메뉴 건너뛰기




Volumn 20, Issue 8, 2000, Pages 2629-2634

P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; ELONGATION FACTOR; MESSENGER RNA; RNA POLYMERASE II; TRANSACTIVATOR PROTEIN;

EID: 0034111019     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.8.2629-2634.2000     Document Type: Short Survey
Times cited : (591)

References (86)
  • 1
    • 0032538444 scopus 로고    scopus 로고
    • FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO
    • Archambault, J., G. Pan, G. K. Dahmus, M. Cartier, N. F. Marshall, S. Zhang, M. E. Dahmus, and J. Greenblatt. 1998. FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO. J. Biol. Chem. 273: 27593-27601.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27593-27601
    • Archambault, J.1    Pan, G.2    Dahmus, G.K.3    Cartier, M.4    Marshall, N.F.5    Zhang, S.6    Dahmus, M.E.7    Greenblatt, J.8
  • 2
    • 0033152538 scopus 로고    scopus 로고
    • Coupling RNA polymerase II transcription with pre-mRNA processing
    • Bentley, D. 1999. Coupling RNA polymerase II transcription with pre-mRNA processing. Curr. Opin. Cell Biol. 11:347-351.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 347-351
    • Bentley, D.1
  • 3
    • 0028969391 scopus 로고
    • Regulation of transcriptional elongation by RNA polymerase II
    • Bentley, D. L. 1995. Regulation of transcriptional elongation by RNA polymerase II. Curr. Opin. Genet. Dev. 5:210-216.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 210-216
    • Bentley, D.L.1
  • 4
    • 0032401752 scopus 로고    scopus 로고
    • Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat
    • Bieniasz, P. D., T. A. Grdina, H. P. Bogerd, and B. R. Cullen. 1998. Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat. EMBO J. 17:7056-7065.
    • (1998) EMBO J. , vol.17 , pp. 7056-7065
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 5
    • 0032991430 scopus 로고    scopus 로고
    • Analysis of the effect of natural sequence variation in Tat and in cyclin T on the formation and RNA binding properties of Tat-cyclin T complexes
    • Bieniasz, P. D., T. A. Grdina, H. P. Bogerd, and B. R. Cullen. 1999. Analysis of the effect of natural sequence variation in Tat and in cyclin T on the formation and RNA binding properties of Tat-cyclin T complexes. J. Virol. 73:5777-5786.
    • (1999) J. Virol. , vol.73 , pp. 5777-5786
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 6
    • 0033002198 scopus 로고    scopus 로고
    • Highly divergent lentiviral Tat proteins activate viral gene expression by a common mechanism
    • Bieniasz, P. D., T. A. Grdina, H. P. Bogerd, and B. R. Cullen. 1999. Highly divergent lentiviral Tat proteins activate viral gene expression by a common mechanism. Mol. Cell. Biol. 19:4592-4599.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4592-4599
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 7
    • 0033529211 scopus 로고    scopus 로고
    • Recruitment of cyclin T1/P-TEFb to an HIV type 1 long terminal repeat promoter proximal RNA target is both necessary and sufficient for full activation of transcription
    • Bieniasz, P. D., T. A. Grdina, H. P. Bogerd, and B. R. Cullen. 1999. Recruitment of cyclin T1/P-TEFb to an HIV type 1 long terminal repeat promoter proximal RNA target is both necessary and sufficient for full activation of transcription. Proc. Natl. Acad. Sci. USA 96:7791-7796.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7791-7796
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 9
    • 0026558060 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 Tat activity by coexpression of heterologous trans activators
    • Carroll, R., B. M. Peterlin, and D. Derse. 1992. Inhibition of human immunodeficiency virus type 1 Tat activity by coexpression of heterologous trans activators. J. Virol. 66:2000-2007.
