메뉴 건너뛰기




Volumn 79, Issue 2, 2006, Pages 388-396

Cyclin T1 but not cyclin T2a is induced by a post-transcriptional mechanism in PAMP-activated monocyte-derived macrophages

Author keywords

Cdk9; HIV Tat; P TEFb; Proteasome; Transcription

Indexed keywords

CYCLIN T1; CYCLIN T2; CYCLINE; LIPOPOLYSACCHARIDE; MESSENGER RNA; POSITIVE TRANSCRIPTION ELONGATION FACTOR B; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN SUBUNIT; SMALL NUCLEAR RNA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR 7SK; TRANSCRIPTION FACTOR HEXIM1; CCNT1 PROTEIN, HUMAN; CCNT2 PROTEIN, HUMAN; HEXIM1 PROTEIN, HUMAN; PEPTIDOGLYCAN; RNA BINDING PROTEIN;

EID: 33646453260     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.0805429     Document Type: Article
Times cited : (27)

References (50)
  • 1
    • 0015044657 scopus 로고
    • Transformation of granulocytes to macrophages in bone marrow colonies in vitro
    • Metcalf, D. (1971) Transformation of granulocytes to macrophages in bone marrow colonies in vitro. J. Cell. Physiol. 77, 277-280.
    • (1971) J. Cell. Physiol. , vol.77 , pp. 277-280
    • Metcalf, D.1
  • 2
    • 0024486273 scopus 로고
    • Origin and turnover of monocytes and macrophages
    • van Furth, R. (1989) Origin and turnover of monocytes and macrophages. Curr. Top. Pathol. 79, 125-150.
    • (1989) Curr. Top. Pathol. , vol.79 , pp. 125-150
    • Van Furth, R.1
  • 3
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signaling
    • Akira, S., Takeda, K. (2004) Toll-like receptor signaling. Nat. Rev. Immunol. 4, 499-511.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 6
    • 0030021084 scopus 로고    scopus 로고
    • Leishmania promastigotes selectively inhibit interleukin 12 induction in bone marrow-derived macrophages from susceptible and resistant mice
    • Carrera, L., Gazzinelli, R. T., Badolato, R., Hieny, S., Muller, W., Kuhn, R., Sacks, D. L. (1996) Leishmania promastigotes selectively inhibit interleukin 12 induction in bone marrow-derived macrophages from susceptible and resistant mice. J. Exp. Med. 183, 515-526.
    • (1996) J. Exp. Med. , vol.183 , pp. 515-526
    • Carrera, L.1    Gazzinelli, R.T.2    Badolato, R.3    Hieny, S.4    Muller, W.5    Kuhn, R.6    Sacks, D.L.7
  • 7
    • 0035140483 scopus 로고    scopus 로고
    • Evasion of host cell defense mechanisms by pathogenic bacteria
    • Pieters, J. (2001) Evasion of host cell defense mechanisms by pathogenic bacteria. Curr. Opin. Immunol. 13, 37-44.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 37-44
    • Pieters, J.1
  • 9
    • 0025342694 scopus 로고
    • HIV-1 entry into quiescent primary lymphocytes: Molecular analysis reveals a labile, latent viral structure
    • Zack, J. A., Arrigo, S. J., Weitsman, S. R., Go, A. S., Haislip, A., Chen, I. S. (1990) HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure. Cell 61, 213-222.
    • (1990) Cell , vol.61 , pp. 213-222
    • Zack, J.A.1    Arrigo, S.J.2    Weitsman, S.R.3    Go, A.S.4    Haislip, A.5    Chen, I.S.6
  • 10
    • 0025238945 scopus 로고
    • HIV-1 replication is controlled at the level of T cell activation and proviral integration
    • Stevenson, M., Stanwick, T. L., Dempsey, M. P., Lamonica, C. A. (1990) HIV-1 replication is controlled at the level of T cell activation and proviral integration. EMBO J. 9, 1551-1560.
