메뉴 건너뛰기




Volumn 161, Issue 2, 2011, Pages 101-114

Host factors mediating HIV-1 replication

Author keywords

Cellular factors; HIV 1 replication; Virus host interactions

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; ADAM10 ENDOPEPTIDASE; BARRIER TO AUTOINTEGRATION FACTOR; CD209 ANTIGEN; CD63 ANTIGEN; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; CYCLOPHILIN A; EMERIN; GALECTIN 1; HEAT SHOCK PROTEIN 70; HIGH MOBILITY GROUP A1B PROTEIN; HIGH MOBILITY GROUP B1 PROTEIN; HISTONE DEACETYLASE 1; KARYOPHERIN; LENS EPITHELIUM DERIVED GROWTH FACTOR; MARAVIROC; MEMBRANE PROTEIN; NUCLEOPORIN; PEPTIDYLPROLYL ISOMERASE PIN1; POLYPEPTIDE; PROTEIN GP340; PROTEIN LAP2 ALPHA; PROTEIN P75; SHORT HAIRPIN RNA; SMALL INTERFERING RNA; SURVIVAL MOTOR NEURON PROTEIN 1; TRANSFER RNA; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

EID: 80053132394     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2011.08.001     Document Type: Review
Times cited : (73)

References (257)
  • 1
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 1999, 18(7):1923-1938.
    • (1999) EMBO J. , vol.18 , Issue.7 , pp. 1923-1938
    • Aagaard, L.1    Laible, G.2    Selenko, P.3    Schmid, M.4    Dorn, R.5    Schotta, G.6    Kuhfittig, S.7    Wolf, A.8    Lebersorger, A.9    Singh, P.B.10    Reuter, G.11    Jenuwein, T.12
  • 3
    • 1542374645 scopus 로고    scopus 로고
    • Expression patterns and different subcellular localization of the growth factors HDGF (hepatoma-derived growth factor) and HRP-3 (HDGF-related protein-3) suggest functions in addition to their mitogenic activity
    • Abouzied M.M., Baader S.L., Dietz F., Kappler J., Gieselmann V., Franken S. Expression patterns and different subcellular localization of the growth factors HDGF (hepatoma-derived growth factor) and HRP-3 (HDGF-related protein-3) suggest functions in addition to their mitogenic activity. Biochem. J 2004, 378(Pt. 1):169-176.
    • (2004) Biochem. J , vol.378 , Issue.PART. 1 , pp. 169-176
    • Abouzied, M.M.1    Baader, S.L.2    Dietz, F.3    Kappler, J.4    Gieselmann, V.5    Franken, S.6
  • 4
    • 0034666051 scopus 로고    scopus 로고
    • Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex
    • Agostini I., Popov S., Li J., Dubrovsky L., Hao T., Bukrinsky M. Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. Exp. Cell Res. 2000, 259(2):398-403.
    • (2000) Exp. Cell Res. , vol.259 , Issue.2 , pp. 398-403
    • Agostini, I.1    Popov, S.2    Li, J.3    Dubrovsky, L.4    Hao, T.5    Bukrinsky, M.6
  • 5
    • 34748852513 scopus 로고    scopus 로고
    • Blocking interactions between HIV-1 integrase and cellular cofactors: an emerging anti-retroviral strategy
    • Al-Mawsawi L.Q., Neamati N. Blocking interactions between HIV-1 integrase and cellular cofactors: an emerging anti-retroviral strategy. Trends Pharmacol. Sci. 2007, 28(10):526-535.
    • (2007) Trends Pharmacol. Sci. , vol.28 , Issue.10 , pp. 526-535
    • Al-Mawsawi, L.Q.1    Neamati, N.2
  • 6
    • 0034665624 scopus 로고    scopus 로고
    • Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding
    • Angelov D., Charra M., Seve M., Cote J., Khochbin S., Dimitrov S. Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding. J. Mol. Biol. 2000, 302(2):315-326.
    • (2000) J. Mol. Biol. , vol.302 , Issue.2 , pp. 315-326
    • Angelov, D.1    Charra, M.2    Seve, M.3    Cote, J.4    Khochbin, S.5    Dimitrov, S.6
  • 8
    • 34250369626 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 integrase with cellular nuclear import receptor importin 7 and its impact on viral replication
    • Ao Z., Huang G., Yao H., Xu Z., Labine M., Cochrane A.W., Yao X. Interaction of human immunodeficiency virus type 1 integrase with cellular nuclear import receptor importin 7 and its impact on viral replication. J. Biol. Chem. 2007, 282(18):13456-13467.
    • (2007) J. Biol. Chem. , vol.282 , Issue.18 , pp. 13456-13467
    • Ao, Z.1    Huang, G.2    Yao, H.3    Xu, Z.4    Labine, M.5    Cochrane, A.W.6    Yao, X.7
  • 9
    • 78349297963 scopus 로고    scopus 로고
    • Revisiting HIV-1 uncoating
    • Arhel N. Revisiting HIV-1 uncoating. Retrovirology 2010, 7:96.
    • (2010) Retrovirology , vol.7 , pp. 96
    • Arhel, N.1
  • 10
    • 0033972923 scopus 로고    scopus 로고
    • How do Rab proteins function in membrane traffic?
    • Armstrong J. How do Rab proteins function in membrane traffic?. Int. J. Biochem. Cell Biol. 2000, 32(3):303-307.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , Issue.3 , pp. 303-307
    • Armstrong, J.1
  • 12
    • 0033548084 scopus 로고    scopus 로고
    • Role of post-transcriptional modifications of primer tRNALys,3 in the fidelity and efficacy of plus strand DNA transfer during HIV-1 reverse transcription
    • Auxilien S., Keith G., Le Grice S.F., Darlix J.L. Role of post-transcriptional modifications of primer tRNALys,3 in the fidelity and efficacy of plus strand DNA transfer during HIV-1 reverse transcription. J. Biol. Chem. 1999, 274(7):4412-4420.
    • (1999) J. Biol. Chem. , vol.274 , Issue.7 , pp. 4412-4420
    • Auxilien, S.1    Keith, G.2    Le Grice, S.F.3    Darlix, J.L.4
  • 13
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst M., Odorizzi G., Estepa E.J., Emr S.D. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 2000, 1(3):248-258.
    • (2000) Traffic , vol.1 , Issue.3 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 15
    • 0034525907 scopus 로고    scopus 로고
    • A rab1 GTPase is required for transport between the endoplasmic reticulum and Golgi apparatus and for normal Golgi movement in plants
    • Batoko H., Zheng H.Q., Hawes C., Moore I. A rab1 GTPase is required for transport between the endoplasmic reticulum and Golgi apparatus and for normal Golgi movement in plants. Plant Cell 2000, 12(11):2201-2218.
