메뉴 건너뛰기




Volumn 78, Issue 6, 2004, Pages 2984-2993

US11 of Herpes Simplex Virus Type 1 Interacts with HIPK2 and Antagonizes HIPK2-Induced Cell Growth Arrest

Author keywords

[No Author keywords available]

Indexed keywords

HOMEODOMAIN INTERACTING PROTEIN KINASE 2; PROTEIN KINASE; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 1542317686     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.6.2984-2993.2004     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 0029863923 scopus 로고    scopus 로고
    • In situ hybridization and immuno-electron microscope analyses of the Us11 gene of herpes simplex virus type 1 during transient expression
    • Besse, S., J.-J. Diaz, E. Pichard, K. Kindbeiter, J.-J. Madjar, and F. Puvion-Dutilleul. 1996. In situ hybridization and immuno-electron microscope analyses of the Us11 gene of herpes simplex virus type 1 during transient expression. Chromosoma 104:434-444.
    • (1996) Chromosoma , vol.104 , pp. 434-444
    • Besse, S.1    Diaz, J.-J.2    Pichard, E.3    Kindbeiter, K.4    Madjar, J.-J.5    Puvion-Dutilleul, F.6
  • 2
    • 0020803450 scopus 로고
    • Two small RNAs encoded by Epstein-Barr virus can functionally substitute for the virus-associated RNAs in the lytic growth of adenovirus 5
    • Bhat, R. A., and B. Thimmappaya. 1983. Two small RNAs encoded by Epstein-Barr virus can functionally substitute for the virus-associated RNAs in the lytic growth of adenovirus 5. Proc. Natl. Acad. Sci. USA 80:4789-4793.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4789-4793
    • Bhat, R.A.1    Thimmappaya, B.2
  • 3
    • 0023204711 scopus 로고
    • Three mutants of herpes simplex virus type 2: One lacking the genes Us10, Us11, Us12 and two in which Rs has been extended by 6 kb to 0, 91 map units with loss of Us sequences between 0, 94 and the Us/TRs junction
    • Brown, S. M., and J. Harland. 1987. Three mutants of herpes simplex virus type 2: one lacking the genes Us10, Us11, Us12 and two in which Rs has been extended by 6 kb to 0, 91 map units with loss of Us sequences between 0, 94 and the Us/TRs junction. J. Gen. Virol. 68:1-18.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1-18
    • Brown, S.M.1    Harland, J.2
  • 4
    • 0036168638 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain
    • Cassady, K. A., and M. Gross. 2002. The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain. J. Virol. 76:2029-2035.
    • (2002) J. Virol. , vol.76 , pp. 2029-2035
    • Cassady, K.A.1    Gross, M.2
  • 6
    • 0000782017 scopus 로고    scopus 로고
    • The homeodomain protein NK-3 recruits Groucho and a histone deacetylase complex to repress transcription
    • Choi, C. Y., Y. H. Kim, H. J. Kwon, and Y. Kim. 1999. The homeodomain protein NK-3 recruits Groucho and a histone deacetylase complex to repress transcription. J. Biol. Chem. 274:33194-33197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33194-33197
    • Choi, C.Y.1    Kim, Y.H.2    Kwon, H.J.3    Kim, Y.4
  • 7
    • 13344276604 scopus 로고    scopus 로고
    • Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein
    • Diaz, J.-J., M. Duc Dodon, N. Schaerer-Uthurralt, D. Simonin, K. Kindbeiter, L. Gazzolo, and J.-J. Madjar. 1996. Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein. Nature 379:273-277.
    • (1996) Nature , vol.379 , pp. 273-277
    • Diaz, J.-J.1    Duc Dodon, M.2    Schaerer-Uthurralt, N.3    Simonin, D.4    Kindbeiter, K.5    Gazzolo, L.6    Madjar, J.-J.7
  • 8
    • 0027481858 scopus 로고
    • The herpes simplex virus type 1 Us11 gene product is a phosphorylated protein found to be non-specifically associated with both ribosomal subunits
    • Diaz, J.-J., D. Simonin, T. Massé, P. Deviller, K. Kindbeiter, L. Denoroy, and J.-J. Madjar. 1993. The herpes simplex virus type 1 Us11 gene product is a phosphorylated protein found to be non-specifically associated with both ribosomal subunits. J. Gen. Virol. 74:397-406.
