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Volumn 85, Issue 15, 2011, Pages 7555-7562

Adenovirus sequesters phosphorylated STAT1 at viral replication centers and inhibits STAT dephosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; COGNATE PROTEIN TYROSINE PHOSPHATASE TC45; PROTEIN TYROSINE PHOSPHATASE; STAT1 PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 79960420849     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00513-11     Document Type: Article
Times cited : (30)

References (50)
  • 1
    • 0025882889 scopus 로고
    • Inhibition of the cellular response to interferons by products of the adenovirus type 5 E1A oncogene
    • Ackrill, A. M., et al. 1991. Inhibition of the cellular response to interferons by products of the adenovirus type 5 E1A oncogene. Nucleic Acids Res. 19:4387-4393.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4387-4393
    • Ackrill, A.M.1
  • 2
    • 0023106727 scopus 로고
    • Adenovirus early region 1A modulation of interferon antiviral activity
    • Anderson, K. P., and E. H. Fennie. 1987. Adenovirus early region 1A modulation of interferon antiviral activity. J. Virol. 61:787-795.
    • (1987) J. Virol. , vol.61 , pp. 787-795
    • Anderson, K.P.1    Fennie, E.H.2
  • 3
    • 23844438197 scopus 로고    scopus 로고
    • Adenovirus type 5 E4orf3 protein targets the Mre11 complex to cytoplasmic aggresomes
    • Araujo, F. D., T. H. Stracker, C. T. Carson, D. V. Lee, and M. D. Weitzman. 2005. Adenovirus type 5 E4orf3 protein targets the Mre11 complex to cytoplasmic aggresomes. J. Virol. 79:11382-11391.
    • (2005) J. Virol. , vol.79 , pp. 11382-11391
    • Araujo, F.D.1    Stracker, T.H.2    Carson, C.T.3    Lee, D.V.4    Weitzman, M.D.5
  • 4
    • 0029100611 scopus 로고
    • Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies
    • Carvalho, T., et al. 1995. Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies. J. Cell Biol. 131:45-56.
    • (1995) J. Cell Biol. , vol.131 , pp. 45-56
    • Carvalho, T.1
  • 5
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • Doucas, V., et al. 1996. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10:196-207.
    • (1996) Genes Dev , vol.10 , pp. 196-207
    • Doucas, V.1
  • 6
    • 18144401244 scopus 로고    scopus 로고
    • Relocalization of the Mre11-Rad50-Nbs1 complex by the adenovirus E4 ORF3 protein is required for viral replication
    • Evans, J. D., and P. Hearing. 2005. Relocalization of the Mre11-Rad50-Nbs1 complex by the adenovirus E4 ORF3 protein is required for viral replication. J. Virol. 79:6207-6215.
    • (2005) J. Virol. , vol.79 , pp. 6207-6215
    • Evans, J.D.1    Hearing, P.2
  • 7
    • 2942615015 scopus 로고    scopus 로고
    • Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function
    • Flowers, L. O., et al. 2004. Characterization of a peptide inhibitor of Janus kinase 2 that mimics suppressor of cytokine signaling 1 function. J. Immunol. 172:7510-7518.
    • (2004) J. Immunol. , vol.172 , pp. 7510-7518
    • Flowers, L.O.1
  • 8
    • 0019996915 scopus 로고
    • Enhanced expression of adenovirus transforming proteins
    • Gaynor, R. B., A. Tsukamoto, C. Montell, and A. J. Berk. 1982. Enhanced expression of adenovirus transforming proteins. J. Virol. 44:276-285.
    • (1982) J. Virol. , vol.44 , pp. 276-285
    • Gaynor, R.B.1    Tsukamoto, A.2    Montell, C.3    Berk, A.J.4
  • 9
    • 0025774036 scopus 로고
    • Repression of the interferon signal transduction pathway by the adenovirus E1A oncogene
    • Gutch, M. J., and N. C. Reich. 1991. Repression of the interferon signal transduction pathway by the adenovirus E1A oncogene. Proc. Natl. Acad. Sci. U. S. A. 88:7913-7917.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7913-7917
    • Gutch, M.J.1    Reich, N.C.2
  • 10
    • 0025359592 scopus 로고
    • The adenovirus L4 100-kilodalton protein is necessary for efficient translation of viral late mRNA species
    • Hayes, B. W., G. C. Telling, M. M. Myat, J. F. Williams, and S. J. Flint. 1990. The adenovirus L4 100-kilodalton protein is necessary for efficient translation of viral late mRNA species. J. Virol. 64:2732-2742.
