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Volumn 81, Issue 10, 2007, Pages 5066-5078

Mitogen-activated protein kinases activate the nuclear localization sequence of human papillomavirus type 11 E1 DNA helicase to promote efficient nuclear import

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; CYCLIN DEPENDENT KINASE; GLYCOPROTEIN E1; GLYCOPROTEIN E2; HELICASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 3; PEPTIDE; SERINE; STRESS ACTIVATED PROTEIN KINASE; VIRUS DNA;

EID: 34248380889     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02480-06     Document Type: Article
Times cited : (40)

References (71)
  • 1
    • 4043175756 scopus 로고    scopus 로고
    • The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2
    • Abbate, E. A., J. M. Berger, and M. R. Botchan. 2004. The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2. Genes. Dev. 18:1981-1996.
    • (2004) Genes. Dev , vol.18 , pp. 1981-1996
    • Abbate, E.A.1    Berger, J.M.2    Botchan, M.R.3
  • 4
    • 0034691115 scopus 로고    scopus 로고
    • Identification of domains of the HPV11 E1 protein required for DNA replication in vitro
    • Amin, A. A., S. Titolo, A. Pelletier, D. Fink, M. G. Cordingley, and J. Archambault. 2000. Identification of domains of the HPV11 E1 protein required for DNA replication in vitro. Virology 272:137-150.
    • (2000) Virology , vol.272 , pp. 137-150
    • Amin, A.A.1    Titolo, S.2    Pelletier, A.3    Fink, D.4    Cordingley, M.G.5    Archambault, J.6
  • 5
    • 23744484474 scopus 로고    scopus 로고
    • Effects of the cyclin-dependent kinase inhibitor CYC202 (R-roscovitine) on the physiology of cultured human keratinocytes
    • Atanasova, G., R. Jans, N. Zhelev, V. Mitev, and Y. Poumay. 2005. Effects of the cyclin-dependent kinase inhibitor CYC202 (R-roscovitine) on the physiology of cultured human keratinocytes. Biochem. Pharmacol. 70:824-836.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 824-836
    • Atanasova, G.1    Jans, R.2    Zhelev, N.3    Mitev, V.4    Poumay, Y.5
  • 6
    • 33644840619 scopus 로고    scopus 로고
    • Retrovirus-mediated gene transfer to analyze HPV gene regulation and protein functions in organotypic "raft" cultures
    • Banerjee, N. S., L. T. Chow, and T. R. Broker. 2005. Retrovirus-mediated gene transfer to analyze HPV gene regulation and protein functions in organotypic "raft" cultures. Methods Mol. Med. 119:187-202.
    • (2005) Methods Mol. Med , vol.119 , pp. 187-202
    • Banerjee, N.S.1    Chow, L.T.2    Broker, T.R.3
  • 7
    • 33645226001 scopus 로고    scopus 로고
    • Molecular analysis of the PI3K-AKT pathway in uterine cervical neoplasia: Frequent PIK3CA amplification and AKT phosphorylation
    • Bertelsen, B. I., S. J. Steine, R. Sandvei, A. Molven, and O. D. Laerum. 2006. Molecular analysis of the PI3K-AKT pathway in uterine cervical neoplasia: frequent PIK3CA amplification and AKT phosphorylation. Int. J. Cancer 118:1877-1883.
    • (2006) Int. J. Cancer , vol.118 , pp. 1877-1883
    • Bertelsen, B.I.1    Steine, S.J.2    Sandvei, R.3    Molven, A.4    Laerum, O.D.5
  • 8
    • 33947355408 scopus 로고    scopus 로고
    • Nuclear import of bovine papillomavirus type 1 E1 protein is mediated by multiple alpha importins and is negatively regulated by phosphorylation near a nuclear localization signal
    • Bian, X. L., G. Rosas-Acosta, Y. C. Wu, and V. G. Wilson. 2007. Nuclear import of bovine papillomavirus type 1 E1 protein is mediated by multiple alpha importins and is negatively regulated by phosphorylation near a nuclear localization signal. J. Virol. 81:2899-2908.
    • (2007) J. Virol , vol.81 , pp. 2899-2908
    • Bian, X.L.1    Rosas-Acosta, G.2    Wu, Y.C.3    Wilson, V.G.4
  • 10
    • 0141682655 scopus 로고    scopus 로고
    • The human papillomavirus HPV2a E5 protein localizes to the Golgi apparatus and modulates signal transduction
    • Cartin, W., and A. Alonso. 2003. The human papillomavirus HPV2a E5 protein localizes to the Golgi apparatus and modulates signal transduction. Virology 314:572-579.