    • (2000) Plant Cell , vol.12 , Issue.11 , pp. 2201-2218
    • Batoko, H.1    Zheng, H.Q.2    Hawes, C.3    Moore, I.4
  • 17
    • 0031957171 scopus 로고    scopus 로고
    • Patterns of CCR5, CXCR4, and CCR3 usage by envelope glycoproteins from human immunodeficiency virus type 1 primary isolates
    • Bazan H.A., Alkhatib G., Broder C.C., Berger E.A. Patterns of CCR5, CXCR4, and CCR3 usage by envelope glycoproteins from human immunodeficiency virus type 1 primary isolates. J. Virol. 1998, 72(5):4485-4491.
    • (1998) J. Virol. , vol.72 , Issue.5 , pp. 4485-4491
    • Bazan, H.A.1    Alkhatib, G.2    Broder, C.C.3    Berger, E.A.4
  • 18
    • 0028955712 scopus 로고
    • The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif
    • Beddow A.L., Richards S.A., Orem N.R., Macara I.G. The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif. Proc. Natl. Acad. Sci. U. S. A. 1995, 92(8):3328-3332.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , Issue.8 , pp. 3328-3332
    • Beddow, A.L.1    Richards, S.A.2    Orem, N.R.3    Macara, I.G.4
  • 19
    • 33645292647 scopus 로고    scopus 로고
    • Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32
    • Berro R., Kehn K., de la Fuente C., Pumfery A., Adair R., Wade J., Colberg-Poley A.M., Hiscott J., Kashanchi F. Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32. J. Virol. 2006, 80(7):3189-3204.
    • (2006) J. Virol. , vol.80 , Issue.7 , pp. 3189-3204
    • Berro, R.1    Kehn, K.2    de la Fuente, C.3    Pumfery, A.4    Adair, R.5    Wade, J.6    Colberg-Poley, A.M.7    Hiscott, J.8    Kashanchi, F.9
  • 21
    • 0031710231 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1
    • Bogerd H.P., Echarri A., Ross T.M., Cullen B.R. Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1. J. Virol. 1998, 72(11):8627-8635.
    • (1998) J. Virol. , vol.72 , Issue.11 , pp. 8627-8635
    • Bogerd, H.P.1    Echarri, A.2    Ross, T.M.3    Cullen, B.R.4
  • 23
    • 70350536784 scopus 로고    scopus 로고
    • Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling
    • Bozkulak E.C., Weinmaster G. Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling. Mol. Cell. Biol. 2009, 29(21):5679-5695.
    • (2009) Mol. Cell. Biol. , vol.29 , Issue.21 , pp. 5679-5695
    • Bozkulak, E.C.1    Weinmaster, G.2
  • 25
    • 77951470419 scopus 로고    scopus 로고
    • Role of human immunodeficiency virus type 1 integrase in uncoating of the viral core
    • Briones M.S., Dobard C.W., Chow S.A. Role of human immunodeficiency virus type 1 integrase in uncoating of the viral core. J. Virol. 2010, 84(10):5181-5190.
    • (2010) J. Virol. , vol.84 , Issue.10 , pp. 5181-5190
    • Briones, M.S.1    Dobard, C.W.2    Chow, S.A.3
  • 26
    • 57149086286 scopus 로고    scopus 로고
    • The host cell sulfonation pathway contributes to retroviral infection at a step coincident with provirus establishment
    • Bruce J.W., Ahlquist P., Young J.A. The host cell sulfonation pathway contributes to retroviral infection at a step coincident with provirus establishment. PLoS Pathog. 2008, 4(11):e1000207.
    • (2008) PLoS Pathog. , vol.4 , Issue.11
    • Bruce, J.W.1    Ahlquist, P.2    Young, J.A.3
  • 27
    • 0036202384 scopus 로고    scopus 로고
    • Structural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: comparison with the heat-annealed complex
    • Brule F., Marquet R., Rong L., Wainberg M.A., Roques B.P., Le Grice S.F., Ehresmann B., Ehresmann C. Structural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: comparison with the heat-annealed complex. RNA 2002, 8(1):8-15.
    • (2002) RNA , vol.8 , Issue.1 , pp. 8-15
    • Brule, F.1    Marquet, R.2    Rong, L.3    Wainberg, M.A.4    Roques, B.P.5    Le Grice, S.F.6    Ehresmann, B.7    Ehresmann, C.8
  • 28
    • 0031775745 scopus 로고    scopus 로고
    • Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton
    • Bukrinskaya A., Brichacek B., Mann A., Stevenson M. Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton. J. Exp. Med. 1998, 188(11):2113-2125.
    • (1998) J. Exp. Med. , vol.188 , Issue.11 , pp. 2113-2125
    • Bukrinskaya, A.1    Brichacek, B.2    Mann, A.3    Stevenson, M.4
  • 29
    • 0027381647 scopus 로고
    • Human immunodeficiency virus type 1 2-LTR circles reside in a nucleoprotein complex which is different from the preintegration complex
    • Bukrinsky M., Sharova N., Stevenson M. Human immunodeficiency virus type 1 2-LTR circles reside in a nucleoprotein complex which is different from the preintegration complex. J. Virol. 1993, 67(11):6863-6865.
    • (1993) J. Virol. , vol.67 , Issue.11 , pp. 6863-6865
    • Bukrinsky, M.1    Sharova, N.2    Stevenson, M.3
  • 31
    • 0023913884 scopus 로고
    • Transcription and replication of human immunodeficiency virus-1 in B lymphocytes in vitro
    • Calman A.F., Busch M.P., Vyas G.N., McHugh T.M., Stites D.P., Peterlin B.M. Transcription and replication of human immunodeficiency virus-1 in B lymphocytes in vitro. AIDS 1988, 2(3):185-193.
    • (1988) AIDS , vol.2 , Issue.3 , pp. 185-193
    • Calman, A.F.1    Busch, M.P.2    Vyas, G.N.3    McHugh, T.M.4    Stites, D.P.5    Peterlin, B.M.6
  • 33
    • 0029896047 scopus 로고    scopus 로고
    • HnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins
    • Cartegni L., Maconi M., Morandi E., Cobianchi F., Riva S., Biamonti G. hnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins. J. Mol. Biol. 1996, 259(3):337-348.
    • (1996) J. Mol. Biol. , vol.259 , Issue.3 , pp. 337-348
    • Cartegni, L.1    Maconi, M.2    Morandi, E.3    Cobianchi, F.4    Riva, S.5    Biamonti, G.6
  • 34
    • 0033516642 scopus 로고    scopus 로고
    • Identification of three major phosphorylation sites within HIV-1 capsid Role of phosphorylation during the early steps of infection
    • Cartier C., Sivard P., Tranchat C., Decimo D., Desgranges C., Boyer V. Identification of three major phosphorylation sites within HIV-1 capsid Role of phosphorylation during the early steps of infection. J. Biol. Chem. 1999, 274(27):19434-19440.
    • (1999) J. Biol. Chem. , vol.274 , Issue.27 , pp. 19434-19440
    • Cartier, C.1    Sivard, P.2    Tranchat, C.3    Decimo, D.4    Desgranges, C.5    Boyer, V.6
  • 35
    • 0033027713 scopus 로고    scopus 로고
    • V3 recombinants indicate a central role for CCR5 as a coreceptor in tissue infection by human immunodeficiency virus type 1
    • Chan S.Y., Speck R.F., Power C., Gaffen S.L., Chesebro B., Goldsmith M.A. V3 recombinants indicate a central role for CCR5 as a coreceptor in tissue infection by human immunodeficiency virus type 1. J. Virol. 1999, 73(3):2350-2358.