    • (1990) J. Virol. , vol.64 , pp. 2732-2742
    • Hayes, B.W.1    Telling, G.C.2    Myat, M.M.3    Williams, J.F.4    Flint, S.J.5
  • 11
    • 0015607334 scopus 로고
    • Synthesis of type 2 adenovirus DNA in the presence of cycloheximide
    • Horwitz, M., C. Brayton, and S. Baum. 1973. Synthesis of type 2 adenovirus DNA in the presence of cycloheximide. J. Virol. 11:544-551.
    • (1973) J. Virol. , vol.11 , pp. 544-551
    • Horwitz, M.1    Brayton, C.2    Baum, S.3
  • 12
    • 0017870263 scopus 로고
    • Isolation of deletion and substitution mutants of adenovirus type 5
    • Jones, N., and T. Shenk. 1978. Isolation of deletion and substitution mutants of adenovirus type 5. Cell 13:181-188.
    • (1978) Cell , vol.13 , pp. 181-188
    • Jones, N.1    Shenk, T.2
  • 13
    • 0025874550 scopus 로고
    • Inhibition of interferon-inducible gene expression by adenovirus E1A proteins: block in transcriptional complex formation
    • Kalvakolanu, D. V., S. K. Bandyopadhyay, M. L. Harter, and G. C. Sen. 1991. Inhibition of interferon-inducible gene expression by adenovirus E1A proteins: block in transcriptional complex formation. Proc. Natl. Acad. Sci. U. S. A. 88:7459-7463.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7459-7463
    • Kalvakolanu, D.V.1    Bandyopadhyay, S.K.2    Harter, M.L.3    Sen, G.C.4
  • 14
    • 0000413462 scopus 로고    scopus 로고
    • Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
    • Kim, T., and T. Maniatis. 1996. Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273:1717-1719.
    • (1996) Science , vol.273 , pp. 1717-1719
    • Kim, T.1    Maniatis, T.2
  • 15
    • 0022447264 scopus 로고
    • Adenovirus VAI RNA antagonizes the antiviral action of interferon by preventing activation of the interferon-induced eIF-2 [alpha] kinase
    • Kitajewski, J., et al. 1986. Adenovirus VAI RNA antagonizes the antiviral action of interferon by preventing activation of the interferon-induced eIF-2 [alpha] kinase. Cell 45:195-200.
    • (1986) Cell , vol.45 , pp. 195-200
    • Kitajewski, J.1
  • 16
    • 58849139353 scopus 로고    scopus 로고
    • A phosphorylation-acetylation switch regulates STAT1 signaling
    • Krämer, O., et al. 2009. A phosphorylation-acetylation switch regulates STAT1 signaling. Genes Dev. 23:223-235.
    • (2009) Genes Dev , vol.23 , pp. 223-235
    • Krämer, O.1
  • 17
    • 0030851840 scopus 로고    scopus 로고
    • Regulation of interferon-responsiveness by the duration of Janus kinase activity
    • Lee, C., H. Bluyssen, and D. Levy. 1997. Regulation of interferon-responsiveness by the duration of Janus kinase activity. J. Biol. Chem. 272:21872-21877.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21872-21877
    • Lee, C.1    Bluyssen, H.2    Levy, D.3
  • 18
    • 0030273782 scopus 로고    scopus 로고
    • Effects of adenovirus E1A protein on interferon-signaling
    • Leonard, G. T., and G. C. Sen. 1996. Effects of adenovirus E1A protein on interferon-signaling. Virology 224:25-33.
    • (1996) Virology , vol.224 , pp. 25-33
    • Leonard, G.T.1    Sen, G.C.2
  • 19
    • 0032169599 scopus 로고    scopus 로고
    • Inhibition of Stat1-mediated gene activation by PIAS1
    • Liu, B., et al. 1998. Inhibition of Stat1-mediated gene activation by PIAS1. Proc. Natl. Acad. Sci. U. S. A. 95:10626-10631.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 10626-10631
    • Liu, B.1
  • 20
    • 0032432076 scopus 로고    scopus 로고
    • Direct suppression of Stat1 function during adenoviral infection
    • Look, D., et al. 1998. Direct suppression of Stat1 function during adenoviral infection. Immunity 9:871-880.
