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Volumn 9, Issue 5, 2013, Pages

Phosphorylation of CDK9 at Ser175 Enhances HIV Transcription and Is a Marker of Activated P-TEFb in CD4+ T Lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 9; SMALL NUCLEAR RIBONUCLEOPROTEIN; T LYMPHOCYTE RECEPTOR; TRANSACTIVATOR PROTEIN; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION ELONGATION FACTOR P TEFB; UNCLASSIFIED DRUG;

EID: 84878491386     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003338     Document Type: Article
Times cited : (85)

References (97)
  • 3
    • 84856484784 scopus 로고    scopus 로고
    • Control of HIV latency by epigenetic and non-epigenetic mechanisms
    • Mbonye U, Karn J, (2011) Control of HIV latency by epigenetic and non-epigenetic mechanisms. Current HIV research 9: 554-567.
    • (2011) Current HIV Research , vol.9 , pp. 554-567
    • Mbonye, U.1    Karn, J.2
  • 4
    • 77249123298 scopus 로고    scopus 로고
    • Mechanisms of HIV latency: an emerging picture of complexity
    • Margolis DM, (2010) Mechanisms of HIV latency: an emerging picture of complexity. Curr HIV/AIDS Rep 7: 37-43.
    • (2010) Curr HIV/AIDS Rep , vol.7 , pp. 37-43
    • Margolis, D.M.1
  • 5
    • 77954633050 scopus 로고    scopus 로고
    • HIV persistence and the prospect of long-term drug-free remissions for HIV-infected individuals
    • Trono D, Van Lint C, Rouzioux C, Verdin E, Barre-Sinoussi F, et al. (2010) HIV persistence and the prospect of long-term drug-free remissions for HIV-infected individuals. Science 329: 174-180.
    • (2010) Science , vol.329 , pp. 174-180
    • Trono, D.1    van Lint, C.2    Rouzioux, C.3    Verdin, E.4    Barre-Sinoussi, F.5
  • 6
    • 0032953920 scopus 로고    scopus 로고
    • Latent infection of CD4+ T cells provides a mechanism for lifelong persistence of HIV-1, even in patients on effective combination therapy
    • Finzi D, Blankson J, Siliciano JD, Margolick JB, Chadwick K, et al. (1999) Latent infection of CD4+ T cells provides a mechanism for lifelong persistence of HIV-1, even in patients on effective combination therapy. Nat Med 5: 512-517.
    • (1999) Nat Med , vol.5 , pp. 512-517
    • Finzi, D.1    Blankson, J.2    Siliciano, J.D.3    Margolick, J.B.4    Chadwick, K.5
  • 7
    • 0032555117 scopus 로고    scopus 로고
    • Early establishment of a pool of latently infected, resting CD4(+) T cells during primary HIV-1 infection
    • Chun T-W, Engel D, Berrey MM, Shea T, Corey L, et al. (1998) Early establishment of a pool of latently infected, resting CD4(+) T cells during primary HIV-1 infection. Proc Natl Acad Sci U S A 95: 8869-8873.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8869-8873
    • Chun, T.-W.1    Engel, D.2    Berrey, M.M.3    Shea, T.4    Corey, L.5
  • 8
    • 68349139711 scopus 로고    scopus 로고
    • HIV reservoir size and persistence are driven by T cell survival and homeostatic proliferation
    • Chomont N, El-Far M, Ancuta P, Trautmann L, Procopio FA, et al. (2009) HIV reservoir size and persistence are driven by T cell survival and homeostatic proliferation. Nat Med 15: 893-900.
    • (2009) Nat Med , vol.15 , pp. 893-900
    • Chomont, N.1    El-Far, M.2    Ancuta, P.3    Trautmann, L.4    Procopio, F.A.5
  • 10
    • 77958485320 scopus 로고    scopus 로고
    • Establishment of HIV-1 latency in resting CD4+ T cells depends on chemokine-induced changes in the actin cytoskeleton
    • Cameron PU, Saleh S, Sallmann G, Solomon A, Wightman F, et al. (2010) Establishment of HIV-1 latency in resting CD4+ T cells depends on chemokine-induced changes in the actin cytoskeleton. Proc Natl Acad Sci U S A 107: 16934-16939.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16934-16939
    • Cameron, P.U.1    Saleh, S.2    Sallmann, G.3    Solomon, A.4    Wightman, F.5
  • 11
    • 55949083820 scopus 로고    scopus 로고
    • HIV rebounds from latently infected cells, rather than from continuing low-level replication
    • Joos B, Fischer M, Kuster H, Pillai SK, Wong JK, et al. (2008) HIV rebounds from latently infected cells, rather than from continuing low-level replication. Proc Natl Acad Sci U S A 105: 16725-16730.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16725-16730
    • Joos, B.1    Fischer, M.2    Kuster, H.3    Pillai, S.K.4    Wong, J.K.5
  • 12
    • 0033930509 scopus 로고    scopus 로고
    • HIV-1 rebound after anti-retroviral therapy
    • Ho DD, Zhang L, (2000) HIV-1 rebound after anti-retroviral therapy. Nat Med 6: 736-737.