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 2350-2358
    • Chan, S.Y.1    Speck, R.F.2    Power, C.3    Gaffen, S.L.4    Chesebro, B.5    Goldsmith, M.A.6
  • 36
    • 53849098555 scopus 로고    scopus 로고
    • HIV-1 Nef induces a Rab11-dependent routing of endocytosed immune costimulatory proteins CD80 and CD86 to the Golgi
    • Chaudhry A., Das S.R., Jameel S., George A., Bal V., Mayor S., Rath S. HIV-1 Nef induces a Rab11-dependent routing of endocytosed immune costimulatory proteins CD80 and CD86 to the Golgi. Traffic 2008, 9(11):1925-1935.
    • (2008) Traffic , vol.9 , Issue.11 , pp. 1925-1935
    • Chaudhry, A.1    Das, S.R.2    Jameel, S.3    George, A.4    Bal, V.5    Mayor, S.6    Rath, S.7
  • 37
    • 0032433829 scopus 로고    scopus 로고
    • The barrier-to-autointegration protein is a host factor for HIV type 1 integration
    • Chen H., Engelman A. The barrier-to-autointegration protein is a host factor for HIV type 1 integration. Proc. Natl. Acad. Sci. U. S. A. 1998, 95(26):15270-15274.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.26 , pp. 15270-15274
    • Chen, H.1    Engelman, A.2
  • 38
    • 10344221084 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase
    • Cherepanov P., Devroe E., Silver P.A., Engelman A. Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase. J. Biol. Chem. 2004, 279(47):48883-48892.
    • (2004) J. Biol. Chem. , vol.279 , Issue.47 , pp. 48883-48892
    • Cherepanov, P.1    Devroe, E.2    Silver, P.A.3    Engelman, A.4
  • 40
    • 0035958946 scopus 로고    scopus 로고
    • The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat
    • Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A., Khochbin S. The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat. J. Biol. Chem. 2001, 276(30):28179-28184.
    • (2001) J. Biol. Chem. , vol.276 , Issue.30 , pp. 28179-28184
    • Col, E.1    Caron, C.2    Seigneurin-Berny, D.3    Gracia, J.4    Favier, A.5    Khochbin, S.6
  • 41
    • 0033929108 scopus 로고    scopus 로고
    • The human factors YY1 and LSF repress the human immunodeficiency virus type 1 long terminal repeat via recruitment of histone deacetylase 1
    • Coull J.J., Romerio F., Sun J.M., Volker J.L., Galvin K.M., Davie J.R., Shi Y., Hansen U., Margolis D.M. The human factors YY1 and LSF repress the human immunodeficiency virus type 1 long terminal repeat via recruitment of histone deacetylase 1. J. Virol. 2000, 74(15):6790-6799.
    • (2000) J. Virol. , vol.74 , Issue.15 , pp. 6790-6799
    • Coull, J.J.1    Romerio, F.2    Sun, J.M.3    Volker, J.L.4    Galvin, K.M.5    Davie, J.R.6    Shi, Y.7    Hansen, U.8    Margolis, D.M.9
  • 44
    • 38049086957 scopus 로고    scopus 로고
    • Distinct roles for DC-SIGN+-dendritic cells and Langerhans cells in HIV-1 transmission
    • de Witte L., Nabatov A., Geijtenbeek T.B. Distinct roles for DC-SIGN+-dendritic cells and Langerhans cells in HIV-1 transmission. Trends Mol. Med. 2008, 14(1):12-19.
    • (2008) Trends Mol. Med. , vol.14 , Issue.1 , pp. 12-19
    • de Witte, L.1    Nabatov, A.2    Geijtenbeek, T.B.3
  • 48
    • 0036714175 scopus 로고    scopus 로고
    • The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies
    • Dietz F., Franken S., Yoshida K., Nakamura H., Kappler J., Gieselmann V. The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies. Biochem. J 2002, 366(Pt. 2):491-500.
    • (2002) Biochem. J , vol.366 , Issue.PART. 2 , pp. 491-500
    • Dietz, F.1    Franken, S.2    Yoshida, K.3    Nakamura, H.4    Kappler, J.5    Gieselmann, V.6
  • 49
    • 4744350877 scopus 로고    scopus 로고
    • The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly
    • Dong J., Lai R., Nielsen K., Fekete C.A., Qiu H., Hinnebusch A.G. The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J. Biol. Chem. 2004, 279(40):42157-42168.
    • (2004) J. Biol. Chem. , vol.279 , Issue.40 , pp. 42157-42168
    • Dong, J.1    Lai, R.2    Nielsen, K.3    Fekete, C.A.4    Qiu, H.5    Hinnebusch, A.G.6
  • 51
    • 34247516888 scopus 로고    scopus 로고
    • Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production
    • Dooher J.E., Schneider B.L., Reed J.C., Lingappa J.R. Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production. Traffic 2007, 8(3):195-211.
    • (2007) Traffic , vol.8 , Issue.3 , pp. 195-211
    • Dooher, J.E.1    Schneider, B.L.2    Reed, J.C.3    Lingappa, J.R.4
  • 54
    • 18144426719 scopus 로고    scopus 로고
    • NF-{kappa}B is transported into the nucleus by importin {alpha}3 and importin {alpha}4
    • Fagerlund R., Kinnunen L., Kohler M., Julkunen I., Melen K. NF-{kappa}B is transported into the nucleus by importin {alpha}3 and importin {alpha}4. J. Biol. Chem. 2005, 280(16):15942-15951.
    • (2005) J. Biol. Chem. , vol.280 , Issue.16 , pp. 15942-15951
    • Fagerlund, R.1    Kinnunen, L.2    Kohler, M.3    Julkunen, I.4    Melen, K.5
  • 55
    • 0031004162 scopus 로고    scopus 로고
    • HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro
    • Farnet C.M., Bushman F.D. HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro. Cell 1997, 88(4):483-492.
    • (1997) Cell , vol.88 , Issue.4 , pp. 483-492
    • Farnet, C.M.1    Bushman, F.D.2
  • 56
    • 0041312658 scopus 로고    scopus 로고
    • Nuclear import of HIV-1 intracellular reverse transcription complexes is mediated by importin 7
    • Fassati A., Gorlich D., Harrison I., Zaytseva L., Mingot J.M. Nuclear import of HIV-1 intracellular reverse transcription complexes is mediated by importin 7. EMBO J. 2003, 22(14):3675-3685.
    • (2003) EMBO J. , vol.22 , Issue.14 , pp. 3675-3685
    • Fassati, A.1    Gorlich, D.2    Harrison, I.3    Zaytseva, L.4    Mingot, J.M.5
  • 57
    • 0035966103 scopus 로고    scopus 로고
    • Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress
    • Fatma N., Singh D.P., Shinohara T., Chylack L.T. Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress. J. Biol. Chem. 2001, 276(52):48899-48907.
