 1642444166 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is a determinant of responsiveness to B cell antigen receptor-mediated Epstein-Barr virus activation
    • Iwakiri D., Takada K. Phosphatidylinositol 3-kinase is a determinant of responsiveness to B cell antigen receptor-mediated Epstein-Barr virus activation. J. Immunol. 2004, 172:1561-1566.
    • (2004) J. Immunol. , vol.172 , pp. 1561-1566
    • Iwakiri, D.1    Takada, K.2
  • 35
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002, 298:1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 36
    • 0041837470 scopus 로고    scopus 로고
    • Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2
    • Kawaguchi Y., Kato K. Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2. Rev. Med. Virol. 2003, 13:331-340.
    • (2003) Rev. Med. Virol. , vol.13 , pp. 331-340
    • Kawaguchi, Y.1    Kato, K.2
  • 37
    • 34249064632 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • Lippinkott-Williams & Wilkins, Philadelphia, D.M. Knipe, P.M. Howley (Eds.)
    • Kieff E., Rickinson A.B. Epstein-Barr virus and its replication. Fields Virology 2007, 2603-2654. Lippinkott-Williams & Wilkins, Philadelphia. fifth ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2007) Fields Virology , pp. 2603-2654
    • Kieff, E.1    Rickinson, A.B.2
  • 39
    • 0023520881 scopus 로고
    • TPA induction of Epstein-Barr virus early antigens in Raji cells is blocked by selective protein kinase-C inhibitors
    • Lazdins J., Zompetta C., Grimaldi S., Barile G., Venanzoni M., Frati L., Faggioni A. TPA induction of Epstein-Barr virus early antigens in Raji cells is blocked by selective protein kinase-C inhibitors. Int. J. Cancer 1987, 40:846-849.
    • (1987) Int. J. Cancer , vol.40 , pp. 846-849
    • Lazdins, J.1    Zompetta, C.2    Grimaldi, S.3    Barile, G.4    Venanzoni, M.5    Frati, L.6    Faggioni, A.7
  • 40
    • 47349133539 scopus 로고    scopus 로고
    • NF-kappaB inhibitors induce lytic cytotoxicity in Epstein-Barr virus-positive nasopharyngeal carcinoma cells
    • Liu S.F., Wang H., Lin X.C., Xiang H., Deng X.Y., Li W., Tang M., Cao Y. NF-kappaB inhibitors induce lytic cytotoxicity in Epstein-Barr virus-positive nasopharyngeal carcinoma cells. Cell Biol. Int. 2008, 32:1006-1013.
    • (2008) Cell Biol. Int. , vol.32 , pp. 1006-1013
    • Liu, S.F.1    Wang, H.2    Lin, X.C.3    Xiang, H.4    Deng, X.Y.5    Li, W.6    Tang, M.7    Cao, Y.8
  • 41
    • 0036255961 scopus 로고    scopus 로고
    • Direct targeting of human cytomegalovirus protein kinase pUL97 by kinase inhibitors is a novel principle for antiviral therapy
    • Marschall M., Stein-Gerlach M., Freitag M., Kupfer R., van den Bogaard M., Stamminger T. Direct targeting of human cytomegalovirus protein kinase pUL97 by kinase inhibitors is a novel principle for antiviral therapy. J. Gen. Virol. 2002, 83:1013-1023.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1013-1023
    • Marschall, M.1    Stein-Gerlach, M.2    Freitag, M.3    Kupfer, R.4    van den Bogaard, M.5    Stamminger, T.6
  • 42
    • 0028220187 scopus 로고
    • Identification of the glycogenic compound 5-iodotubercidin as a general protein kinase inhibitor
    • Massillon D., Stalmans W., van de Werve G., Bollen M. Identification of the glycogenic compound 5-iodotubercidin as a general protein kinase inhibitor. Biochem. J. 1994, 299(Pt. 1):123-128.