    • (2000) Nat Med , vol.6 , pp. 736-737
    • Ho, D.D.1    Zhang, L.2
  • 13
    • 79952204267 scopus 로고    scopus 로고
    • Episomal viral cDNAs identify a reservoir that fuels viral rebound after treatment interruption and that contributes to treatment failure
    • Sharkey M, Babic DZ, Greenough T, Gulick R, Kuritzkes DR, et al. (2011) Episomal viral cDNAs identify a reservoir that fuels viral rebound after treatment interruption and that contributes to treatment failure. PLoS pathogens 7: e1001303.
    • (2011) PLoS Pathogens , vol.7
    • Sharkey, M.1    Babic, D.Z.2    Greenough, T.3    Gulick, R.4    Kuritzkes, D.R.5
  • 14
    • 0033592967 scopus 로고    scopus 로고
    • HIV-1 and T cell dynamics after interruption of highly active antiretroviral therapy (HAART) in patients with a history of sustained viral suppression
    • Davey RT Jr, Bhat N, Yoder C, Chun TW, Metcalf JA, et al. (1999) HIV-1 and T cell dynamics after interruption of highly active antiretroviral therapy (HAART) in patients with a history of sustained viral suppression. Proc Natl Acad Sci U S A 96: 15109-15114.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 15109-15114
    • Davey Jr., R.T.1    Bhat, N.2    Yoder, C.3    Chun, T.W.4    Metcalf, J.A.5
  • 15
    • 0030659177 scopus 로고    scopus 로고
    • Presence of an inducible HIV-1 latent reservoir during highly active antiretroviral therapy
    • Chun TW, Stuyver L, Mizell SB, Ehler LA, Mican JA, et al. (1997) Presence of an inducible HIV-1 latent reservoir during highly active antiretroviral therapy. Proc Natl Acad Sci U S A 94: 13193-13197.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13193-13197
    • Chun, T.W.1    Stuyver, L.2    Mizell, S.B.3    Ehler, L.A.4    Mican, J.A.5
  • 16
    • 14444273439 scopus 로고    scopus 로고
    • Identification of a reservoir for HIV-1 in patients on highly active antiretroviral therapy
    • Finzi D, Hermankova M, Pierson T, Carruth LM, Buck C, et al. (1997) Identification of a reservoir for HIV-1 in patients on highly active antiretroviral therapy. Science 278: 1295-1300.
    • (1997) Science , vol.278 , pp. 1295-1300
    • Finzi, D.1    Hermankova, M.2    Pierson, T.3    Carruth, L.M.4    Buck, C.5
  • 17
    • 70350148394 scopus 로고    scopus 로고
    • Understanding HIV-1 latency provides clues for the eradication of long-term reservoirs
    • Coiras M, Lopez-Huertas MR, Perez-Olmeda M, Alcami J, (2009) Understanding HIV-1 latency provides clues for the eradication of long-term reservoirs. Nat Rev Microbiol 7: 798-812.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 798-812
    • Coiras, M.1    Lopez-Huertas, M.R.2    Perez-Olmeda, M.3    Alcami, J.4
  • 18
    • 79954441735 scopus 로고    scopus 로고
    • The molecular biology of HIV latency: breaking and restoring the Tat-dependent transcriptional circuit
    • Karn J, (2011) The molecular biology of HIV latency: breaking and restoring the Tat-dependent transcriptional circuit. Current opinion in HIV and AIDS 6: 4-11.
    • (2011) Current Opinion in HIV and AIDS , vol.6 , pp. 4-11
    • Karn, J.1
  • 19
    • 41349095731 scopus 로고    scopus 로고
    • Transient-mediated fate determination in a transcriptional circuit of HIV
    • Weinberger LS, Dar RD, Simpson ML, (2008) Transient-mediated fate determination in a transcriptional circuit of HIV. Nat Genet 40: 466-470.
    • (2008) Nat Genet , vol.40 , pp. 466-470
    • Weinberger, L.S.1    Dar, R.D.2    Simpson, M.L.3
  • 21
    • 2342467344 scopus 로고    scopus 로고
    • Chromatin remodeling and modification during HIV-1 Tat-activated transcription
    • Pumfery A, Deng L, Maddukuri A, de la Fuente C, Li H, et al. (2003) Chromatin remodeling and modification during HIV-1 Tat-activated transcription. Curr HIV Res 1: 343-362.
    • (2003) Curr HIV Res , vol.1 , pp. 343-362
    • Pumfery, A.1    Deng, L.2    Maddukuri, A.3    de la Fuente, C.4    Li, H.5
  • 23
    • 79952605355 scopus 로고    scopus 로고
    • Chromatin reassembly factors are involved in transcriptional interference promoting HIV latency
    • Gallastegui E, Millan-Zambrano G, Terme JM, Chavez S, Jordan A, (2011) Chromatin reassembly factors are involved in transcriptional interference promoting HIV latency. Journal of virology 85: 3187-3202.
    • (2011) Journal of Virology , vol.85 , pp. 3187-3202
    • Gallastegui, E.1    Millan-Zambrano, G.2    Terme, J.M.3    Chavez, S.4    Jordan, A.5
  • 24
    • 57349090221 scopus 로고    scopus 로고
    • Epigenetic silencing of human immunodeficiency virus (HIV) transcription by formation of restrictive chromatin structures at the viral long terminal repeat drives the progressive entry of HIV into latency
    • Pearson R, Kim YK, Hokello J, Lassen K, Friedman J, et al. (2008) Epigenetic silencing of human immunodeficiency virus (HIV) transcription by formation of restrictive chromatin structures at the viral long terminal repeat drives the progressive entry of HIV into latency. J Virol 82: 12291-12303.
