메뉴 건너뛰기




Volumn 85, Issue 23, 2011, Pages 12585-12593

Human cytomegalovirus induces multiple means to combat reactive oxygen species

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN PEROXIDE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; RAPTOR PROTEIN; REACTIVE OXYGEN METABOLITE; SERINE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 81255200303     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05572-11     Document Type: Article
Times cited : (46)

References (56)
  • 2
    • 48849093563 scopus 로고    scopus 로고
    • Modulation of host cell stress responses by human cytomegalovirus
    • Alwine, J. C. 2008. Modulation of host cell stress responses by human cytomegalovirus. Curr. Top. Microbiol. Immunol. 325:263-279.
    • (2008) Curr. Top. Microbiol. Immunol. , vol.325 , pp. 263-279
    • Alwine, J.C.1
  • 3
    • 27844562649 scopus 로고    scopus 로고
    • Tuberous sclerosis complex: linking growth and energy signaling pathways with human disease
    • Astrinidis, A., and E. P. Henske. 2005. Tuberous sclerosis complex: linking growth and energy signaling pathways with human disease. Oncogene 24: 7475-7481.
    • (2005) Oncogene , vol.24 , pp. 7475-7481
    • Astrinidis, A.1    Henske, E.P.2
  • 4
    • 4243987802 scopus 로고    scopus 로고
    • L-S,R-Buthionine sulfoximine: historical development and clinical issues
    • Bailey, H. H. 1998. L-S,R-Buthionine sulfoximine: historical development and clinical issues. Chem. Biol. Interact 111-112:239-254.
    • (1998) Chem. Biol. Interact , vol.111-112 , pp. 239-254
    • Bailey, H.H.1
  • 5
    • 0033766453 scopus 로고    scopus 로고
    • Replication of wild-type and mutant human cytomegalovirus in life-extended human diploid fibroblasts
    • Bresnahan, W. A., G. E. Hultman, and T. Shenk. 2000. Replication of wild-type and mutant human cytomegalovirus in life-extended human diploid fibroblasts. J. Virol. 74:10816-10818.
    • (2000) J. Virol. , vol.74 , pp. 10816-10818
    • Bresnahan, W.A.1    Hultman, G.E.2    Shenk, T.3
  • 6
    • 37349040367 scopus 로고    scopus 로고
    • Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly
    • Buchkovich, N. J., T. G. Maguire, A. W. Paton, J. C. Paton, and J. C. Alwine. 2008. Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly. J. Virol. 82:31-39.
    • (2008) J. Virol. , vol.82 , pp. 31-39
    • Buchkovich, N.J.1    Maguire, T.G.2    Paton, A.W.3    Paton, J.C.4    Alwine, J.C.5
  • 7
    • 40949116686 scopus 로고    scopus 로고
    • The TORrid affairs of viruses: effects of mammalian DNA viruses on the PI3KAkt-mTOR signaling pathway
    • Buchkovich, N. J., Y. Yu, C. A. Zampieri, and J. C. Alwine. 2008. The TORrid affairs of viruses: effects of mammalian DNA viruses on the PI3KAkt-mTOR signaling pathway. Nat. Rev. Microbiol. 6:265-275.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 265-275
    • Buchkovich, N.J.1    Yu, Y.2    Zampieri, C.A.3    Alwine, J.C.4
  • 8
    • 75449105003 scopus 로고    scopus 로고
    • Glutamine metabolism is essential for human cytomegalovirus infection
    • Chambers, J. W., T. G. Maguire, and J. C. Alwine. 2010. Glutamine metabolism is essential for human cytomegalovirus infection. J. Virol. 84:1867-1873.