    • (1994) Biochem. J. , vol.299 , Issue.PART 1 , pp. 123-128
    • Massillon, D.1    Stalmans, W.2    van de Werve, G.3    Bollen, M.4
  • 43
    • 0027208282 scopus 로고
    • Inhibition by Ro 31-8220 of acid secretory activity induced by carbachol indicates a stimulatory role for protein kinase C in the action of muscarinic agonists on isolated rat parietal cells
    • McKenna J.P., Hanson P.J. Inhibition by Ro 31-8220 of acid secretory activity induced by carbachol indicates a stimulatory role for protein kinase C in the action of muscarinic agonists on isolated rat parietal cells. Biochem. Pharmacol. 1993, 46:583-588.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 583-588
    • McKenna, J.P.1    Hanson, P.J.2
  • 44
    • 33744736666 scopus 로고    scopus 로고
    • Functional role of phosphatidylinositol 3-kinase/Akt pathway on cell growth and lytic cycle of Epstein-Barr virus in the Burkitt's lymphoma cell line, P3HR-1
    • Mori T., Sairenji T. Functional role of phosphatidylinositol 3-kinase/Akt pathway on cell growth and lytic cycle of Epstein-Barr virus in the Burkitt's lymphoma cell line, P3HR-1. Virus Genes 2006, 32:327-334.
    • (2006) Virus Genes , vol.32 , pp. 327-334
    • Mori, T.1    Sairenji, T.2
  • 46
    • 80052057357 scopus 로고    scopus 로고
    • NF-kappaB-mediated modulation of inducible nitric oxide synthase activity controls induction of the Epstein-Barr virus productive cycle by transforming growth factor beta 1
    • Oussaief L., Ramirez V., Hippocrate A., Arbach H., Cochet C., Proust A., Raphael M., Khelifa R., Joab I. NF-kappaB-mediated modulation of inducible nitric oxide synthase activity controls induction of the Epstein-Barr virus productive cycle by transforming growth factor beta 1. J. Virol. 2011, 85:6502-6512.
    • (2011) J. Virol. , vol.85 , pp. 6502-6512
    • Oussaief, L.1    Ramirez, V.2    Hippocrate, A.3    Arbach, H.4    Cochet, C.5    Proust, A.6    Raphael, M.7    Khelifa, R.8    Joab, I.9
  • 47
    • 0026806059 scopus 로고
    • Herpes simplex virus type 1 gene UL13 encodes a phosphoprotein that is a component of the virion
    • Overton H.A., McMillan D.J., Klavinskis L.S., Hope L., Ritchie A.J., Wong-kai-in P. Herpes simplex virus type 1 gene UL13 encodes a phosphoprotein that is a component of the virion. Virology 1992, 190:184-192.
    • (1992) Virology , vol.190 , pp. 184-192
    • Overton, H.A.1    McMillan, D.J.2    Klavinskis, L.S.3    Hope, L.4    Ritchie, A.J.5    Wong-kai-in, P.6
  • 50
    • 0030772376 scopus 로고    scopus 로고
    • Novel inhibitors of cytokine-induced IkappaBalpha phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo
    • Pierce J.W., Schoenleber R., Jesmok G., Best J., Moore S.A., Collins T., Gerritsen M.E. Novel inhibitors of cytokine-induced IkappaBalpha phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo. J. Biol. Chem. 1997, 272:21096-21103.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21096-21103
    • Pierce, J.W.1    Schoenleber, R.2    Jesmok, G.3    Best, J.4    Moore, S.A.5    Collins, T.6    Gerritsen, M.E.7
  • 51
    • 0033033631 scopus 로고    scopus 로고
    • A recombinant human cytomegalovirus with a large deletion in UL97 has a severe replication deficiency
    • Prichard M.N., Gao N., Jairath S., Mulamba G., Krosky P., Coen D.M., Parker B.O., Pari G.S. A recombinant human cytomegalovirus with a large deletion in UL97 has a severe replication deficiency. J. Virol. 1999, 73:5663-5670.