    • (1992) J. Virol. , vol.66 , pp. 2000-2007
    • Carroll, R.1    Peterlin, B.M.2    Derse, D.3
  • 10
    • 0032935399 scopus 로고    scopus 로고
    • Tat activates human immunodeficiency virus type 1 transcriptional elongation independent of TFIIH kinase
    • Chen, D., and Q. Zhou. 1999. Tat activates human immunodeficiency virus type 1 transcriptional elongation independent of TFIIH kinase. Mol. Cell. Biol. 19:2863-2871.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2863-2871
    • Chen, D.1    Zhou, Q.2
  • 11
  • 12
    • 0024561487 scopus 로고
    • 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro
    • Chodosh, L. A., A. Fire, M. Samuels, and P. A. Sharp. 1989. 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro. J. Biol. Chem. 264:2250-2257.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2250-2257
    • Chodosh, L.A.1    Fire, A.2    Samuels, M.3    Sharp, P.A.4
  • 13
    • 0029909605 scopus 로고    scopus 로고
    • Requirements for RNA polymerase II carboxyl-terminal domain for transcription of human retroviruses, human T-cell lymphotrophic virus, and HIV-1
    • Chun, R. F., and K. T. Jeang. 1996. Requirements for RNA polymerase II carboxyl-terminal domain for transcription of human retroviruses, human T-cell lymphotrophic virus, and HIV-1. J. Biol. Chem. 271:27888-27894.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27888-27894
    • Chun, R.F.1    Jeang, K.T.2
  • 14
    • 0026315385 scopus 로고
    • c-fos gene transcription in murine macrophages is modulated by a calcium-dependent block to elongation in intron 1
    • Collart, M. A., N. Tourkine, D. Belin, P. Vassalli, P. Jeanteur, and J.-M. Blanchard. 1991. c-fos gene transcription in murine macrophages is modulated by a calcium-dependent block to elongation in intron 1, Mol. Cell. Biol. 11:2826-2831.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2826-2831
    • Collart, M.A.1    Tourkine, N.2    Belin, D.3    Vassalli, P.4    Jeanteur, P.5    Blanchard, J.-M.6
  • 15
    • 0030856701 scopus 로고    scopus 로고
    • The HIV transactivator TAT hinds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II
    • Cujec, T. P., H. Okamoto, K. Fujinaga, J. Meyer, H. Chamberlin, D. O. Morgan, B. M. Peterlin. 1997. The HIV transactivator TAT hinds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II. Genes Dev. 11:2645-2657.
    • (1997) Genes Dev. , vol.11 , pp. 2645-2657
    • Cujec, T.P.1    Okamoto, H.2    Fujinaga, K.3    Meyer, J.4    Chamberlin, H.5    Morgan, D.O.6    Peterlin, B.M.7
  • 16
    • 0029796976 scopus 로고    scopus 로고
    • Phosphorylation of mammalian RNA polymerase II
    • Dahmus, M. E. 1996. Phosphorylation of mammalian RNA polymerase II. Methods Enzymol. 273:185-193.
    • (1996) Methods Enzymol. , vol.273 , pp. 185-193
    • Dahmus, M.E.1
  • 17
    • 0031834340 scopus 로고    scopus 로고
    • Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity
    • Edwards, M. C., C. Wong, and S. J. Elledge. 1998. Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity. Mol. Cell. Biol. 18:4291-4300.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4291-4300
    • Edwards, M.C.1    Wong, C.2    Elledge, S.J.3
  • 18
    • 0029862947 scopus 로고    scopus 로고
    • Phosphorylation dependence of the initiation of productive transcription of Balbiani ring 2 genes in living cells
    • Egyhazi, E., A. Ossoinak, A. Pigon, C. Holmgren, J. M. Lee, and A. L. Greenleaf. 1996. Phosphorylation dependence of the initiation of productive transcription of Balbiani ring 2 genes in living cells. Chromosoma 104:422-433.