    • (1993) J. Gen. Virol. , vol.74 , pp. 397-406
    • Diaz, J.-J.1    Simonin, D.2    Massé, T.3    Deviller, P.4    Kindbeiter, K.5    Denoroy, L.6    Madjar, J.-J.7
  • 9
    • 0030767817 scopus 로고    scopus 로고
    • Herpes simplex virus Us11 protein enhances recovery of protein synthesis and survival in heat shock treated HeLa cells
    • Diaz-Latoud, C., J.-J. Diaz, N. Fabre-Jonca, K. Kindbeiter, J.-J. Madjar, and A.-P. Arrigo. 1997. Herpes simplex virus Us11 protein enhances recovery of protein synthesis and survival in heat shock treated HeLa cells. Cell Stress Chaperones 2:119-131.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 119-131
    • Diaz-Latoud, C.1    Diaz, J.-J.2    Fabre-Jonca, N.3    Kindbeiter, K.4    Madjar, J.-J.5    Arrigo, A.-P.6
  • 11
    • 0005541496 scopus 로고    scopus 로고
    • The herpes simplex virus 1 Us11 protein cooperates with suboptimal amounts of human immunodeficiency virus type 1 (HIV-1) Rev protein to rescue HIV-1 production
    • Duc Dodon, M., I. Mikaelian, A. Sergeant, and L. Gazzolo. 2000. The herpes simplex virus 1 Us11 protein cooperates with suboptimal amounts of human immunodeficiency virus type 1 (HIV-1) Rev protein to rescue HIV-1 production. Virology 270:43-53.
    • (2000) Virology , vol.270 , pp. 43-53
    • Duc Dodon, M.1    Mikaelian, I.2    Sergeant, A.3    Gazzolo, L.4
  • 12
    • 0037330454 scopus 로고    scopus 로고
    • The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML
    • Engelhardt, O. G., C. Boutell, A. Orr, E. Ullrich, O. Haller, and R. D. Everett. 2003. The homeodomain-interacting kinase PKM (HIPK-2) modifies ND10 through both its kinase domain and a SUMO-1 interaction motif and alters the posttranslational modification of PML. Exp. Cell Res. 283:36-50.
    • (2003) Exp. Cell Res. , vol.283 , pp. 36-50
    • Engelhardt, O.G.1    Boutell, C.2    Orr, A.3    Ullrich, E.4    Haller, O.5    Everett, R.D.6
  • 13
    • 0032783056 scopus 로고    scopus 로고
    • A surprising role for the proteasome in the regulation of herpesvirus infection
    • Everett, R. D. 1999. A surprising role for the proteasome in the regulation of herpesvirus infection. Trends Biochem. Sci. 24:293-295.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 293-295
    • Everett, R.D.1
  • 14
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R. D., P. Freemont, H. Saitoh, M. Dasso, A. Orr, M. Kathoria, and J. Parkinson. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 15
    • 0031732094 scopus 로고    scopus 로고
    • A computer program for aligning a cDNA sequence with a genomic DNA sequence
    • Florea, L., G. Hartzell, Z. Zhang, G. M. Rubin, and W. Miller. 1998. A computer program for aligning a cDNA sequence with a genomic DNA sequence. Genome Res. 8:967-974.
    • (1998) Genome Res. , vol.8 , pp. 967-974
    • Florea, L.1    Hartzell, G.2    Zhang, Z.3    Rubin, G.M.4    Miller, W.5
  • 16
    • 0016251762 scopus 로고
    • The phosphorylation of liver ribosomal proteins in vivo: Evidence that only a single small subunit protein (S6) is phosphorylated
    • Gressner, A. M., and I. G. Wool. 1974. The phosphorylation of liver ribosomal proteins in vivo: evidence that only a single small subunit protein (S6) is phosphorylated. J. Biol. Chem. 249:6917-6925.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6917-6925
    • Gressner, A.M.1    Wool, I.G.2
  • 17
    • 0034534759 scopus 로고    scopus 로고
    • Human homeodomain-interacting protein kinase-2 (HIPK2) is a member of the DYRK family of protein kinases and maps to chromosome 7q32-q34
    • Hofmann, T. G., A. Mincheva, P. Lichter, W. Droge, and M. Lienhard Schmitz. 2000. Human homeodomain-interacting protein kinase-2 (HIPK2) is a member of the DYRK family of protein kinases and maps to chromosome 7q32-q34. Biochimie 82:1123-1127.