    • (2008) J Virol , vol.82 , pp. 12291-12303
    • Pearson, R.1    Kim, Y.K.2    Hokello, J.3    Lassen, K.4    Friedman, J.5
  • 25
    • 33846536395 scopus 로고    scopus 로고
    • Recruitment of chromatin-modifying enzymes by CTIP2 promotes HIV-1 transcriptional silencing
    • Marban C, Suzanne S, Dequiedt F, de Walque S, Redel L, et al. (2007) Recruitment of chromatin-modifying enzymes by CTIP2 promotes HIV-1 transcriptional silencing. EMBO J 26: 412-423.
    • (2007) EMBO J , vol.26 , pp. 412-423
    • Marban, C.1    Suzanne, S.2    Dequiedt, F.3    de Walque, S.4    Redel, L.5
  • 26
    • 80052287096 scopus 로고    scopus 로고
    • Epigenetic silencing of HIV-1 by the Histone H3 lysine 27 Methyltransferase Enhancer of Zeste 2 (EZH2)
    • Friedman J, Cho WK, Chu CK, Keedy KS, Archin NM, et al. (2011) Epigenetic silencing of HIV-1 by the Histone H3 lysine 27 Methyltransferase Enhancer of Zeste 2 (EZH2). J Virol 85: 9078-9089.
    • (2011) J Virol , vol.85 , pp. 9078-9089
    • Friedman, J.1    Cho, W.K.2    Chu, C.K.3    Keedy, K.S.4    Archin, N.M.5
  • 27
    • 77953313393 scopus 로고    scopus 로고
    • Establishment of HIV latency in primary CD4+ cells is due to epigenetic transcriptional silencing and P-TEFb restriction
    • Tyagi M, Pearson RJ, Karn J, (2010) Establishment of HIV latency in primary CD4+ cells is due to epigenetic transcriptional silencing and P-TEFb restriction. J Virol 84: 6425-6437.
    • (2010) J Virol , vol.84 , pp. 6425-6437
    • Tyagi, M.1    Pearson, R.J.2    Karn, J.3
  • 30
    • 2942586974 scopus 로고    scopus 로고
    • Coaxing HIV-1 from resting CD4 T cells: histone deacetylase inhibition allows latent viral expression
    • Ylisastigui L, Archin NM, Lehrman G, Bosch RJ, Margolis DM, (2004) Coaxing HIV-1 from resting CD4 T cells: histone deacetylase inhibition allows latent viral expression. Aids 18: 1101-1108.
    • (2004) Aids , vol.18 , pp. 1101-1108
    • Ylisastigui, L.1    Archin, N.M.2    Lehrman, G.3    Bosch, R.J.4    Margolis, D.M.5
  • 31
    • 33747605357 scopus 로고    scopus 로고
    • Recruitment of TFIIH to the HIV LTR is a rate-limiting step in the emergence of HIV from latency
    • Kim YK, Bourgeois CF, Pearson R, Tyagi M, West MJ, et al. (2006) Recruitment of TFIIH to the HIV LTR is a rate-limiting step in the emergence of HIV from latency. EMBO J 25: 3596-3604.
    • (2006) EMBO J , vol.25 , pp. 3596-3604
    • Kim, Y.K.1    Bourgeois, C.F.2    Pearson, R.3    Tyagi, M.4    West, M.J.5
  • 32
    • 34249810678 scopus 로고    scopus 로고
    • Sustained induction of NF-kappaB is required for efficient expression of latent human immunodeficiency virus type 1
    • Williams SA, Kwon H, Chen LF, Greene WC, (2007) Sustained induction of NF-kappaB is required for efficient expression of latent human immunodeficiency virus type 1. J Virol 81: 6043-6056.
    • (2007) J Virol , vol.81 , pp. 6043-6056
    • Williams, S.A.1    Kwon, H.2    Chen, L.F.3    Greene, W.C.4
  • 33
    • 59449101108 scopus 로고    scopus 로고
    • Induction of HIV-1 latency and reactivation in primary memory CD4+ T cells
    • Bosque A, Planelles V, (2008) Induction of HIV-1 latency and reactivation in primary memory CD4+ T cells. Blood 113: 58-65.
    • (2008) Blood , vol.113 , pp. 58-65
    • Bosque, A.1    Planelles, V.2
  • 34
    • 0030939152 scopus 로고    scopus 로고
    • The T cell activation factor NF-ATc positively regulates HIV-1 replication and gene expression in T cells
    • Kinoshita S, Su L, Amano M, Timmerman LA, Kaneshima H, et al. (1997) The T cell activation factor NF-ATc positively regulates HIV-1 replication and gene expression in T cells. Immunity 6: 235-244.