    • (1996) Chromosoma , vol.104 , pp. 422-433
    • Egyhazi, E.1    Ossoinak, A.2    Pigon, A.3    Holmgren, C.4    Lee, J.M.5    Greenleaf, A.L.6
  • 19
    • 0033594917 scopus 로고    scopus 로고
    • Host-cell positive transcription elongation factor b kinase activity is essential and limiting for HIV type 1 replication
    • Flores, O., G. Lee, J. Kessler, M. Miller, W. Schlief, J. Tomassini, and D. Hazuda. 1999. Host-cell positive transcription elongation factor b kinase activity is essential and limiting for HIV type 1 replication. Proc. Natl. Acad. Sci. USA 96:7208-7213.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7208-7213
    • Flores, O.1    Lee, G.2    Kessler, J.3    Miller, M.4    Schlief, W.5    Tomassini, J.6    Hazuda, D.7
  • 20
    • 0033521094 scopus 로고    scopus 로고
    • Cyclin K functions as a Cdk9 regulatory subunit and participates in RNA polymerase II transcription
    • Fu, T. J., J. Peng, D. H. Price, and O. Flores. 1999. Cyclin K functions as a Cdk9 regulatory subunit and participates in RNA polymerase II transcription. J. Biol. Chem. 274:34527-34530.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34527-34530
    • Fu, T.J.1    Peng, J.2    Price, D.H.3    Flores, O.4
  • 21
    • 0031846856 scopus 로고    scopus 로고
    • The ability of positive transcription elongation factor B to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat
    • Kujinaga, K., T. P. Cujec, J. Peng, J. Garriga, D. H. Price, X. Grana, and B. M. Peterlin. 1998. The ability of positive transcription elongation factor B to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat. J. Virol. 72:7154-7159.
    • (1998) J. Virol. , vol.72 , pp. 7154-7159
    • Kujinaga, K.1    Cujec, T.P.2    Peng, J.3    Garriga, J.4    Price, D.H.5    Grana, X.6    Peterlin, B.M.7
  • 22
    • 0033179335 scopus 로고    scopus 로고
    • HIV-1 Tat: Coping with negative elongation factors
    • Garber, M. E., and K. A. Jones. 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
  • 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., P. Wei, V. N. KewalRamani, T. P. Mayall, C. H. Herrmann, A. P. Rice, D. R. Littman, and K. A. Jones. 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
    • 0039243885 scopus 로고    scopus 로고
    • Purification of a Tat-associatcd kinase reveals a TFIIH complex that modulates HIV-1 transcription
    • Garcia-Martinez, L. F., G. Mavankal, J. M. Neveu, W. S. Lane, D. Ivanov, and R. B. Gaynor. 1997. Purification of a Tat-associatcd kinase reveals a TFIIH complex that modulates HIV-1 transcription. EMBO J. 16:2836-2850.
    • (1997) EMBO J. , vol.16 , pp. 2836-2850
    • Garcia-Martinez, L.F.1    Mavankal, G.2    Neveu, J.M.3    Lane, W.S.4    Ivanov, D.5    Gaynor, R.B.6
  • 25
    • 0029846068 scopus 로고    scopus 로고
    • The CDC2-related kinase PITALRE is the catalytic subunit of active multimeric protein complexes
    • Garriga, J., X. Mayol, and X. Grana. 1996. The CDC2-related kinase PITALRE is the catalytic subunit of active multimeric protein complexes. Biochem. J. 319:293-298.
    • (1996) Biochem. J. , vol.319 , pp. 293-298
    • Garriga, J.1    Mayol, X.2    Grana, X.3
  • 26
  • 27
    • 0030470273 scopus 로고    scopus 로고
    • Phosphorylation site specificity of the CDC2-related kinase PITALRE
    • Garriga, J., E. Segura, X. Mayol, C. Grubmeyer, and X. Grana. 1996. Phosphorylation site specificity of the CDC2-related kinase PITALRE. Biochem. J. 320:983-989.
    • (1996) Biochem. J. , vol.320 , pp. 983-989
    • Garriga, J.1    Segura, E.2    Mayol, X.3    Grubmeyer, C.4    Grana, X.5
  • 28
    • 0032529484 scopus 로고
    • Targeting of CDK8 to a promoter-proximal RNA element demonstrates catalysis-dependent activation of gene expression
    • Gold, M. O., and A. P. Rice. 1498. Targeting of CDK8 to a promoter-proximal RNA element demonstrates catalysis-dependent activation of gene expression. Nucleic Acids Res. 26:3784-3788.