    • (2003) Virology , vol.314 , pp. 572-579
    • Cartin, W.1    Alonso, A.2
  • 11
    • 2442691552 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 amino acid 83 variants enhance E6-mediated MAPK signaling and differentially regulate tumorigenesis by notch signaling and oncogenic Ras
    • Chakrabarti, O., K. Veeraraghavalu, V. Tergaonkar, Y. Liu, E. J. Androphy, M. A. Stanley, and S. Krishna. 2004. Human papillomavirus type 16 E6 amino acid 83 variants enhance E6-mediated MAPK signaling and differentially regulate tumorigenesis by notch signaling and oncogenic Ras. J. Virol. 78:5934-5945.
    • (2004) J. Virol , vol.78 , pp. 5934-5945
    • Chakrabarti, O.1    Veeraraghavalu, K.2    Tergaonkar, V.3    Liu, Y.4    Androphy, E.J.5    Stanley, M.A.6    Krishna, S.7
  • 12
    • 33846096531 scopus 로고    scopus 로고
    • ErbB4 (JM-b/CYT-1)-induced expression and phosphorylation of c-Jun is abrogated by human papillomavirus type 16 E5 protein
    • Chen, S. L., S. T. Lin, T. C. Tsai, W. C. Hsiao, and Y. P. Tsao. 2007. ErbB4 (JM-b/CYT-1)-induced expression and phosphorylation of c-Jun is abrogated by human papillomavirus type 16 E5 protein. Oncogene 26:42-53.
    • (2007) Oncogene , vol.26 , pp. 42-53
    • Chen, S.L.1    Lin, S.T.2    Tsai, T.C.3    Hsiao, W.C.4    Tsao, Y.P.5
  • 13
    • 0028783782 scopus 로고
    • Differentiation-dependent up-regulation of the human papillomavirus E7 gene reactivates cellular DNA replication in suprabasal differentiated keratinocytes
    • Cheng, S., D. C. Schmidt-Grimminger, T. Murant, T. R. Broker, and L. T. Chow. 1995. Differentiation-dependent up-regulation of the human papillomavirus E7 gene reactivates cellular DNA replication in suprabasal differentiated keratinocytes. Genes Dev. 9:2335-2349.
    • (1995) Genes Dev , vol.9 , pp. 2335-2349
    • Cheng, S.1    Schmidt-Grimminger, D.C.2    Murant, T.3    Broker, T.R.4    Chow, L.T.5
  • 14
    • 0026769936 scopus 로고
    • Viral E1 and E2 proteins support replication of homologous and heterologous papillomaviral origins
    • Chiang, C. M., M. Ustav, A. Stenlund, T. F. Ho, T. R. Broker, and L. T. Chow. 1992. Viral E1 and E2 proteins support replication of homologous and heterologous papillomaviral origins. Proc. Natl. Acad. Sci. USA 89: 5799-5803.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5799-5803
    • Chiang, C.M.1    Ustav, M.2    Stenlund, A.3    Ho, T.F.4    Broker, T.R.5    Chow, L.T.6
  • 15
    • 84919845342 scopus 로고    scopus 로고
    • Human papillomavirus transcription
    • R. L. Garcea and D. OiMaio ed, Springer Science and Business Media, New York, N.Y
    • Chow, L. T., and T. R. Broker. 2007. Human papillomavirus transcription, p. 119-131. In R. L. Garcea and D. OiMaio (ed.), The papillomaviruses. Springer Science and Business Media, New York, N.Y.
    • (2007) The papillomaviruses , pp. 119-131
    • Chow, L.T.1    Broker, T.R.2
  • 16
    • 33646447010 scopus 로고    scopus 로고
    • Mechanisms and regulation of papillomavirus DNA replication
    • M. S. Campo ed, Caister Academic Press, Norwich, United Kingdom
    • Chow, L. T., and T. R. Broker. 2006. Mechanisms and regulation of papillomavirus DNA replication, p. 53-71. In M. S. Campo (ed.), Papillomavirus research: from natural history to vaccines and beyond. Caister Academic Press, Norwich, United Kingdom.
    • (2006) Papillomavirus research: From natural history to vaccines and beyond , pp. 53-71
    • Chow, L.T.1    Broker, T.R.2
  • 17
    • 31144446588 scopus 로고    scopus 로고
    • Papillomavirus E1 protein binds to and stimulates human topoisomerase I
    • Clower, R. V., J. C. Fisk, and T. Melendy. 2006. Papillomavirus E1 protein binds to and stimulates human topoisomerase I. J. Virol. 80:1584-1587.