    • (2001) J. Biol. Chem. , vol.276 , Issue.52 , pp. 48899-48907
    • Fatma, N.1    Singh, D.P.2    Shinohara, T.3    Chylack, L.T.4
  • 60
    • 33847355934 scopus 로고    scopus 로고
    • Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding
    • Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., Hill C.P. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 2007, 128(5):841-852.
    • (2007) Cell , vol.128 , Issue.5 , pp. 841-852
    • Fisher, R.D.1    Chung, H.Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 61
    • 0035313855 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling
    • Flaus A., Owen-Hughes T. Mechanisms for ATP-dependent chromatin remodelling. Curr. Opin. Genet. Dev. 2001, 11(2):148-154.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , Issue.2 , pp. 148-154
    • Flaus, A.1    Owen-Hughes, T.2
  • 62
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R., Gerace L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 1993, 73(7):1267-1279.
    • (1993) Cell , vol.73 , Issue.7 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 63
    • 2342447986 scopus 로고    scopus 로고
    • Importin 7 and importin alpha/importin beta are nuclear import receptors for the glucocorticoid receptor
    • Freedman N.D., Yamamoto K.R. Importin 7 and importin alpha/importin beta are nuclear import receptors for the glucocorticoid receptor. Mol. Biol. Cell 2004, 15(5):2276-2286.
    • (2004) Mol. Biol. Cell , vol.15 , Issue.5 , pp. 2276-2286
    • Freedman, N.D.1    Yamamoto, K.R.2
  • 64
    • 0027165839 scopus 로고
    • Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene
    • Friedmann M., Holth L.T., Zoghbi H.Y., Reeves R. Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene. Nucleic Acids Res. 1993, 21(18):4259-4267.
    • (1993) Nucleic Acids Res. , vol.21 , Issue.18 , pp. 4259-4267
    • Friedmann, M.1    Holth, L.T.2    Zoghbi, H.Y.3    Reeves, R.4
  • 65
    • 78649602770 scopus 로고    scopus 로고
    • Quantitative PCR used to assess HIV-1 integration and 2-LTR circle formation in human macrophages, peripheral blood lymphocytes and a CD4+ cell line
    • Friedrich B., Li G., Dziuba N., Ferguson M.R. Quantitative PCR used to assess HIV-1 integration and 2-LTR circle formation in human macrophages, peripheral blood lymphocytes and a CD4+ cell line. Virol. J. 2010, 7:354.
    • (2010) Virol. J. , vol.7 , pp. 354
    • Friedrich, B.1    Li, G.2    Dziuba, N.3    Ferguson, M.R.4
  • 68
    • 0030987672 scopus 로고    scopus 로고
    • HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway
    • Gallay P., Hope T., Chin D., Trono D. HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway. Proc. Natl. Acad. Sci. U. S. A. 1997, 94(18):9825-9830.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.18 , pp. 9825-9830
    • Gallay, P.1    Hope, T.2    Chin, D.3    Trono, D.4
  • 69
    • 0030065395 scopus 로고    scopus 로고
    • Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import
    • Gallay P., Stitt V., Mundy C., Oettinger M., Trono D. Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. J. Virol. 1996, 70(2):1027-1032.
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 1027-1032
    • Gallay, P.1    Stitt, V.2    Mundy, C.3    Oettinger, M.4    Trono, D.5
  • 74
    • 33745234847 scopus 로고    scopus 로고
    • Cumulative mutations of ubiquitin acceptor sites in human immunodeficiency virus type 1 gag cause a late budding defect
    • Gottwein E., Jager S., Habermann A., Krausslich H.G. Cumulative mutations of ubiquitin acceptor sites in human immunodeficiency virus type 1 gag cause a late budding defect. J. Virol. 2006, 80(13):6267-6275.
    • (2006) J. Virol. , vol.80 , Issue.13 , pp. 6267-6275
    • Gottwein, E.1    Jager, S.2    Habermann, A.3    Krausslich, H.G.4
  • 75
    • 33744938142 scopus 로고    scopus 로고
    • Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines
    • Grigorov B., Arcanger F., Roingeard P., Darlix J.L., Muriaux D. Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines. J. Mol. Biol. 2006, 359(4):848-862.
    • (2006) J. Mol. Biol. , vol.359 , Issue.4 , pp. 848-862
    • Grigorov, B.1    Arcanger, F.2    Roingeard, P.3    Darlix, J.L.4    Muriaux, D.5
  • 76
    • 0037452070 scopus 로고    scopus 로고
    • Microbial pathogenesis and cytoskeletal function
    • Gruenheid S., Finlay B.B. Microbial pathogenesis and cytoskeletal function. Nature 2003, 422(6933):775-781.
    • (2003) Nature , vol.422 , Issue.6933 , pp. 775-781
    • Gruenheid, S.1    Finlay, B.B.2
  • 77
    • 0036311895 scopus 로고    scopus 로고
    • The carboxy-terminal region of the human immunodeficiency virus type 1 protein Rev has multiple roles in mediating CRM1-related Rev functions
    • Hakata Y., Yamada M., Mabuchi N., Shida H. The carboxy-terminal region of the human immunodeficiency virus type 1 protein Rev has multiple roles in mediating CRM1-related Rev functions. J. Virol. 2002, 76(16):8079-8089.
    • (2002) J. Virol. , vol.76 , Issue.16 , pp. 8079-8089
    • Hakata, Y.1    Yamada, M.2    Mabuchi, N.3    Shida, H.4
  • 79
    • 33744908820 scopus 로고    scopus 로고
    • Identification of a novel human immunodeficiency virus type 1 integrase interactor Gemin2, that facilitates efficient viral cDNA synthesis in vivo
    • Hamamoto S., Nishitsuji H., Amagasa T., Kannagi M., Masuda T. Identification of a novel human immunodeficiency virus type 1 integrase interactor Gemin2, that facilitates efficient viral cDNA synthesis in vivo. J. Virol. 2006, 80(12):5670-5677.
    • (2006) J. Virol. , vol.80 , Issue.12 , pp. 5670-5677
    • Hamamoto, S.1    Nishitsuji, H.2    Amagasa, T.3    Kannagi, M.4    Masuda, T.5
  • 80
    • 0021159379 scopus 로고
    • Cyclophilin: a specific cytosolic binding protein for cyclosporin A
    • Handschumacher R.E., Harding M.W., Rice J., Drugge R.J., Speicher D.W. Cyclophilin: a specific cytosolic binding protein for cyclosporin A. Science 1984, 226(4674):544-547.
    • (1984) Science , vol.226 , Issue.4674 , pp. 544-547
    • Handschumacher, R.E.1    Harding, M.W.2    Rice, J.3    Drugge, R.J.4    Speicher, D.W.5
  • 81
    • 0024334173 scopus 로고
    • Role of SP1-binding domains in in vivo transcriptional regulation of the human immunodeficiency virus type 1 long terminal repeat
    • Harrich D., Garcia J., Wu F., Mitsuyasu R., Gonazalez J., Gaynor R. Role of SP1-binding domains in in vivo transcriptional regulation of the human immunodeficiency virus type 1 long terminal repeat. J. Virol. 1989, 63(6):2585-2591.