    • (1990) EMBO J. , vol.9 , pp. 1551-1560
    • Stevenson, M.1    Stanwick, T.L.2    Dempsey, M.P.3    Lamonica, C.A.4
  • 11
    • 0026542238 scopus 로고
    • Increased susceptibility of differentiated mononuclear phagocytes to productive infection with human immunodeficiency virus-1 (HIV-1)
    • Rich, E. A., Chen, I. S., Zack, J. A., Leonard, M. L., O'Brien, W. A. (1992) Increased susceptibility of differentiated mononuclear phagocytes to productive infection with human immunodeficiency virus-1 (HIV-1). J. Clin. Invest. 89, 176-183.
    • (1992) J. Clin. Invest. , vol.89 , pp. 176-183
    • Rich, E.A.1    Chen, I.S.2    Zack, J.A.3    Leonard, M.L.4    O'Brien, W.A.5
  • 12
    • 0031974617 scopus 로고    scopus 로고
    • CCR5 expression correlates with susceptibility of maturing monocytes to human immunodeficiency virus type 1 infection
    • Naif, H. M., Li, S., Alali, M., Sloane, A., Wu, L., Kelly, M., Lynch, G., Lloyd, A., Cunningham, A. L. (1998) CCR5 expression correlates with susceptibility of maturing monocytes to human immunodeficiency virus type 1 infection. J. Virol. 72, 830-836.
    • (1998) J. Virol. , vol.72 , pp. 830-836
    • Naif, H.M.1    Li, S.2    Alali, M.3    Sloane, A.4    Wu, L.5    Kelly, M.6    Lynch, G.7    Lloyd, A.8    Cunningham, A.L.9
  • 13
    • 0031743948 scopus 로고    scopus 로고
    • Tat-associated kinase, TAK, activity is regulated by distinct mechanisms in peripheral blood lymphocytes and promonocytic cell lines
    • Herrmann, C. H., Carroll, R. G., Wei, P., Jones, K. A., Rice, A. P. (1998) Tat-associated kinase, TAK, activity is regulated by distinct mechanisms in peripheral blood lymphocytes and promonocytic cell lines. J. Virol. 72, 9881-9888.
    • (1998) J. Virol. , vol.72 , pp. 9881-9888
    • Herrmann, C.H.1    Carroll, R.G.2    Wei, P.3    Jones, K.A.4    Rice, A.P.5
  • 14
    • 0036839206 scopus 로고    scopus 로고
    • Transient induction of cyclin T1 during human macrophage differentiation regulates human immunodeficiency virus type 1 Tat transactivation function
    • Liou, L. Y., Herrmann, C. H., Rice, A. P. (2002) Transient induction of cyclin T1 during human macrophage differentiation regulates human immunodeficiency virus type 1 Tat transactivation function. J. Virol. 76, 10579-10587.
    • (2002) J. Virol. , vol.76 , pp. 10579-10587
    • Liou, L.Y.1    Herrmann, C.H.2    Rice, A.P.3
  • 15
    • 0033179335 scopus 로고    scopus 로고
    • HIV-1 Tat: Coping with negative elongation factors
    • Garber, M. E., Jones, K. A. (1999) HIV-1 Tat: coping with negative elongation factors. Curr. Opin. Immunol. 11, 460-465.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 460-465
    • Garber, M.E.1    Jones, K.A.2
  • 16
    • 0032701796 scopus 로고    scopus 로고
    • Tackling Tat
    • Karn, J. (1999) Tackling Tat. J. Mol. Biol. 293, 235-254.
    • (1999) J. Mol. Biol. , vol.293 , pp. 235-254
    • Karn, J.1
  • 17
    • 2142817265 scopus 로고    scopus 로고
    • Regulation of TAK/P-TEFb in CD4+ T lymphocytes and macrophages
    • Rice, A. P., Herrmann, C. H. (2003) Regulation of TAK/P-TEFb in CD4+ T lymphocytes and macrophages. Curr. HIV Res. 1, 395-404.
    • (2003) Curr. HIV Res. , vol.1 , pp. 395-404
    • Rice, A.P.1    Herrmann, C.H.2
  • 18
    • 0033604520 scopus 로고    scopus 로고
    • Tat transactivation: A model for the regulation of eukaryotic transcriptional elongation
    • Taube, R., Fujinaga, K., Wimmer, J., Barboric, M., Peterlin, B. M. (1999) Tat transactivation: a model for the regulation of eukaryotic transcriptional elongation. Virology 264, 245-253.