    • (1498) Nucleic Acids Res. , vol.26 , pp. 3784-3788
    • Gold, M.O.1    Rice, A.P.2
  • 29
    • 0031958598 scopus 로고    scopus 로고
    • PITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus Tat transactivation in vivo
    • Gold, M. O., X. Yang, C. H. Herrmann, and A. P. Rice. 1998. PITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus Tat transactivation in vivo. J. Virol. 72:4448-4453.
    • (1998) J. Virol. , vol.72 , pp. 4448-4453
    • Gold, M.O.1    Yang, X.2    Herrmann, C.H.3    Rice, A.P.4
  • 31
    • 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., R. G. Carroll, P. Wei, K. A. Jones, and A. P. Rice. 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
  • 32
    • 0027438621 scopus 로고
    • Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase
    • Herrmann, C. H., and A. P. Rice. 1993. Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase. Virology 197:601-608.
    • (1993) Virology , vol.197 , pp. 601-608
    • Herrmann, C.H.1    Rice, A.P.2
  • 33
    • 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., and A. P. Rice. 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
  • 34
    • 0033105827 scopus 로고    scopus 로고
    • Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme
    • Ho, C. K., and S. Shuman. 1999. Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme. Mol. Cell 3:405-411.
    • (1999) Mol. Cell , vol.3 , pp. 405-411
    • Ho, C.K.1    Shuman, S.2
  • 35
    • 0033618442 scopus 로고    scopus 로고
    • Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation
    • Isel, C., and J. Karn. 1999. Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation. J. Mol. Biol. 290:929-941.
    • (1999) J. Mol. Biol. , vol.290 , pp. 929-941
    • Isel, C.1    Karn, J.2
  • 36
    • 0033978121 scopus 로고    scopus 로고
    • Tat competes with CIITA for the binding to P-TEFb and blocks the expression of MHC class II genes in HIV infection
    • Kanazawa, S., T. Okamoto, and B. M. Peterlin. 1999. Tat competes with CIITA for the binding to P-TEFb and blocks the expression of MHC class II genes in HIV infection. Immunity 12:61-70.
    • (1999) Immunity , vol.12 , pp. 61-70
    • Kanazawa, S.1    Okamoto, T.2    Peterlin, B.M.3
  • 37
    • 0023513563 scopus 로고
    • Antitermination of transcription within the long terminal repeat of HIV by the tat gene product
    • Kao, S.-Y., A. F. Calman, P. A. Luciw, and E. M. Peterlin. 1987. Antitermination of transcription within the long terminal repeat of HIV by the tat gene product. Nature 330:489-493.
    • (1987) Nature , vol.330 , pp. 489-493
    • Kao, S.-Y.1    Calman, A.F.2    Luciw, P.A.3    Peterlin, E.M.4
  • 38
    • 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
  • 39
    • 0030864512 scopus 로고    scopus 로고
    • Transfer of Tat and release of TAR RNA during the activation of the human immunodeficiency virus type-1 transcription elongation complex
    • Keen, N. J., M. J. Churcher, and J. Karn. 1997. Transfer of Tat and release of TAR RNA during the activation of the human immunodeficiency virus type-1 transcription elongation complex. EMBO J. 10-3272.
    • (1997) EMBO J. , pp. 10-3272
    • Keen, N.J.1    Churcher, M.J.2    Karn, J.3
  • 40
    • 0026693315 scopus 로고
    • Stability of Drosophila RNA polymerase II elongation complexes in vitro
    • Kephart, D. D., N. F. Marshall, and D. H. Price. 1992. Stability of Drosophila RNA polymerase II elongation complexes in vitro. Mol. Cell. Biol. 12:2067-2077.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2067-2077
    • Kephart, D.D.1    Marshall, N.F.2    Price, D.H.3
  • 41
    • 0027255297 scopus 로고
    • HIV-1 Tat overcomes inefficient transcriptional elongation in vitro
    • Laspia, M. F., P. Wendel, and M. B. Mathews. 1993. HIV-1 Tat overcomes inefficient transcriptional elongation in vitro. J. Mol. Biol. 232:732-746.