    • (1989) J. Virol. , vol.63 , Issue.6 , pp. 2585-2591
    • Harrich, D.1    Garcia, J.2    Wu, F.3    Mitsuyasu, R.4    Gonazalez, J.5    Gaynor, R.6
  • 82
    • 0034671508 scopus 로고    scopus 로고
    • Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro
    • Harris D., Engelman A. Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro. J. Biol. Chem. 2000, 275(50):39671-39677.
    • (2000) J. Biol. Chem. , vol.275 , Issue.50 , pp. 39671-39677
    • Harris, D.1    Engelman, A.2
  • 83
    • 63449114891 scopus 로고    scopus 로고
    • Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells
    • Harrist A.V., Ryzhova E.V., Harvey T., Gonzalez-Scarano F. Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells. PLoS One 2009, 4(3):e5020.
    • (2009) PLoS One , vol.4 , Issue.3
    • Harrist, A.V.1    Ryzhova, E.V.2    Harvey, T.3    Gonzalez-Scarano, F.4
  • 84
    • 33748744533 scopus 로고    scopus 로고
    • HIV-1 integrase is capable of targeting DNA to the nucleus via an importin alpha/beta-dependent mechanism
    • Hearps A.C., Jans D.A. HIV-1 integrase is capable of targeting DNA to the nucleus via an importin alpha/beta-dependent mechanism. Biochem. J 2006, 398(3):475-484.
    • (2006) Biochem. J , vol.398 , Issue.3 , pp. 475-484
    • Hearps, A.C.1    Jans, D.A.2
  • 85
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 2005, 6(10):801-811.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , Issue.10 , pp. 801-811
    • Hemler, M.E.1
  • 86
    • 0033760929 scopus 로고    scopus 로고
    • High-mobility-group protein I can modulate binding of transcription factors to the U5 region of the human immunodeficiency virus type 1 proviral promoter
    • Henderson A., Bunce M., Siddon N., Reeves R., Tremethick D.J. High-mobility-group protein I can modulate binding of transcription factors to the U5 region of the human immunodeficiency virus type 1 proviral promoter. J. Virol. 2000, 74(22):10523-10534.
    • (2000) J. Virol. , vol.74 , Issue.22 , pp. 10523-10534
    • Henderson, A.1    Bunce, M.2    Siddon, N.3    Reeves, R.4    Tremethick, D.J.5
  • 87
    • 0346993663 scopus 로고    scopus 로고
    • Recruitment of SWI/SNF to the human immunodeficiency virus type 1 promoter
    • Henderson A., Holloway A., Reeves R., Tremethick D.J. Recruitment of SWI/SNF to the human immunodeficiency virus type 1 promoter. Mol. Cell. Biol. 2004, 24(1):389-397.
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.1 , pp. 389-397
    • Henderson, A.1    Holloway, A.2    Reeves, R.3    Tremethick, D.J.4
  • 89
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L., Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 2003, 19:141-172.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 90
    • 0032740649 scopus 로고    scopus 로고
    • Retroviral DNA integration
    • (table of contents)
    • Hindmarsh P., Leis J. Retroviral DNA integration. Microbiol. Mol. Biol. Rev. 1999, 63(4):836-843. (table of contents).
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , Issue.4 , pp. 836-843
    • Hindmarsh, P.1    Leis, J.2
  • 91
    • 0033052713 scopus 로고    scopus 로고
    • HMG protein family members stimulate human immunodeficiency virus type 1 and avian sarcoma virus concerted DNA integration in vitro
    • Hindmarsh P., Ridky T., Reeves R., Andrake M., Skalka A.M., Leis J. HMG protein family members stimulate human immunodeficiency virus type 1 and avian sarcoma virus concerted DNA integration in vitro. J. Virol. 1999, 73(4):2994-3003.
    • (1999) J. Virol. , vol.73 , Issue.4 , pp. 2994-3003
    • Hindmarsh, P.1    Ridky, T.2    Reeves, R.3    Andrake, M.4    Skalka, A.M.5    Leis, J.6
  • 93
    • 3442894720 scopus 로고    scopus 로고
    • Quantitative detection of promoter hypermethylation of multiple genes in the tumor, urine, and serum DNA of patients with renal cancer
    • Hoque M.O., Begum S., Topaloglu O., Jeronimo C., Mambo E., Westra W.H., Califano J.A., Sidransky D. Quantitative detection of promoter hypermethylation of multiple genes in the tumor, urine, and serum DNA of patients with renal cancer. Cancer Res. 2004, 64(15):5511-5517.
    • (2004) Cancer Res. , vol.64 , Issue.15 , pp. 5511-5517
    • Hoque, M.O.1    Begum, S.2    Topaloglu, O.3    Jeronimo, C.4    Mambo, E.5    Westra, W.H.6    Califano, J.A.7    Sidransky, D.8
  • 95
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: structure and mechanism of a membrane-trafficking network
    • Hurley J.H., Emr S.D. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 2006, 35:277-298.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 96
    • 66849125858 scopus 로고    scopus 로고
    • The nuclear pore component Nup358 promotes transportin-dependent nuclear import
    • Hutten S., Walde S., Spillner C., Hauber J., Kehlenbach R.H. The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Sci. 2009, 122(Pt. 8):1100-1110.
    • (2009) J. Cell Sci. , vol.122 , Issue.PART. 8 , pp. 1100-1110
    • Hutten, S.1    Walde, S.2    Spillner, C.3    Hauber, J.4    Kehlenbach, R.H.5
  • 97
    • 33745248642 scopus 로고    scopus 로고
    • The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity
    • Jacque J.M., Stevenson M. The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity. Nature 2006, 441(7093):641-645.
    • (2006) Nature , vol.441 , Issue.7093 , pp. 641-645
    • Jacque, J.M.1    Stevenson, M.2
  • 98
    • 56349162167 scopus 로고    scopus 로고
    • Dominant negative mutant cyclin T1 proteins that inhibit HIV transcription by forming a kinase inactive complex with Tat
    • Jadlowsky J.K., Nojima M., Okamoto T., Fujinaga K. Dominant negative mutant cyclin T1 proteins that inhibit HIV transcription by forming a kinase inactive complex with Tat. J. Gen. Virol. 2008, 89(Pt. 11):2783-2787.
    • (2008) J. Gen. Virol. , vol.89 , Issue.PART. 11 , pp. 2783-2787
    • Jadlowsky, J.K.1    Nojima, M.2    Okamoto, T.3    Fujinaga, K.4
  • 99
    • 0242582629 scopus 로고    scopus 로고
    • The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1
    • Jakel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., Gorlich D. The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1. EMBO J. 1999, 18(9):2411-2423.
    • (1999) EMBO J. , vol.18 , Issue.9 , pp. 2411-2423
    • Jakel, S.1    Albig, W.2    Kutay, U.3    Bischoff, F.R.4    Schwamborn, K.5    Doenecke, D.6    Gorlich, D.7
  • 100
    • 17844364197 scopus 로고
    • The priming of helper T cells
    • Janeway C.A. The priming of helper T cells. Semin. Immunol. 1989, 1(1):13-20.