    • (1997) Immunity , vol.6 , pp. 235-244
    • Kinoshita, S.1    Su, L.2    Amano, M.3    Timmerman, L.A.4    Kaneshima, H.5
  • 35
    • 0031743948 scopus 로고    scopus 로고
    • Tat-associated kinase, TAK, activity is regulated by distinct mechanisms in peripheral blood lymphocytes and promonocytic cell lines
    • Herrmann CH, Carroll RG, Wei P, Jones KA, Rice AP, (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
  • 36
    • 73149118502 scopus 로고    scopus 로고
    • Characterization of Cdk9 T-loop phosphorylation in resting and activated CD4(+) T lymphocytes
    • Ramakrishnan R, Dow EC, Rice AP, (2009) Characterization of Cdk9 T-loop phosphorylation in resting and activated CD4(+) T lymphocytes. J Leukoc Biol 86: 1345-1350.
    • (2009) J Leukoc Biol , vol.86 , pp. 1345-1350
    • Ramakrishnan, R.1    Dow, E.C.2    Rice, A.P.3
  • 37
    • 81755184665 scopus 로고    scopus 로고
    • Cdk9 T-loop phosphorylation is regulated by the calcium signaling pathway
    • Ramakrishnan R, Rice AP, (2011) Cdk9 T-loop phosphorylation is regulated by the calcium signaling pathway. J Cell Physiol 227: 609-617.
    • (2011) J Cell Physiol , vol.227 , pp. 609-617
    • Ramakrishnan, R.1    Rice, A.P.2
  • 38
    • 84857932569 scopus 로고    scopus 로고
    • Regulation of Cyclin T1 and HIV-1 Replication by MicroRNAs in Resting CD4+ T Lymphocytes
    • Chiang K, Sung TL, Rice AP, (2012) Regulation of Cyclin T1 and HIV-1 Replication by MicroRNAs in Resting CD4+ T Lymphocytes. J Virol 86: 3244-3252.
    • (2012) J Virol , vol.86 , pp. 3244-3252
    • Chiang, K.1    Sung, T.L.2    Rice, A.P.3
  • 39
    • 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 ME, Fang S-M, Fischer WH, Jones KA, (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
  • 40
    • 0033574077 scopus 로고    scopus 로고
    • Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T
    • Fujinaga K, Taube R, Wimmer J, Cujec TP, Peterlin BM, (1999) Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T. Proc Natl Acad Sci U S A 96: 1285-1290.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 1285-1290
    • Fujinaga, K.1    Taube, R.2    Wimmer, J.3    Cujec, T.P.4    Peterlin, B.M.5
  • 41
    • 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 PD, Grdina TA, Bogerd HP, Cullen BR, (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
  • 42
    • 0036275982 scopus 로고    scopus 로고
    • Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation
    • Kim YK, Bourgeois CF, Isel C, Churcher MJ, Karn J, (2002) Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation. Mol Cell Biol 22: 4622-4637.
    • (2002) Mol Cell Biol , vol.22 , pp. 4622-4637
    • Kim, Y.K.1    Bourgeois, C.F.2    Isel, C.3    Churcher, M.J.4    Karn, J.5
  • 43
    • 0033618442 scopus 로고    scopus 로고
    • Direct evidence that HIV-1 Tat activates the Tat-associated kinase (TAK) during transcriptional elongation
    • Isel C, Karn J, (1999) Direct evidence that HIV-1 Tat activates the Tat-associated kinase (TAK) during transcriptional elongation. J Mol Biol 290: 929-941.
    • (1999) J Mol Biol , vol.290 , pp. 929-941
    • Isel, C.1    Karn, J.2
  • 44
    • 0029956642 scopus 로고    scopus 로고
    • Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain
    • Parada CA, Roeder RG, (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
  • 45
    • 0026064723 scopus 로고
    • HIV-1 Tat protein promotes formation of more-processive elongation complexes
    • Marciniak RA, Sharp PA, (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
  • 46
    • 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, et al. (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
  • 47
    • 0036150085 scopus 로고    scopus 로고
    • Spt5 cooperates with Tat by preventing premature RNA release at terminator sequences
    • Bourgeois CF, Kim YK, Churcher MJ, West MJ, Karn J, (2002) Spt5 cooperates with Tat by preventing premature RNA release at terminator sequences. Mol Cell Biol 22: 1079-1093.
    • (2002) Mol Cell Biol , vol.22 , pp. 1079-1093
    • Bourgeois, C.F.1    Kim, Y.K.2    Churcher, M.J.3    West, M.J.4    Karn, J.5
  • 48
    • 30744449491 scopus 로고    scopus 로고
    • P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation
    • Yamada T, Yamaguchi Y, Inukai N, Okamoto S, Mura T, et al. (2006) P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation. Mol Cell 21: 227-237.
    • (2006) Mol Cell , vol.21 , pp. 227-237
    • Yamada, T.1    Yamaguchi, Y.2    Inukai, N.3    Okamoto, S.4    Mura, T.5
  • 49
    • 77951959240 scopus 로고    scopus 로고
    • HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription
    • He N, Liu M, Hsu J, Xue Y, Chou S, et al. (2010) HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription. Mol Cell 38: 428-438.
    • (2010) Mol Cell , vol.38 , pp. 428-438
    • He, N.1    Liu, M.2    Hsu, J.3    Xue, Y.4    Chou, S.5
  • 50
    • 77951954237 scopus 로고    scopus 로고
    • HIV-1 Tat assembles a multifunctional transcription elongation complex and stably associates with the 7SK snRNP
    • Sobhian B, Laguette N, Yatim A, Nakamura M, Levy Y, et al. (2010) HIV-1 Tat assembles a multifunctional transcription elongation complex and stably associates with the 7SK snRNP. Mol Cell 38: 439-451.