    • (2000) Biochimie , vol.82 , pp. 1123-1127
    • Hofmann, T.G.1    Mincheva, A.2    Lichter, P.3    Droge, W.4    Lienhard Schmitz, M.5
  • 19
    • 0037200042 scopus 로고    scopus 로고
    • Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo
    • Kim, E. J., J. S. Park, and S. J. Um. 2002. Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo. J. Biol. Chem. 277:32020-320208.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32020-320208
    • Kim, E.J.1    Park, J.S.2    Um, S.J.3
  • 20
    • 0347790260 scopus 로고    scopus 로고
    • Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1
    • Kim, Y. H., C. Y. Choi, and Y. Kim. 1999. Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1. Proc. Natl. Acad. Sci. USA. 96:12350-12355.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12350-12355
    • Kim, Y.H.1    Choi, C.Y.2    Kim, Y.3
  • 21
    • 0345898928 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinases, a novel family of co-repressors for homeodomain transcription factors
    • Kim, Y. H., C. Y. Choi, S. J. Lee, M.A. Conti, and Y. Kim. 1998. Homeodomain-interacting protein kinases, a novel family of co-repressors for homeodomain transcription factors. J. Biol. Chem. 273:25875-25879.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25875-25879
    • Kim, Y.H.1    Choi, C.Y.2    Lee, S.J.3    Conti, M.A.4    Kim, Y.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0030878879 scopus 로고    scopus 로고
    • The herpes simplex virus 1 protein kinase US3 is required for protection from apoptosis induced by the virus
    • Leopardi, R., C. Van Sant, and B. Roizman. 1997. The herpes simplex virus 1 protein kinase US3 is required for protection from apoptosis induced by the virus. Proc. Natl. Acad. Sci. USA 94:7891-7896.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7891-7896
    • Leopardi, R.1    Van Sant, C.2    Roizman, B.3
  • 25
    • 0034703639 scopus 로고    scopus 로고
    • The serine/threonine kinase HIPK2 interacts with TRADD, but not with CD95 or TNF-R1 in 293T cells
    • Li, X., Y. Wang, K. M. Debatin, and H. Hug. 2000. The serine/threonine kinase HIPK2 interacts with TRADD, but not with CD95 or TNF-R1 in 293T cells. Biochem. Biophys. Res. Commun. 277:513-517.
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 513-517
    • Li, X.1    Wang, Y.2    Debatin, K.M.3    Hug, H.4
  • 26
    • 0030048573 scopus 로고    scopus 로고
    • Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures
    • Liptak, L. M., S. L. Uprichard, and D. M. Knipe. 1996. Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures. J. Virol. 70:1759-1767.
    • (1996) J. Virol. , vol.70 , pp. 1759-1767
    • Liptak, L.M.1    Uprichard, S.L.2    Knipe, D.M.3
  • 27
    • 0022504699 scopus 로고
    • Generation of an inverting herpes simplex virus 1 mutants lacking the L-S junction a sequences, an origin of DNA synthesis, and several genes including those specifying glycoprotein E and α 47 gene
    • Longnecker, R., and B. Roizman. 1986. Generation of an inverting herpes simplex virus 1 mutants lacking the L-S junction a sequences, an origin of DNA synthesis, and several genes including those specifying glycoprotein E and α 47 gene. J. Virol. 58:583-591.
    • (1986) J. Virol. , vol.58 , pp. 583-591
    • Longnecker, R.1    Roizman, B.2
  • 28
    • 0030954488 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 prereplicative sites are a heterogeneous population: Only a subset are likely to be precursors to replication compartments
    • Lukonis, C. J., J. Burkham, and S. K. Weller. 1997. Herpes simplex virus type 1 prereplicative sites are a heterogeneous population: only a subset are likely to be precursors to replication compartments. J. Virol. 71:4771-4781.
    • (1997) J. Virol. , vol.71 , pp. 4771-4781
    • Lukonis, C.J.1    Burkham, J.2    Weller, S.K.3
  • 29
    • 0030068159 scopus 로고    scopus 로고
    • Characterization of nuclear structures in cells infected with herpes simplex virus type 1 in the absence of viral DNA replication
    • Lukonis, C. J., and S. K. Weller. 1996. Characterization of nuclear structures in cells infected with herpes simplex virus type 1 in the absence of viral DNA replication. J. Virol. 70:1751-1758.