    • (1989) Semin. Immunol. , vol.1 , Issue.1 , pp. 13-20
    • Janeway, C.A.1
  • 101
    • 34547105037 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains
    • Jolly C., Sattentau Q.J. Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J. Virol. 2007, 81(15):7873-7884.
    • (2007) J. Virol. , vol.81 , Issue.15 , pp. 7873-7884
    • Jolly, C.1    Sattentau, Q.J.2
  • 102
    • 3242670402 scopus 로고    scopus 로고
    • The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities
    • Keckesova Z., Ylinen L.M., Towers G.J. The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities. Proc. Natl. Acad. Sci. U. S. A. 2004, 101(29):10780-10785.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.29 , pp. 10780-10785
    • Keckesova, Z.1    Ylinen, L.M.2    Towers, G.J.3
  • 103
    • 33646457944 scopus 로고    scopus 로고
    • Cyclophilin A renders human immunodeficiency virus type 1 sensitive to Old World monkey but not human TRIM5 alpha antiviral activity
    • Keckesova Z., Ylinen L.M., Towers G.J. Cyclophilin A renders human immunodeficiency virus type 1 sensitive to Old World monkey but not human TRIM5 alpha antiviral activity. J. Virol. 2006, 80(10):4683-4690.
    • (2006) J. Virol. , vol.80 , Issue.10 , pp. 4683-4690
    • Keckesova, Z.1    Ylinen, L.M.2    Towers, G.J.3
  • 104
    • 0033577860 scopus 로고    scopus 로고
    • A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export
    • Kehlenbach R.H., Dickmanns A., Kehlenbach A., Guan T., Gerace L. A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export. J. Cell Biol. 1999, 145(4):645-657.
    • (1999) J. Cell Biol. , vol.145 , Issue.4 , pp. 645-657
    • Kehlenbach, R.H.1    Dickmanns, A.2    Kehlenbach, A.3    Guan, T.4    Gerace, L.5
  • 105
    • 0842308114 scopus 로고    scopus 로고
    • Sequence analysis of twin ATP binding cassette proteins involved in translational control, antibiotic resistance, and ribonuclease L inhibition
    • Kerr I.D. Sequence analysis of twin ATP binding cassette proteins involved in translational control, antibiotic resistance, and ribonuclease L inhibition. Biochem. Biophys. Res. Commun. 2004, 315(1):166-173.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , Issue.1 , pp. 166-173
    • Kerr, I.D.1
  • 106
    • 74549196267 scopus 로고    scopus 로고
    • Regulation of HIV-1 transcription in cells of the monocyte-macrophage lineage
    • Kilareski E.M., Shah S., Nonnemacher M.R., Wigdahl B. Regulation of HIV-1 transcription in cells of the monocyte-macrophage lineage. Retrovirology 2009, 6:118.
    • (2009) Retrovirology , vol.6 , pp. 118
    • Kilareski, E.M.1    Shah, S.2    Nonnemacher, M.R.3    Wigdahl, B.4
  • 107
    • 0036001161 scopus 로고    scopus 로고
    • TRNA(Lys3): the primer tRNA for reverse transcription in HIV-1
    • Kleiman L. tRNA(Lys3): the primer tRNA for reverse transcription in HIV-1. IUBMB Life 2002, 53(2):107-114.
    • (2002) IUBMB Life , vol.53 , Issue.2 , pp. 107-114
    • Kleiman, L.1
  • 108
    • 70349921798 scopus 로고    scopus 로고
    • SiRNA and shRNA screens advance key understanding of host factors required for HIV-1 replication
    • Kok K.H., Lei T., Jin D.Y. siRNA and shRNA screens advance key understanding of host factors required for HIV-1 replication. Retrovirology 2009, 6:78.
    • (2009) Retrovirology , vol.6 , pp. 78
    • Kok, K.H.1    Lei, T.2    Jin, D.Y.3
  • 109
    • 9444244486 scopus 로고    scopus 로고
    • Inhibiting the Arp2/3 complex limits infection of both intracellular mature vaccinia virus and primate lentiviruses
    • Komano J., Miyauchi K., Matsuda Z., Yamamoto N. Inhibiting the Arp2/3 complex limits infection of both intracellular mature vaccinia virus and primate lentiviruses. Mol. Biol. Cell 2004, 15(12):5197-5207.
    • (2004) Mol. Biol. Cell , vol.15 , Issue.12 , pp. 5197-5207
    • Komano, J.1    Miyauchi, K.2    Matsuda, Z.3    Yamamoto, N.4
  • 111
    • 0030474833 scopus 로고    scopus 로고
    • Activation of the JC virus Tat-responsive transcriptional control element by association of the Tat protein of human immunodeficiency virus 1 with cellular protein Pur alpha
    • Krachmarov C.P., Chepenik L.G., Barr-Vagell S., Khalili K., Johnson E.M. Activation of the JC virus Tat-responsive transcriptional control element by association of the Tat protein of human immunodeficiency virus 1 with cellular protein Pur alpha. Proc. Natl. Acad. Sci. U. S. A. 1996, 93(24):14112-14117.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , Issue.24 , pp. 14112-14117
    • Krachmarov, C.P.1    Chepenik, L.G.2    Barr-Vagell, S.3    Khalili, K.4    Johnson, E.M.5
  • 112
    • 0033828672 scopus 로고    scopus 로고
    • SOCS: physiological suppressors of cytokine signaling
    • Krebs D.L., Hilton D.J. SOCS: physiological suppressors of cytokine signaling. J. Cell Sci. 2000, 113(Pt. 16):2813-2819.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART. 16 , pp. 2813-2819
    • Krebs, D.L.1    Hilton, D.J.2
  • 113
    • 18144430655 scopus 로고    scopus 로고
    • Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication
    • Krishnan V., Zeichner S.L. Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication. Retrovirology 2004, 1:42.
    • (2004) Retrovirology , vol.1 , pp. 42
    • Krishnan, V.1    Zeichner, S.L.2
  • 115
    • 0035575518 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: ran, beta and beyond
    • Kuersten S., Ohno M., Mattaj I.W. Nucleocytoplasmic transport: ran, beta and beyond. Trends Cell Biol. 2001, 11(12):497-503.
    • (2001) Trends Cell Biol. , vol.11 , Issue.12 , pp. 497-503
    • Kuersten, S.1    Ohno, M.2    Mattaj, I.W.3
  • 116
    • 29744464493 scopus 로고    scopus 로고
    • Activation of the ATR pathway by human immunodeficiency virus type 1 Vpr involves its direct binding to chromatin in vivo
    • Lai M., Zimmerman E.S., Planelles V., Chen J. Activation of the ATR pathway by human immunodeficiency virus type 1 Vpr involves its direct binding to chromatin in vivo. J. Virol. 2005, 79(24):15443-15451.