    • (2010) J. Virol. , vol.84 , pp. 1867-1873
    • Chambers, J.W.1    Maguire, T.G.2    Alwine, J.C.3
  • 9
    • 21844468767 scopus 로고    scopus 로고
    • Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase
    • Chiang, G. G., and R. T. Abraham. 2005. Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase. J. Biol. Chem. 280:25485-25490.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25485-25490
    • Chiang, G.G.1    Abraham, R.T.2
  • 10
    • 0346995213 scopus 로고    scopus 로고
    • Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1
    • Child, S. J., M. Hakki, K. L. De Niro, and A. P. Geballe. 2004. Evasion of cellular antiviral responses by human cytomegalovirus TRS1 and IRS1. J. Virol. 78:197-205.
    • (2004) J. Virol. , vol.78 , pp. 197-205
    • Child, S.J.1    Hakki, M.2    De Niro, K.L.3    Geballe, A.P.4
  • 11
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu, M. L., and T. Aw. 2010. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic. Biol. Med. 48:749-762.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.2
  • 12
    • 79952844950 scopus 로고    scopus 로고
    • The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection
    • Clippinger, A. J., T. G. Maguire, and J. C. Alwine. 2011. The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection. J. Virol. 85:3930-3939.
    • (2011) J. Virol. , vol.85 , pp. 3930-3939
    • Clippinger, A.J.1    Maguire, T.G.2    Alwine, J.C.3
  • 13
    • 80052428184 scopus 로고    scopus 로고
    • Human cytomegalovirus infection maintains mTOR activity and its perinuclear localization during amino acid deprivation
    • Clippinger, A. J., T. G. Maguire, and J. C. Alwine. 2011. Human cytomegalovirus infection maintains mTOR activity and its perinuclear localization during amino acid deprivation. J. Virol. 85:9369-9376.
    • (2011) J. Virol. , vol.85 , pp. 9369-9376
    • Clippinger, A.J.1    Maguire, T.G.2    Alwine, J.C.3
  • 14
    • 62449266454 scopus 로고    scopus 로고
    • TORC-specific phosphorylation of mammalian target of rapamycin (mTOR): phospho-Ser 2481 is a marker for intact mTOR signaling complex 2
    • Copp, J., G. Manning, and T. Hunter. 2009. TORC-specific phosphorylation of mammalian target of rapamycin (mTOR): phospho-Ser 2481 is a marker for intact mTOR signaling complex 2. Cancer Res. 69:1821-1827.
    • (2009) Cancer Res , vol.69 , pp. 1821-1827
    • Copp, J.1    Manning, G.2    Hunter, T.3
  • 15
    • 29244462498 scopus 로고    scopus 로고
    • Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway
    • Cullinan, S. B., and J. A. Diehl. 2006. Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway. Int. J. Biochem. Cell Biol. 38:317-332.
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 317-332
    • Cullinan, S.B.1    Diehl, J.A.2
  • 16
    • 0141752795 scopus 로고    scopus 로고
    • Identification of Nrf2 as a novel PERK substrate and critical effector of PERK-dependent cell survival
    • Cullinan, S. B., et al. 2003. Identification of Nrf2 as a novel PERK substrate and critical effector of PERK-dependent cell survival. Mol. Cell. Biol. 23: 7198-7209.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7198-7209
    • Cullinan, S.B.1
  • 18
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel, T. 2003. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15:247-254.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 19
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel, T., and N. J. Holbrook. 2000. Oxidants, oxidative stress and the biology of ageing. Nature 408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 20
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Go, Y. M., and D. P. Jones. 2008. Redox compartmentalization in eukaryotic cells. Biochim. Biophys. Acta 1780:1273-1290.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 21
    • 77954509272 scopus 로고    scopus 로고
    • Redox control systems in the nucleus: mechanisms and functions
    • Go, Y. M., and D. P. Jones. 2010. Redox control systems in the nucleus: mechanisms and functions. Antioxid. Redox Signal. 13:489-509.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 489-509
    • Go, Y.M.1    Jones, D.P.2
  • 22
    • 42949139481 scopus 로고    scopus 로고
    • AMPK phosphorylation of raptor mediates a metabolic checkpoint
    • Gwinn, D. M., et al. 2008. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol. Cell 30:214-226.