    • (1993) J. Mol. Biol. , vol.232 , pp. 732-746
    • Laspia, M.F.1    Wendel, P.2    Mathews, M.B.3
  • 42
    • 0000337142 scopus 로고    scopus 로고
    • Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I
    • Lee, J. M., and A. L. Greenleaf. 1997. Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I. J. Biol. Chem. 272:10990-10993.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10990-10993
    • Lee, J.M.1    Greenleaf, A.L.2
  • 44
    • 0032476005 scopus 로고    scopus 로고
    • A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member
    • Liu, M., Z. Xie, and D. H. Price. 1998. A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member. J. Biol. Chem. 273:25541-25544.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25541-25544
    • Liu, M.1    Xie, Z.2    Price, D.H.3
  • 45
    • 0027310927 scopus 로고
    • Genetic analysis of the cofactor requirement for human immunodeficiency virus type 1 Tat function
    • Madore, S. J., and B. R. Cullen. 1993. Genetic analysis of the cofactor requirement for human immunodeficiency virus type 1 Tat function. J. Virol. 67:3703-3711.
    • (1993) J. Virol. , vol.67 , pp. 3703-3711
    • Madore, S.J.1    Cullen, B.R.2
  • 46
    • 0032558678 scopus 로고    scopus 로고
    • Recruitment of the TATA-binding protein to the HIV-1 promoter is a limiting step for Tat transactivation
    • Majello, B., C. Napolitano, and L. Lania. 1998. Recruitment of the TATA-binding protein to the HIV-1 promoter is a limiting step for Tat transactivation. AIDS 12:1957-1964.
    • (1998) AIDS , vol.12 , pp. 1957-1964
    • Majello, B.1    Napolitano, C.2    Lania, L.3
  • 47
    • 0033549883 scopus 로고    scopus 로고
    • Transcriptional regulation by targeted recruitment of cyclin-dependent CDK9 kinase in vivo
    • Majello, B., G. Napolitano, A. Giordano, and L. Lania. 1999. Transcriptional regulation by targeted recruitment of cyclin-dependent CDK9 kinase in vivo. Oncogene 18:4598-4605.
    • (1999) Oncogene , vol.18 , pp. 4598-4605
    • Majello, B.1    Napolitano, G.2    Giordano, A.3    Lania, L.4
  • 49
    • 0026064723 scopus 로고
    • HIV-1 Tat protein promotes formation of more-processive elongation complexes
    • Marciniak, R. A., and P. A. Sharp. 1991. HIV-1 Tat protein promotes formation of more-processive elongation complexes. EMBO J. 10:4189-4196.
    • (1991) EMBO J. , vol.10 , pp. 4189-4196
    • Marciniak, R.A.1    Sharp, P.A.2
  • 50
    • 0033610854 scopus 로고    scopus 로고
    • Regulation of carboxyl-terminal domain phosphatase by HIV-1 Tat protein
    • Marshall, N. F., G. K. Dahmus, and M. E. Dahmus. 1998. Regulation of carboxyl-terminal domain phosphatase by HIV-1 Tat protein. J. Biol. Chem. 273:31726-31730.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31726-31730
    • Marshall, N.F.1    Dahmus, G.K.2    Dahmus, M.E.3
  • 51
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall, N. F., J. Peng, Z. Xie, and D. H. Price. 1996. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:27176-27183.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 52
    • 0026725368 scopus 로고
    • Control of formation of two distinct classes of RNA polymerase H elongation complexes
    • Marshall, N. F., and D. H. Price. 1992. Control of formation of two distinct classes of RNA polymerase H elongation complexes. Mol. Cell. Biol. 12: 2078-2090.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2078-2090
    • Marshall, N.F.1    Price, D.H.2
  • 53
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall, N. F., and D. H. Price. 1995. Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270:12335-12338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 54
    • 0033151767 scopus 로고    scopus 로고
    • mRNA polyadenylation and its coupling to other RNA processing reactions and to transcription
    • Minvielle-Sebastia, L., and W. Keller. 1999. mRNA polyadenylation and its coupling to other RNA processing reactions and to transcription. Curr. Opin. Cell Biol. 11:352-357.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 352-357
    • Minvielle-Sebastia, L.1    Keller, W.2
  • 55
    • 0032858138 scopus 로고    scopus 로고
    • The CDK9-associated cyclins T1 and T2 exert opposite effects on HIV-1 Tat activity
    • Napolitano, G., P. Licciardo, P. Gallo, B. Majello, A. Giordano, L. Lania. 1999. The CDK9-associated cyclins T1 and T2 exert opposite effects on HIV-1 Tat activity. AIDS 13:1453-1459.