    • (2006) J. Virol , vol.80 , pp. 1584-1587
    • Clower, R.V.1    Fisk, J.C.2    Melendy, T.3
  • 18
    • 0030841793 scopus 로고    scopus 로고
    • PDK1, one of the missing links in insulin signal transduction?
    • Cohen, P., D. R. Alessi, and D. A. Cross. 1997. PDK1, one of the missing links in insulin signal transduction? FEBS Lett. 410:3-10.
    • (1997) FEBS Lett , vol.410 , pp. 3-10
    • Cohen, P.1    Alessi, D.R.2    Cross, D.A.3
  • 20
    • 0033613848 scopus 로고    scopus 로고
    • Human papillomavirus DNA replication. Interactions between the viral E1 protein and two subunits of human DNA polymerase alpha/primase
    • Conger, K. L., J. S. Liu, S. R. Kuo, L. T. Chow, and T. S. Wang. 1999. Human papillomavirus DNA replication. Interactions between the viral E1 protein and two subunits of human DNA polymerase alpha/primase. J. Biol. Chem. 274:2696-2705.
    • (1999) J. Biol. Chem , vol.274 , pp. 2696-2705
    • Conger, K.L.1    Liu, J.S.2    Kuo, S.R.3    Chow, L.T.4    Wang, T.S.5
  • 21
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D. A., D. R. Alessi, P. Cohen, M. Andjelkovich, and B. A. Hemmings. 1995. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 22
    • 0030866665 scopus 로고    scopus 로고
    • Enhancement of EGF- and PMA-mediated MAP kinase activation in cells expressing the human papillomavirus type 16 E5 protein
    • Crusius, K., E. Auvinen, and A. Alonso. 1997. Enhancement of EGF- and PMA-mediated MAP kinase activation in cells expressing the human papillomavirus type 16 E5 protein. Oncogene 15:1437-1444.
    • (1997) Oncogene , vol.15 , pp. 1437-1444
    • Crusius, K.1    Auvinen, E.2    Alonso, A.3
  • 23
    • 0031818511 scopus 로고    scopus 로고
    • The human papillomavirus type 16 E5-protein modulates ligand-dependent activation of the EGF receptor family in the human epithelial cell line HaCaT
    • Crusius, K., E. Auvinen, B. Steuer, H. Gaissert, and A. Alonso. 1998. The human papillomavirus type 16 E5-protein modulates ligand-dependent activation of the EGF receptor family in the human epithelial cell line HaCaT. Exp. Cell Res. 241:76-83.
    • (1998) Exp. Cell Res , vol.241 , pp. 76-83
    • Crusius, K.1    Auvinen, E.2    Steuer, B.3    Gaissert, H.4    Alonso, A.5
  • 24
    • 0034064436 scopus 로고    scopus 로고
    • The human papillomavirus type 16 E5 protein modulates ERK1/2 and p38 MAP kinase activation by an EGFR-independent process in stressed human keratinocytes
    • Crusius, K., I. Rodriguez, and A. Alonso. 2000. The human papillomavirus type 16 E5 protein modulates ERK1/2 and p38 MAP kinase activation by an EGFR-independent process in stressed human keratinocytes. Virus Genes 20:65-69.
    • (2000) Virus Genes , vol.20 , pp. 65-69
    • Crusius, K.1    Rodriguez, I.2    Alonso, A.3
  • 25
    • 0031816874 scopus 로고    scopus 로고
    • Functional interaction between the bovine papillomavirus virus type 1 replicative helicase E1 and cyclin E-Cdk2
    • Cueille, N., R. Nougarede, F. Mechali, M. Philippe, and C. Bonne-Andrea. 1998. Functional interaction between the bovine papillomavirus virus type 1 replicative helicase E1 and cyclin E-Cdk2. J. Virol. 72:7255-7262.
    • (1998) J. Virol , vol.72 , pp. 7255-7262
    • Cueille, N.1    Nougarede, R.2    Mechali, F.3    Philippe, M.4    Bonne-Andrea, C.5
  • 26
    • 0141856408 scopus 로고    scopus 로고
    • mRNA splicing regulates human papillomavirus type 11 E1 protein production and DNA replication
    • Deng, W., G. Jin, B. Y. Lin, B. A. Van Tine, T. R. Broker, and L. T. Chow. 2003. mRNA splicing regulates human papillomavirus type 11 E1 protein production and DNA replication. J. Virol. 77:10213-10226.
    • (2003) J. Virol , vol.77 , pp. 10213-10226
    • Deng, W.1    Jin, G.2    Lin, B.Y.3    Van Tine, B.A.4    Broker, T.R.5    Chow, L.T.6
  • 27
    • 10044284508 scopus 로고    scopus 로고
    • Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase
    • Deng, W., B. Y. Lin, G. Jin, C. G. Wheeler, T. Ma, J. W. Harper, T. R. Broker, and L. T. Chow. 2004. Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase. J. Virol. 78:13954-13965.