    • (1996) J. Virol. , vol.70 , pp. 1751-1758
    • Lukonis, C.J.1    Weller, S.K.2
  • 30
    • 0023176178 scopus 로고
    • The products of gene Us11 of herpes simplex virus type 1 are DNA-binding and localize to the nucleoli of infected cells
    • MacLean, C. A., F. J. Rixon, and H. S. Marsden. 1987. The products of gene Us11 of herpes simplex virus type 1 are DNA-binding and localize to the nucleoli of infected cells. J. Gen. Virol. 68:1921-1937.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1921-1937
    • MacLean, C.A.1    Rixon, F.J.2    Marsden, H.S.3
  • 32
    • 0033179146 scopus 로고    scopus 로고
    • Nuclear bodies: Multifaceted subdomains of the interchromatin space
    • Matera, A. G. 1999. Nuclear bodies: multifaceted subdomains of the interchromatin space. Trends Cell Biol. 9:302-309.
    • (1999) Trends Cell Biol. , vol.9 , pp. 302-309
    • Matera, A.G.1
  • 33
    • 0035174668 scopus 로고    scopus 로고
    • A new expression cloning strategy for isolation of substrate-specific kinases by using phosphorylation site-specific antibody
    • Matsuo, R., W. Ochiai, K. Nakashima, and T. Taga. 2001. A new expression cloning strategy for isolation of substrate-specific kinases by using phosphorylation site-specific antibody. J. Immunol. Methods 247:141-151.
    • (2001) J. Immunol. Methods , vol.247 , pp. 141-151
    • Matsuo, R.1    Ochiai, W.2    Nakashima, K.3    Taga, T.4
  • 34
    • 0037054549 scopus 로고    scopus 로고
    • Nuclear and cytoplasmic shuttling of TRADD induces apoptosis via different mechanisms
    • Morgan, M., J. Thorburn, P. P. Pandolfi, and A. Thorburn. 2002. Nuclear and cytoplasmic shuttling of TRADD induces apoptosis via different mechanisms. J. Cell Biol. 157:975-984.
    • (2002) J. Cell Biol. , vol.157 , pp. 975-984
    • Morgan, M.1    Thorburn, J.2    Pandolfi, P.P.3    Thorburn, A.4
  • 35
    • 0029953712 scopus 로고    scopus 로고
    • Green fluorescent protein as a marker for gene expression and subcellular localization in budding yeast
    • Niedenthal, R. K., L. Riles, M. Johnston, and J. H. Hegemann. 1996. Green fluorescent protein as a marker for gene expression and subcellular localization in budding yeast. Yeast 12:773-786.
    • (1996) Yeast , vol.12 , pp. 773-786
    • Niedenthal, R.K.1    Riles, L.2    Johnston, M.3    Hegemann, J.H.4
  • 36
    • 0027185485 scopus 로고
    • The US 9, 10, 11, and 12 genes of herpes simplex virus type 1 are of no importance for its neurovirulence and latency in mice
    • Nishiyama, Y., R. Kurachi, T. Daikoku, and K. Umene. 1993. The US 9, 10, 11, and 12 genes of herpes simplex virus type 1 are of no importance for its neurovirulence and latency in mice. Virology 194:419-423.
    • (1993) Virology , vol.194 , pp. 419-423
    • Nishiyama, Y.1    Kurachi, R.2    Daikoku, T.3    Umene, K.4
  • 37
    • 0036839211 scopus 로고    scopus 로고
    • Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein
    • Peters, G. A., D. Khoo, I. Mohr, and G. C. Sen. 2002. Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein. J. Virol. 76:11054-11064.
    • (2002) J. Virol. , vol.76 , pp. 11054-11064
    • Peters, G.A.1    Khoo, D.2    Mohr, I.3    Sen, G.C.4
  • 39
    • 0023352165 scopus 로고
    • Localization of viral-specific 21kDa protein in nucleoli of herpes simplex infected cells
    • Puvion-Dutilleul, F. 1987. Localization of viral-specific 21kDa protein in nucleoli of herpes simplex infected cells. Eur. J. Cell Biol. 43:487-498.
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 487-498
    • Puvion-Dutilleul, F.1
  • 40
    • 0021233256 scopus 로고
    • The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication
    • Quinlan, M. P., L. B. Chen, and D. M. Knipe. 1984. The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication. Cell 36:857-868.