    • (1999) AIDS , vol.13 , pp. 1453-1459
    • Napolitano, G.1    Licciardo, P.2    Gallo, P.3    Majello, B.4    Giordano, A.5    Lania, L.6
  • 56
    • 0029956642 scopus 로고    scopus 로고
    • Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain
    • Parada, C. A., and R. G. Roeder. 1996. Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. Nature 384:375-378.
    • (1996) Nature , vol.384 , pp. 375-378
    • Parada, C.A.1    Roeder, R.G.2
  • 57
    • 0031032591 scopus 로고    scopus 로고
    • RNA-targeted activators, but not DNA-targeted activators, repress the synthesis of short transcripts at the human immunodeficiency virus type 1 long terminal repeat
    • Pendergrast, P. S., and N. Hernandez. 1997. RNA-targeted activators, but not DNA-targeted activators, repress the synthesis of short transcripts at the human immunodeficiency virus type 1 long terminal repeat. J. Virol. 71:910-917.
    • (1997) J. Virol. , vol.71 , pp. 910-917
    • Pendergrast, P.S.1    Hernandez, N.2
  • 59
    • 0032577577 scopus 로고    scopus 로고
    • Identification of a cyclin subunit required for the function of Drosophila P-TEFb
    • Peng, J., N. F. Marshall, and D. H. Price. 1998. Identification of a cyclin subunit required for the function of Drosophila P-TEFb. J. Biol. Chem. 273:13855-13860.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13855-13860
    • Peng, J.1    Marshall, N.F.2    Price, D.H.3
  • 60
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng, J., Y. Zhu, J. T. Milton, and D. H. Price. 1998. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev. 12:755-762.
    • (1998) Genes Dev. , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milton, J.T.3    Price, D.H.4
  • 61
    • 0033548533 scopus 로고    scopus 로고
    • Tat-associated kinase (P-TEFb): A component of transcription preinitiation and elongation complexes
    • Ping, Y. H., and T. M. Rana. 1999. Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes. J. Biol. Chem. 274:7399-7404.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7399-7404
    • Ping, Y.H.1    Rana, T.M.2
  • 62
    • 0033562094 scopus 로고    scopus 로고
    • Biochemical and functional interactions between HIV-1 Tat protein and TAR RNA
    • Rana, T. M., and K. T. Jeang. 1999. Biochemical and functional interactions between HIV-1 Tat protein and TAR RNA. Arch. Biochem. Biophys. 365: 175-185.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 175-185
    • Rana, T.M.1    Jeang, K.T.2
  • 63
    • 0030249832 scopus 로고    scopus 로고
    • The RNA polymerase II general elongation factors
    • Reines, D., J. W. Conaway, and R. C. Conaway. 1996. The RNA polymerase II general elongation factors. Trends Biochem. Sci. 21:351-355.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 351-355
    • Reines, D.1    Conaway, J.W.2    Conaway, R.C.3
  • 64
    • 0033151808 scopus 로고    scopus 로고
    • Mechanism and regulation of transcriptional elongation by RNA polymerase II
    • Reines, D., R. C. Conaway, and J. W. Conaway. 1999. Mechanism and regulation of transcriptional elongation by RNA polymerase II. Curr. Opin. Cell Biol. 11:342-346.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 342-346
    • Reines, D.1    Conaway, R.C.2    Conaway, J.W.3
  • 65
    • 0017091157 scopus 로고
    • The inhibition by DRB (5,6,-dichloro-1-β-D-ribofuranosylbenzimidazołe) of hnRNA and mRNA production in HeLa cells
    • Sehgal, P. B., J. E. Darnell, and I. Tamm. 1976. The inhibition by DRB (5,6,-dichloro-1-β-D-ribofuranosylbenzimidazołe) of hnRNA and mRNA production in HeLa cells. Cell 9:473-480.