    • (2010) Mol Cell , vol.38 , pp. 439-451
    • Sobhian, B.1    Laguette, N.2    Yatim, A.3    Nakamura, M.4    Levy, Y.5
  • 52
    • 84860774174 scopus 로고    scopus 로고
    • The Ubiquitin Ligase Siah1 Controls ELL2 Stability and Formation of Super Elongation Complexes to Modulate Gene Transcription
    • Liu M, Hsu J, Chan C, Li Z, Zhou Q, (2012) The Ubiquitin Ligase Siah1 Controls ELL2 Stability and Formation of Super Elongation Complexes to Modulate Gene Transcription. Molecular cell 46: 325-334.
    • (2012) Molecular Cell , vol.46 , pp. 325-334
    • Liu, M.1    Hsu, J.2    Chan, C.3    Li, Z.4    Zhou, Q.5
  • 53
    • 79960342414 scopus 로고    scopus 로고
    • T-Cell Receptor Signaling Enhances Transcriptional Elongation from Latent HIV Proviruses by Activating P-TEFb through an ERK-Dependent Pathway
    • Kim YK, Mbonye U, Hokello J, Karn J, (2011) T-Cell Receptor Signaling Enhances Transcriptional Elongation from Latent HIV Proviruses by Activating P-TEFb through an ERK-Dependent Pathway. Journal of molecular biology 410: 896-916.
    • (2011) Journal of Molecular Biology , vol.410 , pp. 896-916
    • Kim, Y.K.1    Mbonye, U.2    Hokello, J.3    Karn, J.4
  • 54
    • 0031942998 scopus 로고    scopus 로고
    • Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter
    • El Kharroubi A, Piras G, Zensen R, Martin MA, (1998) Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. Mol Cell Biol 18: 2535-2544.
    • (1998) Mol Cell Biol , vol.18 , pp. 2535-2544
    • El Kharroubi, A.1    Piras, G.2    Zensen, R.3    Martin, M.A.4
  • 55
    • 33646130853 scopus 로고    scopus 로고
    • Requirement for SWI/SNF chromatin-remodeling complex in Tat-mediated activation of the HIV-1 promoter
    • Treand C, du Chene I, Bres V, Kiernan R, Benarous R, et al. (2006) Requirement for SWI/SNF chromatin-remodeling complex in Tat-mediated activation of the HIV-1 promoter. EMBO J 25: 1690-1699.
    • (2006) EMBO J , vol.25 , pp. 1690-1699
    • Treand, C.1    du Chene, I.2    Bres, V.3    Kiernan, R.4    Benarous, R.5
  • 56
    • 82455219436 scopus 로고    scopus 로고
    • Repressive LTR nucleosome positioning by the BAF complex is required for HIV latency
    • Rafati H, Parra M, Hakre S, Moshkin Y, Verdin E, et al. (2011) Repressive LTR nucleosome positioning by the BAF complex is required for HIV latency. PLoS biology 9: e1001206.
    • (2011) PLoS Biology , vol.9
    • Rafati, H.1    Parra, M.2    Hakre, S.3    Moshkin, Y.4    Verdin, E.5
  • 57
    • 0033529635 scopus 로고    scopus 로고
    • A role for the TFIIH XPB DNA helicase in promoter escape by RNA polymerase II
    • Moreland RJ, Tirode F, Yan Q, Conaway JW, Egly J-M, et al. (1999) A role for the TFIIH XPB DNA helicase in promoter escape by RNA polymerase II. J Biol Chem 274: 22127-22130.
    • (1999) J Biol Chem , vol.274 , pp. 22127-22130
    • Moreland, R.J.1    Tirode, F.2    Yan, Q.3    Conaway, J.W.4    Egly, J.-M.5
  • 58
    • 0033515521 scopus 로고    scopus 로고
    • NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
    • Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, et al. (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
  • 59
    • 0033583290 scopus 로고    scopus 로고
    • Structure and function of the human transcription elongation factor DSIF
    • Yamaguchi Y, Wada T, Watanabe D, Takagi T, Hasegawa J, et al. (1999) Structure and function of the human transcription elongation factor DSIF. J Biol Chem 274: 8085-8092.
    • (1999) J Biol Chem , vol.274 , pp. 8085-8092
    • Yamaguchi, Y.1    Wada, T.2    Watanabe, D.3    Takagi, T.4    Hasegawa, J.5
  • 60
    • 0036232590 scopus 로고    scopus 로고
    • Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA
    • Yamaguchi Y, Inukai N, Narita T, Wada T, Handa H, (2002) Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA. Mol Cell Biol 22: 2918-2927.
    • (2002) Mol Cell Biol , vol.22 , pp. 2918-2927
    • Yamaguchi, Y.1    Inukai, N.2    Narita, T.3    Wada, T.4    Handa, H.5
  • 61
    • 34447122581 scopus 로고    scopus 로고
    • Negative elongation factor NELF represses human immunodeficiency virus transcription by pausing the RNA polymerase II complex
    • Zhang Z, Klatt A, Gilmour DS, Henderson AJ, (2007) Negative elongation factor NELF represses human immunodeficiency virus transcription by pausing the RNA polymerase II complex. J Biol Chem 282: 16981-16988.