    • (1999) Virology , vol.264 , pp. 245-253
    • Taube, R.1    Fujinaga, K.2    Wimmer, J.3    Barboric, M.4    Peterlin, B.M.5
  • 19
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price, D. H. (2000) P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 20, 2629-2634.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2629-2634
    • Price, D.H.1
  • 20
    • 0141815505 scopus 로고    scopus 로고
    • Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation
    • Palancade, B., Bensaude, O. (2003) Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation. Eur. J. Biochem. 270, 3859-3870.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3859-3870
    • Palancade, B.1    Bensaude, O.2
  • 21
    • 0346095303 scopus 로고    scopus 로고
    • Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element
    • Fujinaga, K., Irwin, D., Huang, Y., Taube, R., Kurosu, T., Peterlin, B. M. (2004) Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element. Mol. Cell. Biol. 24, 787-795.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 787-795
    • Fujinaga, K.1    Irwin, D.2    Huang, Y.3    Taube, R.4    Kurosu, T.5    Peterlin, B.M.6
  • 22
    • 0342748478 scopus 로고    scopus 로고
    • Domains in the SPT5 protein that modulate its transcriptional regulatory properties
    • Ivanov, D., Kwak, Y. T., Guo, J., Gaynor, R. B. (2000) Domains in the SPT5 protein that modulate its transcriptional regulatory properties. Mol. Cell. Biol. 20, 2970-2983.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2970-2983
    • Ivanov, D.1    Kwak, Y.T.2    Guo, J.3    Gaynor, R.B.4
  • 23
    • 0032533253 scopus 로고    scopus 로고
    • The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
    • Garber, M. E., Wei, P., KewalRamani, V. N., Mayall, T. P., Herrmann, C. H., Rice, A. P., Littman, D. R., Jones, K. A. (1998) The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes Dev. 12, 3512-3527.
    • (1998) Genes Dev. , vol.12 , pp. 3512-3527
    • Garber, M.E.1    Wei, P.2    Kewalramani, V.N.3    Mayall, T.P.4    Herrmann, C.H.5    Rice, A.P.6    Littman, D.R.7    Jones, K.A.8
  • 24
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei, P., Garber, M. E., Fang, S. M., Fischer, W. H., Jones, K. A. (1998) A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92, 451-462.
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 25
    • 0035891288 scopus 로고    scopus 로고
    • 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
    • Nguyen, V. T., Kiss, T., Michels, A. A., Bensaude, O. (2001) 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes. Nature 414, 322-325.
    • (2001) Nature , vol.414 , pp. 322-325
    • Nguyen, V.T.1    Kiss, T.2    Michels, A.A.3    Bensaude, O.4
  • 26
    • 0035891271 scopus 로고    scopus 로고
    • The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription
    • Yang, Z., Zhu, Q., Luo, K., Zhou, Q. (2001) The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription. Nature 414, 317-322.
    • (2001) Nature , vol.414 , pp. 317-322
    • Yang, Z.1    Zhu, Q.2    Luo, K.3    Zhou, Q.4
  • 28
    • 18144371989 scopus 로고    scopus 로고
    • HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK
    • Byers, S. A., Price, J. P., Cooper, J. J., Li, Q., Price, D. H. (2005) HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK. J. Biol. Chem. 280, 16360-16367.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16360-16367
    • Byers, S.A.1    Price, J.P.2    Cooper, J.J.3    Li, Q.4    Price, D.H.5
  • 29
    • 27744459377 scopus 로고    scopus 로고
    • siRNA depletion of 7SK snRNA induces apoptosis but does not affect expression of the HIV-1 LTR or P-TEFb-dependent cellular genes
    • Haaland, R. E., Herrmann, C. H., Rice, A. P. (2005) siRNA depletion of 7SK snRNA induces apoptosis but does not affect expression of the HIV-1 LTR or P-TEFb-dependent cellular genes. J. Cell. Physiol. 205, 463-470.