    • (2008) Mol. Cell , vol.30 , pp. 214-226
    • Gwinn, D.M.1
  • 23
    • 33751224189 scopus 로고    scopus 로고
    • Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1
    • Hakki, M., E. E. Marshall, K. L. De Niro, and A. P. Geballe. 2006. Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1. J. Virol. 80:11817-11826.
    • (2006) J. Virol. , vol.80 , pp. 11817-11826
    • Hakki, M.1    Marshall, E.E.2    De Niro, K.L.3    Geballe, A.P.4
  • 24
    • 0031799930 scopus 로고    scopus 로고
    • Phosphorylation of the human cytomegalovirus 86-kilodalton immediate-early protein IE2
    • Harel, N. Y., and J. C. Alwine. 1998. Phosphorylation of the human cytomegalovirus 86-kilodalton immediate-early protein IE2. J. Virol. 72:5481-5492.
    • (1998) J. Virol. , vol.72 , pp. 5481-5492
    • Harel, N.Y.1    Alwine, J.C.2
  • 25
    • 0034697149 scopus 로고    scopus 로고
    • Antagonism between members of the CNC-bZIP family and the immediate-early protein IE2 of human cytomegalovirus
    • Huang, C.-F., et al. 2000. Antagonism between members of the CNC-bZIP family and the immediate-early protein IE2 of human cytomegalovirus. J. Biol. Chem. 275:12313-12320.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12313-12320
    • Huang, C.-F.1
  • 26
    • 40949158668 scopus 로고    scopus 로고
    • Production of infectious HCMV virions is inhibited by drugs that disrupt calcium homeostasis in the endoplasmic reticulum
    • Isler, J. A., T. G. Maguire, and J. C. Alwine. 2005. Production of infectious HCMV virions is inhibited by drugs that disrupt calcium homeostasis in the endoplasmic reticulum. J. Virol. 79:15338-15397.
    • (2005) J. Virol. , vol.79 , pp. 15338-15397
    • Isler, J.A.1    Maguire, T.G.2    Alwine, J.C.3
  • 27
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler, J. A., A. H. Skalet, and J. C. Alwine. 2005. Human cytomegalovirus infection activates and regulates the unfolded protein response. J. Virol. 79:6890-6899.
    • (2005) J. Virol. , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 28
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • Itoh, K., T. Ishii, N. Wakabayashi, and M. Yamamoto. 1999. Regulatory mechanisms of cellular response to oxidative stress. Free Radic. Res. 31: 319-324.
    • (1999) Free Radic. Res. , vol.31 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4
  • 29
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto, E., et al. 2004. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6:1122-1128.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1122-1128
    • Jacinto, E.1
  • 30
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrientsensitive complex that signals to the cell growth machinery
    • Kim, D. H., et al. 2002. mTOR interacts with raptor to form a nutrientsensitive complex that signals to the cell growth machinery. Cell 110:163-175.
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1
  • 31
    • 4644252994 scopus 로고    scopus 로고
    • Human cytomegalovirus infection induces rapamycin insensitive phosphorylation of downstream effectors of mTOR kinase
    • Kudchodkar, S., Y. Yu, T. Maguire, and J. C. Alwine. 2004. Human cytomegalovirus infection induces rapamycin insensitive phosphorylation of downstream effectors of mTOR kinase. J. Virol. 78:11030-11039.
    • (2004) J. Virol. , vol.78 , pp. 11030-11039
    • Kudchodkar, S.1    Yu, Y.2    Maguire, T.3    Alwine, J.C.4
  • 32
    • 33947403537 scopus 로고    scopus 로고
    • AMPK-mediated inhibition of mTOR kinase is circumvented during immediate-early times of human cytomegalovirus infection
    • Kudchodkar, S. B., G. Q. Del Prete, T. G. Maguire, and J. C. Alwine. 2007. AMPK-mediated inhibition of mTOR kinase is circumvented during immediate-early times of human cytomegalovirus infection. J. Virol. 81:3649-3651.