    • (2004) J. Virol , vol.78 , pp. 13954-13965
    • Deng, W.1    Lin, B.Y.2    Jin, G.3    Wheeler, C.G.4    Ma, T.5    Harper, J.W.6    Broker, T.R.7    Chow, L.T.8
  • 28
    • 0033548196 scopus 로고    scopus 로고
    • Biochemical and electron microscopic image analysis of the hexameric E1 helicase
    • Fouts, E. T., X. Yu, E. H. Egelman, and M. R. Botchan. 1999. Biochemical and electron microscopic image analysis of the hexameric E1 helicase. J. Biol. Chem. 274:4447-4458.
    • (1999) J. Biol. Chem , vol.274 , pp. 4447-4458
    • Fouts, E.T.1    Yu, X.2    Egelman, E.H.3    Botchan, M.R.4
  • 29
    • 0035847076 scopus 로고    scopus 로고
    • Selective targeting of MAPKs to the ETS domain transcription factor SAP-1
    • Galanis, A., S. H. Yang, and A. D. Sharrocks. 2001. Selective targeting of MAPKs to the ETS domain transcription factor SAP-1. J. Biol. Chem. 276:965-973.
    • (2001) J. Biol. Chem , vol.276 , pp. 965-973
    • Galanis, A.1    Yang, S.H.2    Sharrocks, A.D.3
  • 30
    • 1842639246 scopus 로고    scopus 로고
    • Regulation of MAPK activation, AP-1 transcription factor expression and keratinocyte differentiation in wounded fetal skin
    • Gangnuss, S., A. J. Cowin, I. S. Daehn, N. Hatzirodos, J. A. Rothnagel, A. Varelias, and T. E. Rayner. 2004. Regulation of MAPK activation, AP-1 transcription factor expression and keratinocyte differentiation in wounded fetal skin. J. Investig. Dermatol. 122:791-804.
    • (2004) J. Investig. Dermatol , vol.122 , pp. 791-804
    • Gangnuss, S.1    Cowin, A.J.2    Daehn, I.S.3    Hatzirodos, N.4    Rothnagel, J.A.5    Varelias, A.6    Rayner, T.E.7
  • 31
    • 0022516246 scopus 로고
    • Synthetic peptides as nuclear localization signals
    • Goldfarb, D. S., J. Gariepy, G. Schoolnik, and R. D. Kornberg. 1986. Synthetic peptides as nuclear localization signals. Nature 322:641-644.
    • (1986) Nature , vol.322 , pp. 641-644
    • Goldfarb, D.S.1    Gariepy, J.2    Schoolnik, G.3    Kornberg, R.D.4
  • 32
    • 0028788028 scopus 로고
    • Effect of human papillomavirus type 16 oncogenes on MAP kinase activity
    • Gu, Z., and G. Matlashewski. 1995. Effect of human papillomavirus type 16 oncogenes on MAP kinase activity. J. Virol. 69:8051-8056.
    • (1995) J. Virol , vol.69 , pp. 8051-8056
    • Gu, Z.1    Matlashewski, G.2
  • 33
    • 0033060916 scopus 로고    scopus 로고
    • Interactions of the papovavirus DNA replication initiator proteins, bovine papillomavirus type 1 E1 and simian virus 40 large T antigen, with human replication protein A
    • Han, Y., Y. M. Loo, K. T. Militello, and T. Melendy. 1999. Interactions of the papovavirus DNA replication initiator proteins, bovine papillomavirus type 1 E1 and simian virus 40 large T antigen, with human replication protein A. J. Virol. 73:4899-4907.
    • (1999) J. Virol , vol.73 , pp. 4899-4907
    • Han, Y.1    Loo, Y.M.2    Militello, K.T.3    Melendy, T.4
  • 35
    • 33845806868 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of bovine papillomavirus E1 helicase downregulates viral DNA replication in S phase
    • Hsu, C. Y., F. Mechali, and C. Bonne-Andrea. 2007. Nucleocytoplasmic shuttling of bovine papillomavirus E1 helicase downregulates viral DNA replication in S phase. J. Virol. 81:384-394.
    • (2007) J. Virol , vol.81 , pp. 384-394
    • Hsu, C.Y.1    Mechali, F.2    Bonne-Andrea, C.3
  • 36
    • 0038495741 scopus 로고    scopus 로고
    • JNK phosphorylates paxillin and regulates cell migration
    • Huang, C., Z. Rajfur, C. Borchers, M. D. Schaller, and K. Jacobson. 2003. JNK phosphorylates paxillin and regulates cell migration. Nature 424:219-223.