    • (2005) J. Cell. Physiol. , vol.205 , pp. 463-470
    • Haaland, R.E.1    Herrmann, C.H.2    Rice, A.P.3
  • 30
    • 3242711219 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 infection induces cyclin T1 expression in macrophages
    • Liou, L. Y., Herrmann, C. H., Rice, A. P. (2004) Human immunodeficiency virus type 1 infection induces cyclin T1 expression in macrophages. J. Virol. 78, 8114-8119.
    • (2004) J. Virol. , vol.78 , pp. 8114-8119
    • Liou, L.Y.1    Herrmann, C.H.2    Rice, A.P.3
  • 31
    • 0031747965 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 vectors efficiently transduce human hematopoietic stem cells
    • Sutton, R. E., Wu, H. T., Rigg, R., Bohnlein, E., Brown, P. O. (1998) Human immunodeficiency virus type 1 vectors efficiently transduce human hematopoietic stem cells. J. Virol. 72, 5781-5788.
    • (1998) J. Virol. , vol.72 , pp. 5781-5788
    • Sutton, R.E.1    Wu, H.T.2    Rigg, R.3    Bohnlein, E.4    Brown, P.O.5
  • 32
    • 0028831057 scopus 로고
    • Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: Candidate for a Tat cofactor
    • Herrmann, C. H., Rice, A. P. (1995) Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor. J. Virol. 69, 1612-1620.
    • (1995) J. Virol. , vol.69 , pp. 1612-1620
    • Herrmann, C.H.1    Rice, A.P.2
  • 33
    • 1642366130 scopus 로고    scopus 로고
    • Increased association of 7SK snRNA with Tat cofactor P-TEFb following activation of peripheral blood lymphocytes
    • Haaland, R. E., Herrmann, C. H., Rice, A. P. (2003) Increased association of 7SK snRNA with Tat cofactor P-TEFb following activation of peripheral blood lymphocytes. AIDS 17, 2429-2436.
    • (2003) AIDS , vol.17 , pp. 2429-2436
    • Haaland, R.E.1    Herrmann, C.H.2    Rice, A.P.3
  • 34
    • 18144422796 scopus 로고    scopus 로고
    • Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance of active and inactive positive transcription elongation factor b complexes for control of transcription
    • Yik, J. H., Chen, R., Pezda, A. C., Zhou, Q. (2005) Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance of active and inactive positive transcription elongation factor b complexes for control of transcription. J. Biol. Chem. 280, 16368-16376.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16368-16376
    • Yik, J.H.1    Chen, R.2    Pezda, A.C.3    Zhou, Q.4
  • 35
    • 15944395145 scopus 로고    scopus 로고
    • Insights into host responses against pathogens from transcriptional profiling
    • Jenner, R. G., Young, R. A. (2005) Insights into host responses against pathogens from transcriptional profiling. Nat. Rev. Microbiol. 3, 281-294.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 281-294
    • Jenner, R.G.1    Young, R.A.2
  • 36
    • 14744272605 scopus 로고    scopus 로고
    • Differential localization and expression of the Cdk9 42k and 55k isoforms
    • Liu, H., Herrmann, C. H. (2005) Differential localization and expression of the Cdk9 42k and 55k isoforms. J. Cell. Physiol. 203, 251-260.
    • (2005) J. Cell. Physiol. , vol.203 , pp. 251-260
    • Liu, H.1    Herrmann, C.H.2
  • 37
    • 0026658625 scopus 로고
    • Macrophage response to bacteria: Induction of marked secretory and cellular activities by lipoteichoic acids
    • Keller, R., Fischer, W., Keist, R., Bassetti, S. (1992) Macrophage response to bacteria: induction of marked secretory and cellular activities by lipoteichoic acids. Infect. Immun. 60, 3664-3672.
    • (1992) Infect. Immun. , vol.60 , pp. 3664-3672
    • Keller, R.1    Fischer, W.2    Keist, R.3    Bassetti, S.4
  • 39
    • 0023936157 scopus 로고
    • Regulation of tumor necrosis factor/cachectin and IL-1 secretion in human mononuclear phagocytes
    • Burchett, S. K., Weaver, W. M., Westall, J. A., Larsen, A., Kronheim, S., Wilson, C. B. (1988) Regulation of tumor necrosis factor/cachectin and IL-1 secretion in human mononuclear phagocytes. J. Immunol. 140, 3473-3481.