    • (1976) Cell , vol.9 , pp. 473-480
    • Sehgal, P.B.1    Darnell, J.E.2    Tamm, I.3
  • 66
    • 0031763366 scopus 로고    scopus 로고
    • Factors regulating the transcriptional elongation activity of RNA polymerase II
    • Shilatifard, A. 1998. Factors regulating the transcriptional elongation activity of RNA polymerase II. FASEB J. 12:1437-1446.
    • (1998) FASEB J. , vol.12 , pp. 1437-1446
    • Shilatifard, A.1
  • 67
    • 0019321229 scopus 로고
    • Short capped hnRNA precursor chains in HeLa cells: Continued synthesis in the presence of 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole
    • Tamm, I., T. Kikuchi, J. E. Darnell, and M. Salditt-Georgeieff. 1980. Short capped hnRNA precursor chains in HeLa cells: continued synthesis in the presence of 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole. Biochemistry 19:2743-2748.
    • (1980) Biochemistry , vol.19 , pp. 2743-2748
    • Tamm, I.1    Kikuchi, T.2    Darnell, J.E.3    Salditt-Georgeieff, M.4
  • 68
    • 0033986157 scopus 로고    scopus 로고
    • Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1
    • Taube, R., K. Fujinaga, D. Irwin, J. Wimmer, M. Geyer, and B. M. Peterlin. 2000. Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1. J. Virol. 74:892-898.
    • (2000) J. Virol. , vol.74 , pp. 892-898
    • Taube, R.1    Fujinaga, K.2    Irwin, D.3    Wimmer, J.4    Geyer, M.5    Peterlin, B.M.6
  • 69
    • 0033604520 scopus 로고    scopus 로고
    • Tat transactivation: A model for the regulation of eukaryotic transcriptional elongation
    • Taube, R., K. Fujinaga, J. Wimmer, M. Barborie, and B. M. Peterlin. 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    Barborie, M.4    Peterlin, B.M.5
  • 70
    • 0024635688 scopus 로고
    • formation of short RNA polymerase II transcripts that terminate within the HIV-1 and HIV-2 promoter-proximal downstream regions
    • Toohey, M. G., and K. A. Jones. 1989. In vitro formation of short RNA polymerase II transcripts that terminate within the HIV-1 and HIV-2 promoter-proximal downstream regions. Genes Dev. 3:265-282.
    • (1989) Genes Dev. , vol.3 , pp. 265-282
    • Toohey, M.G.1    Jones, K.A.2
  • 72
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • Wada, T., T. Takagi, Y. Yamaguchi, D. Watanabe, and H. Handa. 1998. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J. 17:7395-7403.
    • (1998) EMBO J. , vol.17 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 73
    • 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., M. E. Garber, S. M. Fang, W. H. Fischer, and K. A. Jones. 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
  • 74
    • 0033566042 scopus 로고    scopus 로고
    • Transcription elongation factor hSPT5 stimulates mRNA capping
    • Wen, Y., and A. J. Shatkin. 1999. Transcription elongation factor hSPT5 stimulates mRNA capping. Genes Dev. 13:1774-1779.
    • (1999) Genes Dev. , vol.13 , pp. 1774-1779
    • Wen, Y.1    Shatkin, A.J.2
  • 75
    • 0033102387 scopus 로고    scopus 로고
    • Interactions between Tat and TAR and human immunodeficiency virus replication are facilitated by human cyclin T1 but not cyclins T2a or T2b
    • Wimmer, J., K. Fujinaga, R. Taube, T. P. Cujec, Y. Zhu, J. Peng, D. H. Price, and B. M. Peterlin. 1999. Interactions between Tat and TAR and human immunodeficiency virus replication are facilitated by human cyclin T1 but not cyclins T2a or T2b. Virology 255:182-189.
    • (1999) Virology , vol.255 , pp. 182-189
    • Wimmer, J.1    Fujinaga, K.2    Taube, R.3    Cujec, T.P.4    Zhu, Y.5    Peng, J.6    Price, D.H.7    Peterlin, B.M.8
  • 76
    • 0032571254 scopus 로고    scopus 로고
    • Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation
    • Wu-Baer, F., W. S. Lane, and R. B. Gaynor. 1998. Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation. J. Mol. Biol. 277:179-197.