    • (2003) Nature , vol.424 , pp. 219-223
    • Huang, C.1    Rajfur, Z.2    Borchers, C.3    Schaller, M.D.4    Jacobson, K.5
  • 37
    • 0033555229 scopus 로고    scopus 로고
    • Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
    • Jacobs, D., D. Glossip, H. Xing, A. J. Muslin, and K. Kornfeld. 1999. Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev. 13:163-175.
    • (1999) Genes Dev , vol.13 , pp. 163-175
    • Jacobs, D.1    Glossip, D.2    Xing, H.3    Muslin, A.J.4    Kornfeld, K.5
  • 38
    • 0029797971 scopus 로고    scopus 로고
    • Regulation of protein transport to the nucleus: Central role of phosphorylation
    • Jans, D. A., and S. Hubner. 1996. Regulation of protein transport to the nucleus: Central role of phosphorylation. Physiol. Rev. 76:651-685.
    • (1996) Physiol. Rev , vol.76 , pp. 651-685
    • Jans, D.A.1    Hubner, S.2
  • 39
    • 33646585409 scopus 로고    scopus 로고
    • Human papillomavirus 16 E5 up-regulates the expression of vascular endothelial growth factor through the activation of epidermal growth factor receptor, MEK/ERK1,2 and PI3K/Akt
    • Kim, S. H., Y. S. Juhnn, S. Kang, S. W. Park, M. W. Sung, Y. J. Bang, and Y. S. Song. 2006. Human papillomavirus 16 E5 up-regulates the expression of vascular endothelial growth factor through the activation of epidermal growth factor receptor, MEK/ERK1,2 and PI3K/Akt. Cell. Mol. Life Sci. 63:930-938.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 930-938
    • Kim, S.H.1    Juhnn, Y.S.2    Kang, S.3    Park, S.W.4    Sung, M.W.5    Bang, Y.J.6    Song, Y.S.7
  • 40
    • 0028003643 scopus 로고
    • Cell-free replication of the human papillomavirus DNA with homologous viral E1 and E2 proteins and human cell extracts
    • Kuo, S. R., J. S. Liu, T. R. Broker, and L. T. Chow. 1994. Cell-free replication of the human papillomavirus DNA with homologous viral E1 and E2 proteins and human cell extracts. J. Biol. Chem. 269:24058-24065.
    • (1994) J. Biol. Chem , vol.269 , pp. 24058-24065
    • Kuo, S.R.1    Liu, J.S.2    Broker, T.R.3    Chow, L.T.4
  • 41
    • 0028100499 scopus 로고
    • Genetically defined nuclear localization signal sequence of bovine papillomavirus E1 protein is necessary and sufficient for the nuclear localization of E1-beta-galactosidase fusion proteins
    • Leng, X., and V. G. Wilson. 1994. Genetically defined nuclear localization signal sequence of bovine papillomavirus E1 protein is necessary and sufficient for the nuclear localization of E1-beta-galactosidase fusion proteins. J. Gen. Virol. 75:2463-2467.
    • (1994) J. Gen. Virol , vol.75 , pp. 2463-2467
    • Leng, X.1    Wilson, V.G.2
  • 42
    • 0027394518 scopus 로고
    • The E1 replication protein of bovine papillomavirus type 1 contains an extended nuclear localization signal that includes a p34cdc2 phosphorylation site
    • Lentz, M. R., D. Pak, I. Mohr, and M. R. Botchan. 1993. The E1 replication protein of bovine papillomavirus type 1 contains an extended nuclear localization signal that includes a p34cdc2 phosphorylation site. J. Virol. 67:1414-1423.
    • (1993) J. Virol , vol.67 , pp. 1414-1423
    • Lentz, M.R.1    Pak, D.2    Mohr, I.3    Botchan, M.R.4
  • 43
    • 0009494546 scopus 로고    scopus 로고
    • HeLa cells are phenotypically limiting in cyclin E/CDK2 for efficient human papillomavirus DNA replication
    • Lin, B. Y., T. Ma, J. S. Liu, S. R. Kuo, G. Jin, T. R. Broker, J. W. Harper, and L. T. Chow. 2000. HeLa cells are phenotypically limiting in cyclin E/CDK2 for efficient human papillomavirus DNA replication. J. Biol. Chem. 275: 6167-6174.