    • (2007) J. Virol. , vol.81 , pp. 3649-3651
    • Kudchodkar, S.B.1    Del Prete, G.Q.2    Maguire, T.G.3    Alwine, J.C.4
  • 33
    • 33749040235 scopus 로고    scopus 로고
    • Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor- and rictor-containing complexes
    • Kudchodkar, S. B., Y. Yu, T. G. Maguire, and J. C. Alwine. 2006. Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor- and rictor-containing complexes. Proc. Natl. Acad. Sci. U. S. A. 103:14182-14187.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14182-14187
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 34
    • 57649221592 scopus 로고    scopus 로고
    • Hypoxic reactive oxygen species regulate the integrated stress response and cell survival
    • Liu, L., D. R. Wise, J. A. Diehl, and M. C. Simon. 2008. Hypoxic reactive oxygen species regulate the integrated stress response and cell survival. J. Biol. Chem. 283:31153-31162.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31153-31162
    • Liu, L.1    Wise, D.R.2    Diehl, J.A.3    Simon, M.C.4
  • 36
    • 21244456553 scopus 로고    scopus 로고
    • Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency
    • Long, X., S. Ortiz-Vega, Y. Lin, and J. Avruch. 2005. Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency. J. Biol. Chem. 280:23433-23436.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23433-23436
    • Long, X.1    Ortiz-Vega, S.2    Lin, Y.3    Avruch, J.4
  • 38
    • 32644446560 scopus 로고    scopus 로고
    • Phosphorylation and dephosphorylation events that regulate viral mRNA translation
    • Mohr, I. 2006. Phosphorylation and dephosphorylation events that regulate viral mRNA translation. Virus Res. 119:89-99.
    • (2006) Virus Res , vol.119 , pp. 89-99
    • Mohr, I.1
  • 39
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman, N. J., et al. 2008. Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 3:1-10.
    • (2008) Cell Host Microbe , vol.3 , pp. 1-10
    • Moorman, N.J.1
  • 40
    • 33845970245 scopus 로고    scopus 로고
    • Dynamics of the cellular metabolome during human cytomegalovirus infection
    • Munger, J., S. U. Bajad, H. A. Coller, T. Shenk, and J. D. Rabinowitz. 2006. Dynamics of the cellular metabolome during human cytomegalovirus infection. PLoS Pathog. 2:1165-1175.
    • (2006) PLoS Pathog , vol.2 , pp. 1165-1175
    • Munger, J.1    Bajad, S.U.2    Coller, H.A.3    Shenk, T.4    Rabinowitz, J.D.5
  • 41
    • 53649110425 scopus 로고    scopus 로고
    • Systems-level metabolic flux profiling identifies fatty acid synthesis as a target for antiviral therapy
    • Munger, J., et al. 2008. Systems-level metabolic flux profiling identifies fatty acid synthesis as a target for antiviral therapy. Nat. Biotechnol. 26:1179-1186.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1179-1186
    • Munger, J.1
  • 43
    • 10744225986 scopus 로고    scopus 로고
    • Coding potential of laboratory and clinical strains of human cytomegalovirus
    • Murphy, E., et al. 2003. Coding potential of laboratory and clinical strains of human cytomegalovirus. Proc. Natl. Acad. Sci. U. S. A. 25:14976-14981.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.25 , pp. 14976-14981
    • Murphy, E.1
  • 44
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave, B. T., D. M. Ouwens, D. J. Withers, D. R. Alessi, and P. R. Shepherd. 1999. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 344:427-431.
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, D.M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 45
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling gene expression mediated by the antioxidant response element
    • Nguyen, T., P. Sherratt, and C. Pickett. 2003. Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annu. Rev. Pharmacol. Toxicol. 43:233-260.