    • (2007) J Biol Chem , vol.282 , pp. 16981-16988
    • Zhang, Z.1    Klatt, A.2    Gilmour, D.S.3    Henderson, A.J.4
  • 62
    • 0035891288 scopus 로고    scopus 로고
    • 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
    • Nguyen VT, Kiss T, Michels AA, 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
  • 63
    • 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
  • 64
    • 0242361319 scopus 로고    scopus 로고
    • Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA
    • Yik JH, Chen R, Nishimura R, Jennings JL, Link AJ, et al. (2003) Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA. Mol Cell 12: 971-982.
    • (2003) Mol Cell , vol.12 , pp. 971-982
    • Yik, J.H.1    Chen, R.2    Nishimura, R.3    Jennings, J.L.4    Link, A.J.5
  • 65
    • 0038111978 scopus 로고    scopus 로고
    • MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner
    • Michels AA, Nguyen M, Fraldi A, Labas V, Edwards M, et al. (2003) MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner. Mol Cell Biol 23: 4859-4869.
    • (2003) Mol Cell Biol , vol.23 , pp. 4859-4869
    • Michels, A.A.1    Nguyen, M.2    Fraldi, A.3    Labas, V.4    Edwards, M.5
  • 66
    • 23344437022 scopus 로고    scopus 로고
    • Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
    • Li Q, Price JP, Byers SA, Cheng D, Peng J, et al. (2005) Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186. J Biol Chem 280: 28819-28826.
    • (2005) J Biol Chem , vol.280 , pp. 28819-28826
    • Li, Q.1    Price, J.P.2    Byers, S.A.3    Cheng, D.4    Peng, J.5
  • 67
    • 77449119756 scopus 로고    scopus 로고
    • A capping-independent function of MePCE in stabilizing 7SK snRNA and facilitating the assembly of 7SK snRNP
    • Xue Y, Yang Z, Chen R, Zhou Q, (2010) A capping-independent function of MePCE in stabilizing 7SK snRNA and facilitating the assembly of 7SK snRNP. Nucleic Acids Res 38: 360-369.
    • (2010) Nucleic Acids Res , vol.38 , pp. 360-369
    • Xue, Y.1    Yang, Z.2    Chen, R.3    Zhou, Q.4
  • 68
    • 44649135099 scopus 로고    scopus 로고
    • The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes
    • Markert A, Grimm M, Martinez J, Wiesner J, Meyerhans A, et al. (2008) The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes. EMBO Rep 9: 569-575.
    • (2008) EMBO Rep , vol.9 , pp. 569-575
    • Markert, A.1    Grimm, M.2    Martinez, J.3    Wiesner, J.4    Meyerhans, A.5
  • 69
    • 1042289789 scopus 로고    scopus 로고
    • Phosphorylated positive transcription elongation factor b (P-TEFb) is tagged for inhibition through association with 7SK snRNA
    • Chen R, Yang Z, Zhou Q, (2004) Phosphorylated positive transcription elongation factor b (P-TEFb) is tagged for inhibition through association with 7SK snRNA. J Biol Chem 279: 4153-4160.
    • (2004) J Biol Chem , vol.279 , pp. 4153-4160
    • Chen, R.1    Yang, Z.2    Zhou, Q.3
  • 70
    • 44149117974 scopus 로고    scopus 로고
    • PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling
    • Chen R, Liu M, Li H, Xue Y, Ramey WN, et al. (2008) PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling. Genes Dev 22: 1356-1368.
    • (2008) Genes Dev , vol.22 , pp. 1356-1368
    • Chen, R.1    Liu, M.2    Li, H.3    Xue, Y.4    Ramey, W.N.5
  • 71
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo AA, Jeffrey PD, Pavletich NP, (1996) Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol 3: 696-700.
    • (1996) Nat Struct Biol , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 72
    • 84871977941 scopus 로고    scopus 로고
    • Cyclin T1 and CDK9 T-loop phosphorylation are downregulated during establishment of HIV-1 latency in primary resting memory CD4+ T cells
    • Budhiraja S, Famiglietti M, Bosque A, Planelles V, Rice AP, (2012) Cyclin T1 and CDK9 T-loop phosphorylation are downregulated during establishment of HIV-1 latency in primary resting memory CD4+ T cells. J Virol 87: 1211-1220.
    • (2012) J Virol , vol.87 , pp. 1211-1220
    • Budhiraja, S.1    Famiglietti, M.2    Bosque, A.3    Planelles, V.4    Rice, A.P.5
  • 73
    • 77952485555 scopus 로고    scopus 로고
    • T-loop phosphorylated Cdk9 localizes to nuclear speckle domains which may serve as sites of active P-TEFb function and exchange between the Brd4 and 7SK/HEXIM1 regulatory complexes
    • Dow EC, Liu H, Rice AP, (2010) T-loop phosphorylated Cdk9 localizes to nuclear speckle domains which may serve as sites of active P-TEFb function and exchange between the Brd4 and 7SK/HEXIM1 regulatory complexes. J Cell Physiol 224: 84-93.