    • (2005) J. Virol. , vol.79 , Issue.24 , pp. 15443-15451
    • Lai, M.1    Zimmerman, E.S.2    Planelles, V.3    Chen, J.4
  • 117
    • 0030425032 scopus 로고    scopus 로고
    • Structural and functional evidence that initiation and elongation of HIV-1 reverse transcription are distinct processes
    • Lanchy J.M., Isel C., Ehresmann C., Marquet R., Ehresmann B. Structural and functional evidence that initiation and elongation of HIV-1 reverse transcription are distinct processes. Biochimie 1996, 78(11-12):1087-1096.
    • (1996) Biochimie , vol.78 , Issue.11-12 , pp. 1087-1096
    • Lanchy, J.M.1    Isel, C.2    Ehresmann, C.3    Marquet, R.4    Ehresmann, B.5
  • 118
    • 0032539631 scopus 로고    scopus 로고
    • A previously unidentified host protein protects retroviral DNA from autointegration
    • Lee M.S., Craigie R. A previously unidentified host protein protects retroviral DNA from autointegration. Proc. Natl. Acad. Sci. U. S. A. 1998, 95(4):1528-1533.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.4 , pp. 1528-1533
    • Lee, M.S.1    Craigie, R.2
  • 120
    • 73149108847 scopus 로고    scopus 로고
    • Inhibition of HIV-1 integrase nuclear import and replication by a peptide bearing integrase putative nuclear localization signal
    • Levin A., Armon-Omer A., Rosenbluh J., Melamed-Book N., Graessmann A., Waigmann E., Loyter A. Inhibition of HIV-1 integrase nuclear import and replication by a peptide bearing integrase putative nuclear localization signal. Retrovirology 2009, 6:112.
    • (2009) Retrovirology , vol.6 , pp. 112
    • Levin, A.1    Armon-Omer, A.2    Rosenbluh, J.3    Melamed-Book, N.4    Graessmann, A.5    Waigmann, E.6    Loyter, A.7
  • 122
    • 77950199793 scopus 로고    scopus 로고
    • The HIV-1 matrix protein p17 activates the transcription factors c-Myc and CREB in human B cells
    • Li S., Bozzo L., Wu Z., Lu W., Romerio F. The HIV-1 matrix protein p17 activates the transcription factors c-Myc and CREB in human B cells. New Microbiol. 2010, 33(1):13-24.
    • (2010) New Microbiol. , vol.33 , Issue.1 , pp. 13-24
    • Li, S.1    Bozzo, L.2    Wu, Z.3    Lu, W.4    Romerio, F.5
  • 123
    • 0032190621 scopus 로고    scopus 로고
    • The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor
    • Li X.Y., Green M.R. The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor. Genes Dev. 1998, 12(19):2992-2996.
    • (1998) Genes Dev. , vol.12 , Issue.19 , pp. 2992-2996
    • Li, X.Y.1    Green, M.R.2
  • 124
    • 70350319201 scopus 로고    scopus 로고
    • Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A
    • Li Y., Kar A.K., Sodroski J. Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A. J. Virol. 2009, 83(21):10951-10962.
    • (2009) J. Virol. , vol.83 , Issue.21 , pp. 10951-10962
    • Li, Y.1    Kar, A.K.2    Sodroski, J.3
  • 125
    • 0032516864 scopus 로고    scopus 로고
    • Mechanistic studies of early pausing events during initiation of HIV-1 reverse transcription
    • Liang C., Rong L., Gotte M., Li X., Quan Y., Kleiman L., Wainberg M.A. Mechanistic studies of early pausing events during initiation of HIV-1 reverse transcription. J. Biol. Chem. 1998, 273(33):21309-21315.
    • (1998) J. Biol. Chem. , vol.273 , Issue.33 , pp. 21309-21315
    • Liang, C.1    Rong, L.2    Gotte, M.3    Li, X.4    Quan, Y.5    Kleiman, L.6    Wainberg, M.A.7
  • 127
    • 0344211405 scopus 로고    scopus 로고
    • The barrier-to-autointegration factor is a component of functional human immunodeficiency virus type 1 preintegration complexes
    • Lin C.W., Engelman A. The barrier-to-autointegration factor is a component of functional human immunodeficiency virus type 1 preintegration complexes. J. Virol. 2003, 77(8):5030-5036.
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 5030-5036
    • Lin, C.W.1    Engelman, A.2
  • 128
    • 35748951311 scopus 로고    scopus 로고
    • ATR pathway is the primary pathway for activating G2/M checkpoint induction after re-replication
    • Lin J.J., Dutta A. ATR pathway is the primary pathway for activating G2/M checkpoint induction after re-replication. J. Biol. Chem. 2007, 282(42):30357-30362.
    • (2007) J. Biol. Chem. , vol.282 , Issue.42 , pp. 30357-30362
    • Lin, J.J.1    Dutta, A.2
  • 130
    • 0032587326 scopus 로고    scopus 로고
    • Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin
    • Liu B., Dai R., Tian C.J., Dawson L., Gorelick R., Yu X.F. Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin. J. Virol. 1999, 73(4):2901-2908.
    • (1999) J. Virol. , vol.73 , Issue.4 , pp. 2901-2908
    • Liu, B.1    Dai, R.2    Tian, C.J.3    Dawson, L.4    Gorelick, R.5    Yu, X.F.6
  • 132
    • 11244255412 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase
    • Llano M., Delgado S., Vanegas M., Poeschla E.M. Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase. J. Biol. Chem. 2004, 279(53):55570-55577.
    • (2004) J. Biol. Chem. , vol.279 , Issue.53 , pp. 55570-55577
    • Llano, M.1    Delgado, S.2    Vanegas, M.3    Poeschla, E.M.4
  • 133
    • 4143092604 scopus 로고    scopus 로고
    • LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes
    • Llano M., Vanegas M., Fregoso O., Saenz D., Chung S., Peretz M., Poeschla E.M. LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes. J. Virol. 2004, 78(17):9524-9537.
    • (2004) J. Virol. , vol.78 , Issue.17 , pp. 9524-9537
    • Llano, M.1    Vanegas, M.2    Fregoso, O.3    Saenz, D.4    Chung, S.5    Peretz, M.6    Poeschla, E.M.7
  • 134
    • 0031016658 scopus 로고    scopus 로고
    • Ran-binding protein 1 (RanBP1) forms a ternary complex with Ran and karyopherin beta and reduces Ran GTPase-activating protein (RanGAP) inhibition by karyopherin beta
    • Lounsbury K.M., Macara I.G. Ran-binding protein 1 (RanBP1) forms a ternary complex with Ran and karyopherin beta and reduces Ran GTPase-activating protein (RanGAP) inhibition by karyopherin beta. J. Biol. Chem. 1997, 272(1):551-555.
    • (1997) J. Biol. Chem. , vol.272 , Issue.1 , pp. 551-555
    • Lounsbury, K.M.1    Macara, I.G.2
  • 135
    • 49649107395 scopus 로고    scopus 로고
    • HIV-1 infection: going nuclear with TNPO3/Transportin-SR2 and integrase
    • Luban J. HIV-1 infection: going nuclear with TNPO3/Transportin-SR2 and integrase. Curr. Biol. 2008, 18(16):R710-R713.