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherratt, P.2    Pickett, C.3
  • 46
    • 33750044112 scopus 로고    scopus 로고
    • Stress and mTORture signaling
    • Reiling, J. H., and D. M. Sabatini. 2006. Stress and mTORture signaling. Oncogene 25:6373-6383.
    • (2006) Oncogene , vol.25 , pp. 6373-6383
    • Reiling, J.H.1    Sabatini, D.M.2
  • 48
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov, D. D., et al. 2004. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14:1296-1302.
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1
  • 50
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • Sekulic, A., et al. 2000. A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res. 60:3504-3513.
    • (2000) Cancer Res , vol.60 , pp. 3504-3513
    • Sekulic, A.1
  • 51
    • 0029806823 scopus 로고    scopus 로고
    • Role of reactive oxygen intermediates in cytomegalovirus gene expression and in the response of human smooth muscle cells to viral infection
    • Speir, E., T. Shibutani, Z. X. Yu, V. Ferrans, and S. E. Epstein. 1996. Role of reactive oxygen intermediates in cytomegalovirus gene expression and in the response of human smooth muscle cells to viral infection. Circ. Res. 79:1143-1152.
    • (1996) Circ. Res. , vol.79 , pp. 1143-1152
    • Speir, E.1    Shibutani, T.2    Yu, Z.X.3    Ferrans, V.4    Epstein, S.E.5
  • 52
    • 20744448501 scopus 로고    scopus 로고
    • Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells
    • Walsh, D., C. Perez, J. Notary, and I. Mohr. 2005. Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J. Virol. 79:8057-8064.
    • (2005) J. Virol. , vol.79 , pp. 8057-8064
    • Walsh, D.1    Perez, C.2    Notary, J.3    Mohr, I.4
  • 53
    • 64049088651 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death
    • Xuan, B., Z. Qian, E. Torigoi, and D. Yu. 2009. Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death. J. Virol. 83:3463-3474.
    • (2009) J. Virol. , vol.83 , pp. 3463-3474
    • Xuan, B.1    Qian, Z.2    Torigoi, E.3    Yu, D.4
  • 54
    • 0036200413 scopus 로고    scopus 로고
    • Human cytomegalovirus major immediateearly proteins and simian virus 40 large T antigen can inhibit apoptosis through activation of the phosphatidylinositide 3'-OH kinase pathway and cellular kinase Akt
    • Yu, Y., and J. C. Alwine. 2002. Human cytomegalovirus major immediateearly proteins and simian virus 40 large T antigen can inhibit apoptosis through activation of the phosphatidylinositide 3'-OH kinase pathway and cellular kinase Akt. J. Virol. 76:3731-3738.
    • (2002) J. Virol. , vol.76 , pp. 3731-3738
    • Yu, Y.1    Alwine, J.C.2
  • 55
    • 42449090225 scopus 로고    scopus 로고
    • Interaction between simian virus 40 large T antigen and insulin receptor substrate 1 is disrupted by the K1 mutation, resulting in the loss of large T antigen-mediated phosphorylation of Akt
    • Yu, Y., and J. C. Alwine. 2008. Interaction between simian virus 40 large T antigen and insulin receptor substrate 1 is disrupted by the K1 mutation, resulting in the loss of large T antigen-mediated phosphorylation of Akt. J. Virol. 82:4521-4526.
    • (2008) J. Virol. , vol.82 , pp. 4521-4526
    • Yu, Y.1    Alwine, J.C.2
  • 56
    • 77649272110 scopus 로고    scopus 로고
    • A systems biology perspective on Nrf2-mediated antioxidant response
    • Zhang, Q., J. Pi, C. G. Woods, and M. E. Andersen. 2010. A systems biology perspective on Nrf2-mediated antioxidant response. Toxicol. Appl. Pharmacol. 244:84-97.
    • (2010) Toxicol. Appl. Pharmacol. , vol.244 , pp. 84-97
    • Zhang, Q.1    Pi, J.2    Woods, C.G.3    Andersen, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.