    • (1984) Cell , vol.36 , pp. 857-868
    • Quinlan, M.P.1    Chen, L.B.2    Knipe, D.M.3
  • 41
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 42
    • 0029878581 scopus 로고    scopus 로고
    • Structure and function in the herpes simplex virus 1 RNA-binding protein Us11: Mapping of the domain required for ribosomal and nucleolar association and RNA binding in vitro
    • Roller, R. J., L. L. Monk, D. Stuart, and B. Roizman. 1996. Structure and function in the herpes simplex virus 1 RNA-binding protein Us11: mapping of the domain required for ribosomal and nucleolar association and RNA binding in vitro. J. Virol. 70:2842-2851.
    • (1996) J. Virol. , vol.70 , pp. 2842-2851
    • Roller, R.J.1    Monk, L.L.2    Stuart, D.3    Roizman, B.4
  • 43
    • 0026719341 scopus 로고
    • The herpes simplex virus 1 RNA binding protein Us11 is a virion component and associates with ribosomal 60S subunits
    • Roller, R. J., and B. Roizman. 1992. The herpes simplex virus 1 RNA binding protein Us11 is a virion component and associates with ribosomal 60S subunits. J. Virol. 66:3624-3632.
    • (1992) J. Virol. , vol.66 , pp. 3624-3632
    • Roller, R.J.1    Roizman, B.2
  • 44
    • 0023288548 scopus 로고
    • Splicing of messenger RNA precursors
    • Sharp, P. A. 1987. Splicing of messenger RNA precursors. Science 235:766-771.
    • (1987) Science , vol.235 , pp. 766-771
    • Sharp, P.A.1
  • 45
    • 0029157725 scopus 로고
    • Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression
    • Simonin, D., J.-J. Diaz, K. Kindbeiter, P. Pernas, and J.-J. Madjar. 1995. Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression. Electrophoresis 16:1317-1322.
    • (1995) Electrophoresis , vol.16 , pp. 1317-1322
    • Simonin, D.1    Diaz, J.-J.2    Kindbeiter, K.3    Pernas, P.4    Madjar, J.-J.5
  • 47
    • 0034629471 scopus 로고    scopus 로고
    • Characterization of a novel serine/threonine kinase associated with nuclear bodies
    • Trost, M., G. Kochs, and O. Haller. 2000. Characterization of a novel serine/threonine kinase associated with nuclear bodies. J. Biol. Chem. 275: 7373-7377.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7373-7377
    • Trost, M.1    Kochs, G.2    Haller, O.3
  • 48
    • 0029099409 scopus 로고
    • Ras-Raf interaction: Two-hybrid analysis
    • Vojtek, A. B., and S. M. Hollenberg. 1995. Ras-Raf interaction: two-hybrid analysis. Methods Enzymol. 255:331-342.
    • (1995) Methods Enzymol. , vol.255 , pp. 331-342
    • Vojtek, A.B.1    Hollenberg, S.M.2
  • 49
    • 0034633528 scopus 로고    scopus 로고
    • Identification and cloning of a CD43-associated serine/threonine kinase
    • Wang, W., V. Link, and J. M. Green. 2000. Identification and cloning of a CD43-associated serine/threonine kinase. Cell. Immunol. 205:34-39.
    • (2000) Cell. Immunol. , vol.205 , pp. 34-39
    • Wang, W.1    Link, V.2    Green, J.M.3
  • 50
    • 2542500783 scopus 로고    scopus 로고
    • HIPK2 overexpression leads to stabilization of p53 protein and increased p53 transcriptional activity by decreasing Mdm2 protein levels
    • Wang, Y., K. M. Debatin, and H. Hug. 2001. HIPK2 overexpression leads to stabilization of p53 protein and increased p53 transcriptional activity by decreasing Mdm2 protein levels. BMC Mol. Biol. 2:8.
    • (2001) BMC Mol. Biol. , vol.2 , pp. 8
    • Wang, Y.1    Debatin, K.M.2    Hug, H.3
  • 52
    • 0028131153 scopus 로고
    • Herpes simplex genes: The blueprint of a successful human pathogen
    • Ward, P. L., and B. Roizman. 1994. Herpes simplex genes: the blueprint of a successful human pathogen. Trends Genet. 10:267-274.
    • (1994) Trends Genet. , vol.10 , pp. 267-274
    • Ward, P.L.1    Roizman, B.2
  • 53
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M. 1994. The structure and function of proline-rich regions in proteins. Biochem. J. 297:249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.