    • (2000) J. Biol. Chem , vol.275 , pp. 6167-6174
    • Lin, B.Y.1    Ma, T.2    Liu, J.S.3    Kuo, S.R.4    Jin, G.5    Broker, T.R.6    Harper, J.W.7    Chow, L.T.8
  • 44
    • 0036723643 scopus 로고    scopus 로고
    • Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein
    • Lin, B. Y., A. M. Makhov, J. D. Griffith, T. R. Broker, and L. T. Chow. 2002. Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein. Mol. Cell. Biol. 22:6592-6604.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6592-6604
    • Lin, B.Y.1    Makhov, A.M.2    Griffith, J.D.3    Broker, T.R.4    Chow, L.T.5
  • 45
    • 15144340443 scopus 로고    scopus 로고
    • Human Hsp70 and Hsp40 chaperone proteins facilitate human papillomavirus-11 E1 protein binding to the origin and stimulate cell-free DNA replication
    • Liu, J. S., S. R. Kuo, A. M. Makhov, D. M. Cyr, J. D. Griffith, T. R. Broker, and L. T. Chow. 1998. Human Hsp70 and Hsp40 chaperone proteins facilitate human papillomavirus-11 E1 protein binding to the origin and stimulate cell-free DNA replication. J. Biol. Chem. 273:30704-30712.
    • (1998) J. Biol. Chem , vol.273 , pp. 30704-30712
    • Liu, J.S.1    Kuo, S.R.2    Makhov, A.M.3    Cyr, D.M.4    Griffith, J.D.5    Broker, T.R.6    Chow, L.T.7
  • 46
    • 0842304459 scopus 로고    scopus 로고
    • Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNA
    • Loo, Y. M., and T. Melendy. 2004. Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNA. J. Virol. 78:1605-1615.
    • (2004) J. Virol , vol.78 , pp. 1605-1615
    • Loo, Y.M.1    Melendy, T.2
  • 47
    • 0029778177 scopus 로고    scopus 로고
    • Role of c-Src tyrosine kinase in G protein-coupled receptor- and Gβγ subunit-mediated activation of mitogen-activated protein kinases
    • Luttrell, L. M., B. E. Hawes, T. van Biesen, D. K. Luttrell, T. J. Lansing, and R. J. Lefkowitz. 1996. Role of c-Src tyrosine kinase in G protein-coupled receptor- and Gβγ subunit-mediated activation of mitogen-activated protein kinases. J. Biol. Chem. 271:19443-19450.
    • (1996) J. Biol. Chem , vol.271 , pp. 19443-19450
    • Luttrell, L.M.1    Hawes, B.E.2    van Biesen, T.3    Luttrell, D.K.4    Lansing, T.J.5    Lefkowitz, R.J.6
  • 48
    • 0033582278 scopus 로고    scopus 로고
    • Interaction between cyclin-dependent kinases and human papillomavirus replication-initiation protein E1 is required for efficient viral replication
    • Ma, T., N. Zou, B. Y. Lin, L. T. Chow, and J. W. Harper. 1999. Interaction between cyclin-dependent kinases and human papillomavirus replication-initiation protein E1 is required for efficient viral replication. Proc. Natl. Acad. Sci. USA 96:382-387.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 382-387
    • Ma, T.1    Zou, N.2    Lin, B.Y.3    Chow, L.T.4    Harper, J.W.5
  • 49
    • 0036828204 scopus 로고    scopus 로고
    • Regulation of bovine papillomavirus replicative helicase e1 by the ubiquitin-proteasome pathway
    • Malcles, M. H., N. Cueille, F. Mechali, O. Coux, and C. Bonne-Andrea. 2002. Regulation of bovine papillomavirus replicative helicase e1 by the ubiquitin-proteasome pathway. J. Virol. 76:11350-11358.
    • (2002) J. Virol , vol.76 , pp. 11350-11358
    • Malcles, M.H.1    Cueille, N.2    Mechali, F.3    Coux, O.4    Bonne-Andrea, C.5
  • 50
    • 0031818287 scopus 로고    scopus 로고
    • A C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit
    • Masterson, P. J., M. A. Stanley, A. P. Lewis, and M. A. Romanos. 1998. A C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit. J. Virol. 72:7407-7419.
    • (1998) J. Virol , vol.72 , pp. 7407-7419
    • Masterson, P.J.1    Stanley, M.A.2    Lewis, A.P.3    Romanos, M.A.4
  • 51
    • 0033590164 scopus 로고    scopus 로고
    • Distantly related cousins of MAP kinase: Biochemical properties and possible physiological functions
    • Miyata, Y., and E. Nishida. 1999. Distantly related cousins of MAP kinase: biochemical properties and possible physiological functions. Biochem. Biophys. Res. Commun. 266:291-295.