    • (2010) J Cell Physiol , vol.224 , pp. 84-93
    • Dow, E.C.1    Liu, H.2    Rice, A.P.3
  • 74
    • 34247874793 scopus 로고    scopus 로고
    • Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription
    • Barboric M, Yik JH, Czudnochowski N, Yang Z, Chen R, et al. (2007) Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription. Nucleic Acids Res 35: 2003-2012.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2003-2012
    • Barboric, M.1    Yik, J.H.2    Czudnochowski, N.3    Yang, Z.4    Chen, R.5
  • 75
    • 34547850648 scopus 로고    scopus 로고
    • Manipulation of P-TEFb control machinery by HIV: recruitment of P-TEFb from the large form by Tat and binding of HEXIM1 to TAR
    • Sedore SC, Byers SA, Biglione S, Price JP, Maury WJ, et al. (2007) Manipulation of P-TEFb control machinery by HIV: recruitment of P-TEFb from the large form by Tat and binding of HEXIM1 to TAR. Nucleic Acids Res 35: 4347-4358.
    • (2007) Nucleic Acids Res , vol.35 , pp. 4347-4358
    • Sedore, S.C.1    Byers, S.A.2    Biglione, S.3    Price, J.P.4    Maury, W.J.5
  • 76
    • 77954383344 scopus 로고    scopus 로고
    • RNA-mediated displacement of an inhibitory snRNP complex activates transcription elongation
    • D'Orso I, Frankel AD, (2010) RNA-mediated displacement of an inhibitory snRNP complex activates transcription elongation. Nat Struct Mol Biol 17: 815-821.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 815-821
    • D'Orso, I.1    Frankel, A.D.2
  • 77
    • 77957880315 scopus 로고    scopus 로고
    • The mechanism of release of P-TEFb and HEXIM1 from the 7SK snRNP by viral and cellular activators includes a conformational change in 7SK
    • Krueger BJ, Varzavand K, Cooper JJ, Price DH, (2010) The mechanism of release of P-TEFb and HEXIM1 from the 7SK snRNP by viral and cellular activators includes a conformational change in 7SK. PLoS One 5: e12335.
    • (2010) PLoS One , vol.5
    • Krueger, B.J.1    Varzavand, K.2    Cooper, J.J.3    Price, D.H.4
  • 80
    • 23744467035 scopus 로고    scopus 로고
    • Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4
    • Yang Z, Yik JH, Chen R, He N, Jang MK, et al. (2005) Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4. Mol Cell 19: 535-545.
    • (2005) Mol Cell , vol.19 , pp. 535-545
    • Yang, Z.1    Yik, J.H.2    Chen, R.3    He, N.4    Jang, M.K.5
  • 81
    • 67349221027 scopus 로고    scopus 로고
    • Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells
    • Cho S, Schroeder S, Kaehlcke K, Kwon HS, Pedal A, et al. (2009) Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells. EMBO J 28: 1407-1417.
    • (2009) EMBO J , vol.28 , pp. 1407-1417
    • Cho, S.1    Schroeder, S.2    Kaehlcke, K.3    Kwon, H.S.4    Pedal, A.5
  • 82
    • 80052627807 scopus 로고    scopus 로고
    • Epigenetic displacement of HP1 from heterochromatin by HIV-1 Vpr causes premature sister chromatid separation
    • Shimura M, Toyoda Y, Iijima K, Kinomoto M, Tokunaga K, et al. (2011) Epigenetic displacement of HP1 from heterochromatin by HIV-1 Vpr causes premature sister chromatid separation. The Journal of cell biology 194: 721-735.
    • (2011) The Journal of Cell Biology , vol.194 , pp. 721-735
    • Shimura, M.1    Toyoda, Y.2    Iijima, K.3    Kinomoto, M.4    Tokunaga, K.5
  • 83
    • 46949093191 scopus 로고    scopus 로고
    • The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
    • Baumli S, Lolli G, Lowe ED, Troiani S, Rusconi L, et al. (2008) The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation. EMBO J 27: 1907-1918.
    • (2008) EMBO J , vol.27 , pp. 1907-1918
    • Baumli, S.1    Lolli, G.2    Lowe, E.D.3    Troiani, S.4    Rusconi, L.5
  • 84
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • Jang MK, Mochizuki K, Zhou M, Jeong HS, Brady JN, et al. (2005) The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol Cell 19: 523-534.
    • (2005) Mol Cell , vol.19 , pp. 523-534
    • Jang, M.K.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.S.4    Brady, J.N.5
  • 85
    • 84871725205 scopus 로고    scopus 로고
    • The BET bromodomain inhibitor JQ1 activates HIV latency through antagonizing Brd4 inhibition of Tat-transactivation
    • Li Z, Guo J, Wu Y, Zhou Q, (2013) The BET bromodomain inhibitor JQ1 activates HIV latency through antagonizing Brd4 inhibition of Tat-transactivation. Nucleic acids research 41: 277-287.
    • (2013) Nucleic Acids Research , vol.41 , pp. 277-287
    • Li, Z.1    Guo, J.2    Wu, Y.3    Zhou, Q.4
  • 87
    • 84875525579 scopus 로고    scopus 로고
    • BET bromodomain-targeting compounds reactivate HIV from latency via a Tat-independent mechanism
    • Boehm D, Calvanese V, Dar RD, Xing S, Schroeder S, et al. (2013) BET bromodomain-targeting compounds reactivate HIV from latency via a Tat-independent mechanism. Cell cycle 12: 452-462.