    • (1999) J. Virol. , vol.73 , pp. 5663-5670
    • Prichard, M.N.1    Gao, N.2    Jairath, S.3    Mulamba, G.4    Krosky, P.5    Coen, D.M.6    Parker, B.O.7    Pari, G.S.8
  • 52
    • 34249064632 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • Lippinkott-Wiliams & Wilkins, Philadelphia, D.M. Knipe, P.M. Howley (Eds.)
    • Rickinson A.B., Kieff E.D. Epstein-Barr virus. Fields Virology 2007, 2655-2700. Lippinkott-Wiliams & Wilkins, Philadelphia. fifth ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2007) Fields Virology , pp. 2655-2700
    • Rickinson, A.B.1    Kieff, E.D.2
  • 53
    • 33644536722 scopus 로고    scopus 로고
    • Mechanisms of apoptosis-induction by rottlerin: therapeutic implications for B-CLL
    • Ringshausen I., Oelsner M., Weick K., Bogner C., Peschel C., Decker T. Mechanisms of apoptosis-induction by rottlerin: therapeutic implications for B-CLL. Leukemia 2006, 20:514-520.
    • (2006) Leukemia , vol.20 , pp. 514-520
    • Ringshausen, I.1    Oelsner, M.2    Weick, K.3    Bogner, C.4    Peschel, C.5    Decker, T.6
  • 54
    • 0033021095 scopus 로고    scopus 로고
    • The interaction of mitogen-activated protein kinases to Epstein-Barr virus activation in Akata cells
    • Satoh T., Hoshikawa Y., Satoh Y., Kurata T., Sairenji T. The interaction of mitogen-activated protein kinases to Epstein-Barr virus activation in Akata cells. Virus Genes 1999, 18:57-64.
    • (1999) Virus Genes , vol.18 , pp. 57-64
    • Satoh, T.1    Hoshikawa, Y.2    Satoh, Y.3    Kurata, T.4    Sairenji, T.5
  • 55
    • 0033614949 scopus 로고    scopus 로고
    • Paullones, a series of cyclin-dependent kinase inhibitors: synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity
    • Schultz C., Link A., Leost M., Zaharevitz D.W., Gussio R., Sausville E.A., Meijer L., Kunick C. Paullones, a series of cyclin-dependent kinase inhibitors: synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity. J. Med. Chem. 1999, 42:2909-2919.
    • (1999) J. Med. Chem. , vol.42 , pp. 2909-2919
    • Schultz, C.1    Link, A.2    Leost, M.3    Zaharevitz, D.W.4    Gussio, R.5    Sausville, E.A.6    Meijer, L.7    Kunick, C.8
  • 56
    • 0021351866 scopus 로고
    • Cross-linking of cell surface immunoglobulins induces Epstein-Barr virus in Burkitt lymphoma lines
    • Takada K. Cross-linking of cell surface immunoglobulins induces Epstein-Barr virus in Burkitt lymphoma lines. Int. J. Cancer 1984, 33:27-32.
    • (1984) Int. J. Cancer , vol.33 , pp. 27-32
    • Takada, K.1
  • 57
    • 0025726282 scopus 로고
    • An Epstein-Barr virus-producer line Akata: establishment of the cell line and analysis of viral DNA
    • Takada K., Horinouchi K., Ono Y., Aya T., Osato T., Takahashi M., Hayasaka S. An Epstein-Barr virus-producer line Akata: establishment of the cell line and analysis of viral DNA. Virus Genes 1991, 5:147-156.
    • (1991) Virus Genes , vol.5 , pp. 147-156
    • Takada, K.1    Horinouchi, K.2    Ono, Y.3    Aya, T.4    Osato, T.5    Takahashi, M.6    Hayasaka, S.7
  • 58
    • 0018129364 scopus 로고
    • Activation of latent Epstein-Barr virus by antibody to human IgM
    • Tovey M.G., Lenoir G., Begon-Lours J. Activation of latent Epstein-Barr virus by antibody to human IgM. Nature 1978, 276:270-272.