    • (1998) Immunity , vol.9 , pp. 871-880
    • Look, D.1
  • 21
    • 45749157223 scopus 로고    scopus 로고
    • RUNX1 permits E4orf6-directed nuclear localization of the adenovirus E1B-55K protein and associates with centers of viral DNA and RNA synthesis
    • Marshall, L. J., et al. 2008. RUNX1 permits E4orf6-directed nuclear localization of the adenovirus E1B-55K protein and associates with centers of viral DNA and RNA synthesis. J. Virol. 82:6395-6408.
    • (2008) J. Virol. , vol.82 , pp. 6395-6408
    • Marshall, L.J.1
  • 22
    • 0034669111 scopus 로고    scopus 로고
    • Nuclear export signal located within the DNA-binding domain of the STAT1 transcription factor
    • McBride, K., C. McDonald, and N. Reich. 2000. Nuclear export signal located within the DNA-binding domain of the STAT1 transcription factor. EMBO J. 19:6196-6206.
    • (2000) EMBO J , vol.19 , pp. 6196-6206
    • McBride, K.1    McDonald, C.2    Reich, N.3
  • 23
    • 33845718240 scopus 로고    scopus 로고
    • Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain
    • Mertens, C., et al. 2006. Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain. Genes Dev. 20:3372-3381.
    • (2006) Genes Dev , vol.20 , pp. 3372-3381
    • Mertens, C.1
  • 24
    • 0035831040 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 modulates IFN [alpha]/[beta]-induced transcription
    • Mowen, K., et al. 2001. Arginine methylation of STAT1 modulates IFN [alpha]/[beta]-induced transcription. Cell 104:731-741.
    • (2001) Cell , vol.104 , pp. 731-741
    • Mowen, K.1
  • 25
    • 0033201446 scopus 로고    scopus 로고
    • p48 (ISGF-3) is involved in interferon-induced suppression of hepatitis B virus enhancer-1 activity
    • Nakao, K., et al. 1999. p48 (ISGF-3) is involved in interferon-induced suppression of hepatitis B virus enhancer-1 activity. J. Biol. Chem. 274:28075-28078.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28075-28078
    • Nakao, K.1
  • 26
    • 66149151694 scopus 로고    scopus 로고
    • Adenovirus induction of IRF3 occurs through a binary trigger targeting Jun N-terminal kinase and TBK1 kinase cascades and type I interferon autocrine signaling
    • Nociari, M., O. Ocheretina, M. Murphy, and E. Falck-Pedersen. 2009. Adenovirus induction of IRF3 occurs through a binary trigger targeting Jun N-terminal kinase and TBK1 kinase cascades and type I interferon autocrine signaling. J. Virol. 83:4081-4091.
    • (2009) J. Virol. , vol.83 , pp. 4081-4091
    • Nociari, M.1    Ocheretina, O.2    Murphy, M.3    Falck-Pedersen, E.4
  • 27
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • Platanias, L. 2005. Mechanisms of type-I- and type-II-interferon-mediated signalling. Nat. Rev. Immunol. 5:375-386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.1
  • 28
    • 0028092203 scopus 로고
    • Adenovirus replication and transcription sites are spatially separated in the nucleus of infected cells
    • Pombo, A., J. Ferreira, E. Bridge, and M. Carmo-Fonseca. 1994. Adenovirus replication and transcription sites are spatially separated in the nucleus of infected cells. EMBO J. 13:5075-5085.
    • (1994) EMBO J , vol.13 , pp. 5075-5085
    • Pombo, A.1    Ferreira, J.2    Bridge, E.3    Carmo-Fonseca, M.4
  • 29
    • 36348940608 scopus 로고    scopus 로고
    • Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures
    • Randall, R. E., and S. Goodbourn. 2008. Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures. J. Gen. Virol. 89:1-47.
    • (2008) J. Gen. Virol. , vol.89 , pp. 1-47
    • Randall, R.E.1    Goodbourn, S.2
  • 30
    • 0035793624 scopus 로고    scopus 로고
    • Lack of a role of the interferonstimulated response element-like region in interferon-induced suppression of hepatitis B virus in vitro
    • Rang, A., T. Heise, and H. Will. 2001. Lack of a role of the interferonstimulated response element-like region in interferon-induced suppression of hepatitis B virus in vitro. J. Biol. Chem. 276:3531-3535.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3531-3535
    • Rang, A.1    Heise, T.2    Will, H.3
  • 31
    • 0023883901 scopus 로고
    • Transcription of interferon-stimulated genes is induced by adenovirus particles but is suppressed by E1A gene products
    • Reich, N., R. Pine, D. Levy, and J. E. Darnell, Jr. 1988. Transcription of interferon-stimulated genes is induced by adenovirus particles but is suppressed by E1A gene products. J. Virol. 62:114-119.