    • (1999) Biochem. Biophys. Res. Commun , vol.266 , pp. 291-295
    • Miyata, Y.1    Nishida, E.2
  • 52
    • 1942437991 scopus 로고    scopus 로고
    • SUMO: A regulator of gene expression and genome integrity
    • Muller, S., A. Ledl, and D. Schmidt. 2004. SUMO: a regulator of gene expression and genome integrity. Oncogene 23:1998-2008.
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Muller, S.1    Ledl, A.2    Schmidt, D.3
  • 53
    • 0033578418 scopus 로고    scopus 로고
    • Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination
    • Oda, H., S. Kumar, and P. M. Howley. 1999. Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination. Proc. Natl. Acad. Sci. USA 96:9557-9562.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9557-9562
    • Oda, H.1    Kumar, S.2    Howley, P.M.3
  • 54
    • 0028133256 scopus 로고
    • The cellular DNA polymerase alpha-primase is required for papillomavirus DNA replication and associates with the viral E1 helicase
    • Park, P., W. Copeland, L. Yang, T. Wang, M. R. Botchan, and I. J. Mohr. 1994. The cellular DNA polymerase alpha-primase is required for papillomavirus DNA replication and associates with the viral E1 helicase. Proc. Natl. Acad. Sci. USA 91:8700-8704.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8700-8704
    • Park, P.1    Copeland, W.2    Yang, L.3    Wang, T.4    Botchan, M.R.5    Mohr, I.J.6
  • 55
    • 0035052197 scopus 로고    scopus 로고
    • Human papillomavirus type 6b virus-like particles are able to activate the Ras-MAP kinase pathway and induce cell proliferation
    • Payne, E., M. R. Bowles, A. Don, J. F. Hancock, and N. A. McMillan. 2001. Human papillomavirus type 6b virus-like particles are able to activate the Ras-MAP kinase pathway and induce cell proliferation. J. Virol. 75:4150-4157.
    • (2001) J. Virol , vol.75 , pp. 4150-4157
    • Payne, E.1    Bowles, M.R.2    Don, A.3    Hancock, J.F.4    McMillan, N.A.5
  • 56
    • 28344447599 scopus 로고    scopus 로고
    • Activation of the protein kinase B pathway by the HPV-16 E7 oncoprotein occurs through a mechanism involving interaction with PP2A
    • Pim, D., P. Massimi, S. M. Dilworth, and L. Banks. 2005. Activation of the protein kinase B pathway by the HPV-16 E7 oncoprotein occurs through a mechanism involving interaction with PP2A. Oncogene 24:7830-7838.
    • (2005) Oncogene , vol.24 , pp. 7830-7838
    • Pim, D.1    Massimi, P.2    Dilworth, S.M.3    Banks, L.4
  • 57
    • 0034730653 scopus 로고    scopus 로고
    • Bovine papillomavirus E1 protein is sumoylated by the host cell Ubc9 protein
    • Rangasamy, D., and V. G. Wilson. 2000. Bovine papillomavirus E1 protein is sumoylated by the host cell Ubc9 protein. J. Biol. Chem. 275:30487-30495.
    • (2000) J. Biol. Chem , vol.275 , pp. 30487-30495
    • Rangasamy, D.1    Wilson, V.G.2
  • 58
    • 0034532450 scopus 로고    scopus 로고
    • SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation
    • Rangasamy, D., K. Woytek, S. A. Khan, and V. G. Wilson. 2000. SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation. J. Biol. Chem. 275:37999-38004.
    • (2000) J. Biol. Chem , vol.275 , pp. 37999-38004
    • Rangasamy, D.1    Woytek, K.2    Khan, S.A.3    Wilson, V.G.4
  • 59
    • 9944247534 scopus 로고    scopus 로고
    • Proteins of the PIAS family enhance the sumoylation of the papillomavirus E1 protein
    • Rosas-Acosta, G., M. A. Langereis, A. Deyrieux, and V. G. Wilson. 2005. Proteins of the PIAS family enhance the sumoylation of the papillomavirus E1 protein. Virology 331:190-203.
    • (2005) Virology , vol.331 , pp. 190-203
    • Rosas-Acosta, G.1    Langereis, M.A.2    Deyrieux, A.3    Wilson, V.G.4
  • 60
    • 27644484567 scopus 로고    scopus 로고
    • Assembly of a double hexameric helicase
    • Schuck, S., and A. Stenlund. 2005. Assembly of a double hexameric helicase. Mol. Cell 20:377-389.