    • (2013) Cell Cycle , vol.12 , pp. 452-462
    • Boehm, D.1    Calvanese, V.2    Dar, R.D.3    Xing, S.4    Schroeder, S.5
  • 89
    • 8644281176 scopus 로고    scopus 로고
    • Sequence variation within the dominant amino terminus epitope affects antibody binding and neutralization of human immunodeficiency virus type 1 Tat protein
    • Ruckwardt TJ, Tikhonov I, Berg S, Hatfield GS, Chandra A, et al. (2004) Sequence variation within the dominant amino terminus epitope affects antibody binding and neutralization of human immunodeficiency virus type 1 Tat protein. Journal of virology 78: 13190-13196.
    • (2004) Journal of Virology , vol.78 , pp. 13190-13196
    • Ruckwardt, T.J.1    Tikhonov, I.2    Berg, S.3    Hatfield, G.S.4    Chandra, A.5
  • 90
    • 0345086416 scopus 로고    scopus 로고
    • Degradation of ZAP-70 following antigenic stimulation in human T lymphocytes: role of calpain proteolytic pathway
    • Penna D, Muller S, Martinon F, Demotz S, Iwashima M, et al. (1999) Degradation of ZAP-70 following antigenic stimulation in human T lymphocytes: role of calpain proteolytic pathway. J Immunol 163: 50-56.
    • (1999) J Immunol , vol.163 , pp. 50-56
    • Penna, D.1    Muller, S.2    Martinon, F.3    Demotz, S.4    Iwashima, M.5
  • 91
    • 1842331510 scopus 로고    scopus 로고
    • Degradation of T cell receptor (TCR)-CD3-zeta complexes after antigenic stimulation
    • Valitutti S, Muller S, Salio M, Lanzavecchia A, (1997) Degradation of T cell receptor (TCR)-CD3-zeta complexes after antigenic stimulation. J Exp Med 185: 1859-1864.
    • (1997) J Exp Med , vol.185 , pp. 1859-1864
    • Valitutti, S.1    Muller, S.2    Salio, M.3    Lanzavecchia, A.4
  • 92
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • Valitutti S, Muller S, Cella M, Padovan E, Lanzavecchia A, (1995) Serial triggering of many T-cell receptors by a few peptide-MHC complexes. Nature 375: 148-151.
    • (1995) Nature , vol.375 , pp. 148-151
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Padovan, E.4    Lanzavecchia, A.5
  • 93
    • 78651509617 scopus 로고    scopus 로고
    • Studies of HIV-1 latency in an ex vivo model that uses primary central memory T cells
    • Bosque A, Planelles V, (2011) Studies of HIV-1 latency in an ex vivo model that uses primary central memory T cells. Methods 53: 54-61.
    • (2011) Methods , vol.53 , pp. 54-61
    • Bosque, A.1    Planelles, V.2
  • 94
    • 35348816030 scopus 로고    scopus 로고
    • Conserved P-TEFb-interacting domain of BRD4 inhibits HIV transcription
    • Bisgrove DA, Mahmoudi T, Henklein P, Verdin E, (2007) Conserved P-TEFb-interacting domain of BRD4 inhibits HIV transcription. Proc Natl Acad Sci U S A 104: 13690-13695.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13690-13695
    • Bisgrove, D.A.1    Mahmoudi, T.2    Henklein, P.3    Verdin, E.4
  • 95
    • 84862911038 scopus 로고    scopus 로고
    • Two-pronged binding with bromodomain-containing protein 4 liberates positive transcription elongation factor b from inactive ribonucleoprotein complexes
    • Schroder S, Cho S, Zeng L, Zhang Q, Kaehlcke K, et al. (2012) Two-pronged binding with bromodomain-containing protein 4 liberates positive transcription elongation factor b from inactive ribonucleoprotein complexes. J Biol Chem 287: 1090-1099.
    • (2012) J Biol Chem , vol.287 , pp. 1090-1099
    • Schroder, S.1    Cho, S.2    Zeng, L.3    Zhang, Q.4    Kaehlcke, K.5
  • 96
    • 84878873135 scopus 로고    scopus 로고
    • Targeting HIV latency: pharmacologic strategies toward eradication
    • doi:10.1016/j.drudis.2012.1012.1008
    • Xing S, Siliciano RF, (2013) Targeting HIV latency: pharmacologic strategies toward eradication. Drug discovery today doi: 10.1016/j.drudis.2012.1012.1008.
    • (2013) Drug Discovery Today
    • Xing, S.1    Siliciano, R.F.2
  • 97
    • 79952739523 scopus 로고    scopus 로고
    • A proteomic study of myosin II motor proteins during tumor cell migration
    • Betapudi V, Gokulrangan G, Chance MR, Egelhoff TT, (2011) A proteomic study of myosin II motor proteins during tumor cell migration. J Mol Biol 407: 673-686.
    • (2011) J Mol Biol , vol.407 , pp. 673-686
    • Betapudi, V.1    Gokulrangan, G.2    Chance, M.R.3    Egelhoff, T.T.4


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