    • (1988) J. Virol. , vol.62 , pp. 114-119
    • Reich, N.1    Pine, R.2    Levy, D.3    Darnell Jr., J.E.4
  • 32
    • 0041529514 scopus 로고    scopus 로고
    • SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation
    • Rogers, R. S., C. M. Horvath, and M. J. Matunis. 2003. SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation. J. Biol. Chem. 278:30091-30097.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30091-30097
    • Rogers, R.S.1    Horvath, C.M.2    Matunis, M.J.3
  • 33
    • 0034954729 scopus 로고    scopus 로고
    • Functional analysis of adenovirus protein IX identifies domains involved in capsid stability, transcriptional activity, and nuclear reorganization
    • Rosa-Calatrava, M., L. Grave, F. Puvion-Dutilleul, B. Chatton, and C. Kedinger. 2001. Functional analysis of adenovirus protein IX identifies domains involved in capsid stability, transcriptional activity, and nuclear reorganization. J. Virol. 75:7131-7141.
    • (2001) J. Virol. , vol.75 , pp. 7131-7141
    • Rosa-Calatrava, M.1    Grave, L.2    Puvion-Dutilleul, F.3    Chatton, B.4    Kedinger, C.5
  • 34
    • 0242439337 scopus 로고    scopus 로고
    • Adenovirus protein IX sequesters host-cell promyelocytic leukaemia protein and contributes to efficient viral proliferation
    • Rosa-Calatrava, M., F. Puvion-Dutilleul, P. Lutz, and D. Dreyer. 2003. Adenovirus protein IX sequesters host-cell promyelocytic leukaemia protein and contributes to efficient viral proliferation. EMBO Rep. 4:969-975.
    • (2003) EMBO Rep , vol.4 , pp. 969-975
    • Rosa-Calatrava, M.1    Puvion-Dutilleul, F.2    Lutz, P.3    Dreyer, D.4
  • 35
    • 0030032903 scopus 로고    scopus 로고
    • Inhibition of IFN-stimulated gene expression and IFN induction of cytolytic resistance to natural killer cell lysis correlate with E1A-p300 binding
    • Routes, J. M., H. Li, S. T. Bayley, S. Ryan, and D. J. Klemm. 1996. Inhibition of IFN-stimulated gene expression and IFN induction of cytolytic resistance to natural killer cell lysis correlate with E1A-p300 binding. J. Immunol. 156:1055-1061.
    • (1996) J. Immunol. , vol.156 , pp. 1055-1061
    • Routes, J.M.1    Li, H.2    Bayley, S.T.3    Ryan, S.4    Klemm, D.J.5
  • 36
    • 0037141146 scopus 로고    scopus 로고
    • Modulation of human immunodeficiency virus 1 replication by interferon regulatory factors
    • Sgarbanti, M., et al. 2002. Modulation of human immunodeficiency virus 1 replication by interferon regulatory factors. J. Exp. Med. 195:1359-1370.
    • (2002) J. Exp. Med. , vol.195 , pp. 1359-1370
    • Sgarbanti, M.1
  • 37
    • 36749029351 scopus 로고    scopus 로고
    • Inhibition of Jak1-dependent signal transduction in airway epithelial cells infected with adenovirus
    • Shi, L., M. Ramaswamy, L. Manzel, and D. Look. 2007. Inhibition of Jak1-dependent signal transduction in airway epithelial cells infected with adenovirus. Am. J. Respir. Cell Mol. Biol. 37:720-728.
    • (2007) Am. J. Respir. Cell Mol. Biol. , vol.37 , pp. 720-728
    • Shi, L.1    Ramaswamy, M.2    Manzel, L.3    Look, D.4
  • 38
    • 0027090310 scopus 로고
    • Activation of transcription by IFN-gamma: tyrosine phosphorylation of a 91-kD DNA binding protein
    • Shuai, K., C. Schindler, V. Prezioso, and J. Darnell, Jr. 1992. Activation of transcription by IFN-gamma: tyrosine phosphorylation of a 91-kD DNA binding protein. Science 258:1808-1812.
    • (1992) Science , vol.258 , pp. 1808-1812
    • Shuai, K.1    Schindler, C.2    Prezioso, V.3    Darnell Jr., J.4
  • 39
    • 0037087117 scopus 로고    scopus 로고
    • Adenovirus infection targets the cellular protein kinase CK2 and RNA activated protein kinase (PKR) into viral inclusions of the cell nucleus
    • Souquere Besse, et al. 2002. Adenovirus infection targets the cellular protein kinase CK2 and RNA activated protein kinase (PKR) into viral inclusions of the cell nucleus. Microsc. Res. Tech. 56:465-478.