    • (1978) Nature , vol.276 , pp. 270-272
    • Tovey, M.G.1    Lenoir, G.2    Begon-Lours, J.3
  • 59
    • 45149137825 scopus 로고
    • Inhibition of epidermal growth factor-induced DNA synthesis by tyrosine kinase inhibitors
    • Umezawa K., Hori T., Tajima H., Imoto M., Isshiki K., Takeuchi T. Inhibition of epidermal growth factor-induced DNA synthesis by tyrosine kinase inhibitors. FEBS Lett. 1990, 260:198-200.
    • (1990) FEBS Lett. , vol.260 , pp. 198-200
    • Umezawa, K.1    Hori, T.2    Tajima, H.3    Imoto, M.4    Isshiki, K.5    Takeuchi, T.6
  • 60
    • 0030955930 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein is phosphorylated and a component of virions
    • van Zeijl M., Fairhurst J., Baum E.Z., Sun L., Jones T.R. The human cytomegalovirus UL97 protein is phosphorylated and a component of virions. Virology 1997, 231:72-80.
    • (1997) Virology , vol.231 , pp. 72-80
    • van Zeijl, M.1    Fairhurst, J.2    Baum, E.Z.3    Sun, L.4    Jones, T.R.5
  • 61
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos C.J., Matter W.F., Hui K.Y., Brown R.F. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 1994, 269:5241-5248.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 62
    • 70450170134 scopus 로고    scopus 로고
    • Maribavir inhibits Epstein-Barr viral transcription in addition to viral DNA replication
    • Wang F.Z., Roy D., Gershburg E., Whitehurst C.B., Dittmer D.P., Pagano J.S. Maribavir inhibits Epstein-Barr viral transcription in addition to viral DNA replication. J Virol. 2009, 83:12108-12117.
    • (2009) J Virol. , vol.83 , pp. 12108-12117
    • Wang, F.Z.1    Roy, D.2    Gershburg, E.3    Whitehurst, C.B.4    Dittmer, D.P.5    Pagano, J.S.6
  • 64
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • Wymann M.P., Bulgarelli-Leva G., Zvelebil M.J., Pirola L., Vanhaesebroeck B., Waterfield M.D., Panayotou G. Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol. 1996, 16:1722-1733.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarelli-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroeck, B.5    Waterfield, M.D.6    Panayotou, G.7
  • 65
    • 0032816076 scopus 로고    scopus 로고
    • Inhibition of Epstein-Barr virus replication by a benzimidazole l-riboside: novel antiviral mechanism of 5,6-dichloro-2-(isopropylamino)-1-beta-l-ribofuranosyl-1H-benzimidazole
    • Zacny V.L., Gershburg E., Davis M.G., Biron K.K., Pagano J.S. Inhibition of Epstein-Barr virus replication by a benzimidazole l-riboside: novel antiviral mechanism of 5,6-dichloro-2-(isopropylamino)-1-beta-l-ribofuranosyl-1H-benzimidazole. J. Virol. 1999, 73:7271-7277.
    • (1999) J. Virol. , vol.73 , pp. 7271-7277
    • Zacny, V.L.1    Gershburg, E.2    Davis, M.G.3    Biron, K.K.4    Pagano, J.S.5
  • 66
    • 0033152122 scopus 로고    scopus 로고
    • Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases
    • Zaharevitz D.W., Gussio R., Leost M., Senderowicz A.M., Lahusen T., Kunick C., Meijer L., Sausville E.A. Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases. Cancer Res. 1999, 59:2566-2569.
    • (1999) Cancer Res. , vol.59 , pp. 2566-2569
    • Zaharevitz, D.W.1    Gussio, R.2    Leost, M.3    Senderowicz, A.M.4    Lahusen, T.5    Kunick, C.6    Meijer, L.7    Sausville, E.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.