    • (2005) Mol. Cell , vol.20 , pp. 377-389
    • Schuck, S.1    Stenlund, A.2
  • 61
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of SUMO
    • Seeler, J. S., and A. Dejean. 2003. Nuclear and unclear functions of SUMO. Nat. Rev. Mol. Cell Biol. 4:690-699.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 690-699
    • Seeler, J.S.1    Dejean, A.2
  • 62
    • 0030712317 scopus 로고    scopus 로고
    • Further evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/ PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216
    • Shaw, M., P. Cohen, and D. R. Alessi. 1997. Further evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/ PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216. FEBS Lett. 416:307-311.
    • (1997) FEBS Lett , vol.416 , pp. 307-311
    • Shaw, M.1    Cohen, P.2    Alessi, D.R.3
  • 63
    • 0141891451 scopus 로고    scopus 로고
    • Initiation of DNA replication: Lessons from viral initiator proteins
    • Stenlund, A. 2003. Initiation of DNA replication: lessons from viral initiator proteins. Nat. Rev. Mol. Cell Biol. 4:777-785.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 777-785
    • Stenlund, A.1
  • 64
    • 0000557716 scopus 로고    scopus 로고
    • Human papillomavirus DNA replication compartments in a transient DNA replication system
    • Swindle, C. S., N. Zou, B. A. Van Tine, G. M. Shaw, J. A. Engler, and L. T. Chow. 1999. Human papillomavirus DNA replication compartments in a transient DNA replication system. J. Virol. 73:1001-1009.
    • (1999) J. Virol , vol.73 , pp. 1001-1009
    • Swindle, C.S.1    Zou, N.2    Van Tine, B.A.3    Shaw, G.M.4    Engler, J.A.5    Chow, L.T.6
  • 65
    • 0037400611 scopus 로고    scopus 로고
    • Molecular recognitions in the MAP kinase cascades
    • Tanoue, T., and E. Nishida. 2003. Molecular recognitions in the MAP kinase cascades. Cell. Signal. 15:455-462.
    • (2003) Cell. Signal , vol.15 , pp. 455-462
    • Tanoue, T.1    Nishida, E.2
  • 66
    • 3142544806 scopus 로고    scopus 로고
    • Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1
    • Terui, Y., N. Saad, S. Jia, F. McKeon, and J. Yuan. 2004. Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1. J. Biol. Chem. 279:28257-28265.
    • (2004) J. Biol. Chem , vol.279 , pp. 28257-28265
    • Terui, Y.1    Saad, N.2    Jia, S.3    McKeon, F.4    Yuan, J.5
  • 68
    • 0036787917 scopus 로고    scopus 로고
    • E7 abolishes raf-induced arrest via mislocalization of p21(Cip1)
    • Westbrook, T. F., D. X. Nguyen, B. R. Thrash, and D. J. McCance. 2002. E7 abolishes raf-induced arrest via mislocalization of p21(Cip1). Mol. Cell. Biol. 22:7041-7052.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7041-7052
    • Westbrook, T.F.1    Nguyen, D.X.2    Thrash, B.R.3    McCance, D.J.4
  • 69
    • 16444367966 scopus 로고    scopus 로고
    • Stress-activated protein kinases mediate cell migration in human airway epithelial cells
    • White, S. R., R. Tse, and B. A. Marroquin. 2005. Stress-activated protein kinases mediate cell migration in human airway epithelial cells. Am. J. Respir. Cell Mol. Biol. 32:301-310.
    • (2005) Am. J. Respir. Cell Mol. Biol , vol.32 , pp. 301-310
    • White, S.R.1    Tse, R.2    Marroquin, B.A.3
  • 70
    • 1642279290 scopus 로고    scopus 로고
    • TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor
    • Xu, J., Y. J. Lai, W. C. Lin, and F. T. Lin. 2004. TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor. J. Biol. Chem. 279:10459-10468.
    • (2004) J. Biol. Chem , vol.279 , pp. 10459-10468
    • Xu, J.1    Lai, Y.J.2    Lin, W.C.3    Lin, F.T.4
  • 71
    • 17144434362 scopus 로고    scopus 로고
    • The hinge of the human papillomavirus type 11 E2 protein contains major determinants for nuclear localization and nuclear matrix association
    • Zou, N., B. Y. Lin, F. Duan, K. Y. Lee, G. Jin, R. Guan, G. Yao, E. J. Lefkowitz, T. R. Broker, and L. T. Chow. 2000. The hinge of the human papillomavirus type 11 E2 protein contains major determinants for nuclear localization and nuclear matrix association. J. Virol. 74:3761-3770.
    • (2000) J. Virol , vol.74 , pp. 3761-3770
    • Zou, N.1    Lin, B.Y.2    Duan, F.3    Lee, K.Y.4    Jin, G.5    Guan, R.6    Yao, G.7    Lefkowitz, E.J.8    Broker, T.R.9    Chow, L.T.10


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