    • (2002) Microsc. Res. Tech. , vol.56 , pp. 465-478
    • Besse, S.1
  • 40
    • 0037130170 scopus 로고    scopus 로고
    • Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex
    • Stracker, T. H., C. T. Carson, and M. D. Weitzman. 2002. Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex. Nature 418:348-352.
    • (2002) Nature , vol.418 , pp. 348-352
    • Stracker, T.H.1    Carson, C.T.2    Weitzman, M.D.3
  • 41
    • 0036318564 scopus 로고    scopus 로고
    • Identification of a nuclear Stat1 protein tyrosine phosphatase
    • Ten Hoeve, et al. 2002. Identification of a nuclear Stat1 protein tyrosine phosphatase. Mol. Cell. Biol. 22:5662-5668.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5662-5668
    • Hoeve, T.1
  • 42
    • 0032825452 scopus 로고    scopus 로고
    • Estimating transcription factor bindability on DNA
    • Tsunoda, T., and T. Takagi. 1999. Estimating transcription factor bindability on DNA. Bioinformatics 15:622-630.
    • (1999) Bioinformatics , vol.15 , pp. 622-630
    • Tsunoda, T.1    Takagi, T.2
  • 43
    • 34247562651 scopus 로고    scopus 로고
    • Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral response
    • Ullman, A. J., N. C. Reich, and P. Hearing. 2007. Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral response. J. Virol. 81:4744-4752.
    • (2007) J. Virol. , vol.81 , pp. 4744-4752
    • Ullman, A.J.1    Reich, N.C.2    Hearing, P.3
  • 44
    • 22044431593 scopus 로고    scopus 로고
    • SUMO-1 conjugation selectively modulates STAT1-mediated gene responses
    • Ungureanu, D., S. Vanhatupa, J. Gronholm, J. J. Palvimo, and O. Silvennoinen. 2005. SUMO-1 conjugation selectively modulates STAT1-mediated gene responses. Blood 106:224-226.
    • (2005) Blood , vol.106 , pp. 224-226
    • Ungureanu, D.1    Vanhatupa, S.2    Gronholm, J.3    Palvimo, J.J.4    Silvennoinen, O.5
  • 45
    • 0142152429 scopus 로고    scopus 로고
    • PIAS proteins promote SUMO-1 conjugation to STAT1
    • Ungureanu, D., et al. 2003. PIAS proteins promote SUMO-1 conjugation to STAT1. Blood 102:3311-3313.
    • (2003) Blood , vol.102 , pp. 3311-3313
    • Ungureanu, D.1
  • 46
    • 4744363325 scopus 로고    scopus 로고
    • SOCS-1 localizes to the microtubule organizing complex-associated 20S proteasome
    • Vuong, B. Q., et al. 2004. SOCS-1 localizes to the microtubule organizing complex-associated 20S proteasome. Mol. Cell. Biol. 24:9092-9101.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9092-9101
    • Vuong, B.Q.1
  • 47
    • 0029117304 scopus 로고
    • Maximal activation of transcription by Statl and Stat3 requires both tyrosine and serine phosphorylation
    • Wen, Z., Z. Zhong, and J. E. Darnell. 1995. Maximal activation of transcription by Statl and Stat3 requires both tyrosine and serine phosphorylation. Cell 82:241-250.
    • (1995) Cell , vol.82 , pp. 241-250
    • Wen, Z.1    Zhong, Z.2    Darnell, J.E.3
  • 48
    • 0037033046 scopus 로고    scopus 로고
    • SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei
    • Wu, T., et al. 2002. SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei. J. Biol. Chem. 277:47572-47580.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47572-47580
    • Wu, T.1
  • 49
    • 0037177212 scopus 로고    scopus 로고
    • Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant
    • Xie, L., Y. Zhang, and Z. Zhang. 2002. Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant. Biochemistry 41:4032-4039.
    • (2002) Biochemistry , vol.41 , pp. 4032-4039
    • Xie, L.1    Zhang, Y.2    Zhang, Z.3
  • 50
    • 0036033161 scopus 로고    scopus 로고
    • The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation
    • Yamamoto, T., et al. 2002. The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation. Biochem. Biophys. Res. Commun. 297:811-817.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 811-817
    • Yamamoto, T.1


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