    • (1998) J. Mol. Biol. , vol.277 , pp. 179-197
    • Wu-Baer, F.1    Lane, W.S.2    Gaynor, R.B.3
  • 77
    • 15844396178 scopus 로고    scopus 로고
    • Purification of an RNA polymerase II transcript release factor from Drosophila
    • Xie, Z., and D. H. Price. 1996. Purification of an RNA polymerase II transcript release factor from Drosophila. J. Biol. Chem. 271:11043-11046.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11043-11046
    • Xie, Z.1    Price, D.H.2
  • 78
    • 0031438709 scopus 로고    scopus 로고
    • Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity
    • Xie, Z., and D. H. Price. 1997. Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity. J. Biol. Chem. 272:31902-31907.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31902-31907
    • Xie, Z.1    Price, D.H.2
  • 79
    • 0033515521 scopus 로고    scopus 로고
    • NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
    • Yamaguchi, Y., T. Takagi, T. Wada, K. Yano, A. Furuya, S. Sugimoto, J. Hasegawa, and H. Handa. 1999. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell 97:41-51.
    • (1999) Cell , vol.97 , pp. 41-51
    • Yamaguchi, Y.1    Takagi, T.2    Wada, T.3    Yano, K.4    Furuya, A.5    Sugimoto, S.6    Hasegawa, J.7    Handa, H.8
  • 81
    • 0030780092 scopus 로고    scopus 로고
    • TAK. an HIV TAT-associated kinase, is a memher of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines
    • Yang, X. Z., M. O. Gold, D. N. Tang, D. E. Lewis, E. Aguilarcordova, A. P. Rice, and C. H. Herrmann. 1997. TAK. an HIV TAT-associated kinase, is a memher of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines. Proc. Natl. Acad. Sci. USA 94:12331-12336.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12331-12336
    • Yang, X.Z.1    Gold, M.O.2    Tang, D.N.3    Lewis, D.E.4    Aguilarcordova, E.5    Rice, A.P.6    Herrmann, C.H.7
  • 82
    • 0032543570 scopus 로고    scopus 로고
    • Transcriptional control: Tat cofactors and transcriptional elongation
    • Yankulov, K., and D. Bentley. 1998. Transcriptional control: Tat cofactors and transcriptional elongation. Curr. Biol. 8:R447-R449.
    • (1998) Curr. Biol. , vol.8
    • Yankulov, K.1    Bentley, D.2
  • 83
    • 0019902611 scopus 로고
    • Mechanism of action of dichloro-beta-D-ribofuranosylbenzimidazole: Effect on in vitro transcription
    • Zandomeni, R., B. Mittleman, D. Bunick, S. Ackerman, and R. Weinmann. 1982. Mechanism of action of dichloro-beta-D-ribofuranosylbenzimidazole: effect on in vitro transcription. Proc. Natl. Acad. Sci. USA 79:3167-3170.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3167-3170
    • Zandomeni, R.1    Mittleman, B.2    Bunick, D.3    Ackerman, S.4    Weinmann, R.5
  • 84
    • 0029074137 scopus 로고
    • Recycling of the general transcription factors during RNA polymerase II transcription
    • Zawel, L., K. P. Kumar, and D. Reinberg. 1995. Recycling of the general transcription factors during RNA polymerase II transcription. Genes Dev. 9:1479-1490.
    • (1995) Genes Dev. , vol.9 , pp. 1479-1490
    • Zawel, L.1    Kumar, K.P.2    Reinberg, D.3
  • 85
    • 0032127436 scopus 로고    scopus 로고
    • Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages
    • Zhou, Q., D. Chen, E. Pierstorff, and K. Luo. 1998. Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages. EMBO J. 17:3681-3691.
    • (1998) EMBO J. , vol.17 , pp. 3681-3691
    • Zhou, Q.1    Chen, D.2    Pierstorff, E.3    Luo, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.