    • (1988) J. Immunol. , vol.140 , pp. 3473-3481
    • Burchett, S.K.1    Weaver, W.M.2    Westall, J.A.3    Larsen, A.4    Kronheim, S.5    Wilson, C.B.6
  • 40
    • 0023639560 scopus 로고
    • Regulation of tumor necrosis factor (TNF) expression: Interferon-γ enhances the accumulation of mRNA for TNF induced by lipopolysaccharide in murine peritoneal macrophages
    • Koerner, T. J., Adams, D. O., Hamilton, T. A. (1987) Regulation of tumor necrosis factor (TNF) expression: interferon-γ enhances the accumulation of mRNA for TNF induced by lipopolysaccharide in murine peritoneal macrophages. Cell. Immunol. 109, 437-443.
    • (1987) Cell. Immunol. , vol.109 , pp. 437-443
    • Koerner, T.J.1    Adams, D.O.2    Hamilton, T.A.3
  • 41
    • 0029852069 scopus 로고    scopus 로고
    • Lipoteichoic acid from viridans streptococci induces the production of tumor necrosis factor and nitric oxide by murine macrophages
    • English, B. K., Patrick, C. C., Orlicek, S. L., McCordic, R., Shenep, J. L. (1996) Lipoteichoic acid from viridans streptococci induces the production of tumor necrosis factor and nitric oxide by murine macrophages. J. Infect. Dis. 174, 1348-1351.
    • (1996) J. Infect. Dis. , vol.174 , pp. 1348-1351
    • English, B.K.1    Patrick, C.C.2    Orlicek, S.L.3    McCordic, R.4    Shenep, J.L.5
  • 42
    • 0029048442 scopus 로고
    • Peptidoglycan induces transcription and secretion of TNF-α and activation of lyn, extracellular signal-regulated kinase, and rsk signal transduction proteins in mouse macrophages
    • Gupta, D., Jin, Y. P., Dziarski, R. (1995) Peptidoglycan induces transcription and secretion of TNF-α and activation of lyn, extracellular signal-regulated kinase, and rsk signal transduction proteins in mouse macrophages. J. Immunol. 155, 2620-2630.
    • (1995) J. Immunol. , vol.155 , pp. 2620-2630
    • Gupta, D.1    Jin, Y.P.2    Dziarski, R.3
  • 43
    • 2142768833 scopus 로고    scopus 로고
    • Regulation of proinflammatory cytokine expression by Shiga toxin 1 and/or lipopolysaccharides in the human monocytic cell line THP-1
    • Harrison, L. M., van Haaften, W. C., Tesh, V. L. (2004) Regulation of proinflammatory cytokine expression by Shiga toxin 1 and/or lipopolysaccharides in the human monocytic cell line THP-1. Infect. Immun. 72, 2618-2627.
    • (2004) Infect. Immun. , vol.72 , pp. 2618-2627
    • Harrison, L.M.1    Van Haaften, W.C.2    Tesh, V.L.3
  • 45
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., Rogers, S. W. (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
  • 46
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • Orlowski, M., Wilk, S. (2003) Ubiquitin-independent proteolytic functions of the proteasome. Arch. Biochem. Biophys. 415, 1-5.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 47
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome
    • Jariel-Encontre, I., Pariat, M., Martin, F., Carillo, S., Salvat, C., Piechaczyk, M. (1995) Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome. J. Biol. Chem. 270, 11623-11627.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 48
    • 0034616885 scopus 로고    scopus 로고
    • Ca2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination
    • Tarcsa, E., Szymanska, G., Lecker, S., O'Connor, C. M., Goldberg, A. L. (2000) Ca2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination. J. Biol. Chem. 275, 20295-20301.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20295-20301
    • Tarcsa, E.1    Szymanska, G.2    Lecker, S.3    O'Connor, C.M.4    Goldberg, A.L.5
  • 50
    • 0036791010 scopus 로고    scopus 로고
    • Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1
    • Asher, G., Lotem, J., Sachs, L., Kahana, C., Shaul, Y. (2002) Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1. Proc. Natl. Acad. Sci. USA 99, 13125-13130.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13125-13130
    • Asher, G.1    Lotem, J.2    Sachs, L.3    Kahana, C.4    Shaul, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.