    • (2008) Curr. Biol. , vol.18 , Issue.16
    • Luban, J.1
  • 137
    • 0030812830 scopus 로고    scopus 로고
    • Primer tRNAs for reverse transcription
    • Mak J., Kleiman L. Primer tRNAs for reverse transcription. J. Virol. 1997, 71(11):8087-8095.
    • (1997) J. Virol. , vol.71 , Issue.11 , pp. 8087-8095
    • Mak, J.1    Kleiman, L.2
  • 139
    • 0344736902 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions
    • Mansharamani M., Graham D.R., Monie D., Lee K.K., Hildreth J.E., Siliciano R.F., Wilson K.L. Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions. J. Virol. 2003, 77(24):13084-13092.
    • (2003) J. Virol. , vol.77 , Issue.24 , pp. 13084-13092
    • Mansharamani, M.1    Graham, D.R.2    Monie, D.3    Lee, K.K.4    Hildreth, J.E.5    Siliciano, R.F.6    Wilson, K.L.7
  • 140
    • 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., Van Lint C., Aunis D., Rohr O. Recruitment of chromatin-modifying enzymes by CTIP2 promotes HIV-1 transcriptional silencing. EMBO J. 2007, 26(2):412-423.
    • (2007) EMBO J. , vol.26 , Issue.2 , pp. 412-423
    • Marban, C.1    Suzanne, S.2    Dequiedt, F.3    de Walque, S.4    Redel, L.5    Van Lint, C.6    Aunis, D.7    Rohr, O.8
  • 142
    • 14744280620 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina
    • Margalit A., Segura-Totten M., Gruenbaum Y., Wilson K.L. Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina. Proc. Natl. Acad. Sci. U. S. A. 2005, 102(9):3290-3295.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.9 , pp. 3290-3295
    • Margalit, A.1    Segura-Totten, M.2    Gruenbaum, Y.3    Wilson, K.L.4
  • 143
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano J., Zang T., Bieniasz P.D. Role of ESCRT-I in retroviral budding. J. Virol. 2003, 77(8):4794-4804.
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 144
    • 70349947190 scopus 로고    scopus 로고
    • The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors
    • Mascarenhas A.P., Musier-Forsyth K. The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors. FEBS J. 2009, 276(21):6118-6127.
    • (2009) FEBS J. , vol.276 , Issue.21 , pp. 6118-6127
    • Mascarenhas, A.P.1    Musier-Forsyth, K.2
  • 145
    • 25144431798 scopus 로고    scopus 로고
    • DC-SIGN points the way to a novel mechanism for HIV-1 transmission
    • Masso M. DC-SIGN points the way to a novel mechanism for HIV-1 transmission. MedGenMed 2003, 5(2):2.
    • (2003) MedGenMed , vol.5 , Issue.2 , pp. 2
    • Masso, M.1
  • 146
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda A., Krainer A.R. Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 1992, 68(2):365-375.
    • (1992) Cell , vol.68 , Issue.2 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 147
    • 79952069224 scopus 로고    scopus 로고
    • Dendritic cells and HIV-1 trans-infection
    • McDonald D. Dendritic cells and HIV-1 trans-infection. Viruses 2010, 2(8):1704-1717.
    • (2010) Viruses , vol.2 , Issue.8 , pp. 1704-1717
    • McDonald, D.1
  • 150
    • 37849027311 scopus 로고    scopus 로고
    • Galectin-1 promotes HIV-1 infectivity in macrophages through stabilization of viral adsorption
    • Mercier S., St-Pierre C., Pelletier I., Ouellet M., Tremblay M.J., Sato S. Galectin-1 promotes HIV-1 infectivity in macrophages through stabilization of viral adsorption. Virology 2008, 371(1):121-129.
    • (2008) Virology , vol.371 , Issue.1 , pp. 121-129
    • Mercier, S.1    St-Pierre, C.2    Pelletier, I.3    Ouellet, M.4    Tremblay, M.J.5    Sato, S.6
  • 152
  • 153
    • 0024273639 scopus 로고
    • Binding region for human immunodeficiency virus (HIV) and epitopes for HIV-blocking monoclonal antibodies of the CD4 molecule defined by site-directed mutagenesis
    • Mizukami T., Fuerst T.R., Berger E.A., Moss B. Binding region for human immunodeficiency virus (HIV) and epitopes for HIV-blocking monoclonal antibodies of the CD4 molecule defined by site-directed mutagenesis. Proc. Natl. Acad. Sci. U. S. A. 1988, 85(23):9273-9277.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , Issue.23 , pp. 9273-9277
    • Mizukami, T.1    Fuerst, T.R.2    Berger, E.A.3    Moss, B.4
  • 154
    • 11944273616 scopus 로고
    • New perspectives on the structure and function of ubiquitin
    • Monia B., Ecker D., Crooke S. New perspectives on the structure and function of ubiquitin. Biotechnology 1990, 8:209-215.
    • (1990) Biotechnology , vol.8 , pp. 209-215
    • Monia, B.1    Ecker, D.2    Crooke, S.3
  • 156
    • 44949158982 scopus 로고    scopus 로고
    • The LEM domain proteins emerin and LAP2alpha are dispensable for human immunodeficiency virus type 1 and murine leukemia virus infections
    • Mulky A., Cohen T.V., Kozlov S.V., Korbei B., Foisner R., Stewart C.L., KewalRamani V.N. The LEM domain proteins emerin and LAP2alpha are dispensable for human immunodeficiency virus type 1 and murine leukemia virus infections. J. Virol. 2008, 82(12):5860-5868.
    • (2008) J. Virol. , vol.82 , Issue.12 , pp. 5860-5868
    • Mulky, A.1    Cohen, T.V.2    Kozlov, S.V.3    Korbei, B.4    Foisner, R.5    Stewart, C.L.6    KewalRamani, V.N.7
  • 158
    • 1342289622 scopus 로고    scopus 로고
    • Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network
    • Nakatsu F., Ohno H. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct. Funct. 2003, 28(5):419-429.
    • (2003) Cell Struct. Funct. , vol.28 , Issue.5 , pp. 419-429
    • Nakatsu, F.1    Ohno, H.2
  • 159
    • 33746564761 scopus 로고    scopus 로고
    • Hepatoma-derived growth factor is expressed after vascular injury in the rat and stimulates smooth muscle cell migration
    • Narron J.V., Stoops T.D., Barringhaus K., Matsumura M., Everett A.D. Hepatoma-derived growth factor is expressed after vascular injury in the rat and stimulates smooth muscle cell migration. Pediatr. Res. 2006, 59(6):778-783.
    • (2006) Pediatr. Res. , vol.59 , Issue.6 , pp. 778-783
    • Narron, J.V.1    Stoops, T.D.2    Barringhaus, K.3    Matsumura, M.4    Everett, A.D.5
  • 160
    • 33645960667 scopus 로고    scopus 로고
    • UnPAKing human immunodeficiency virus (HIV) replication: using small interfering RNA screening to identify novel cofactors and elucidate the role of group I PAKs in HIV infection
    • Nguyen D.G., Wolff K.C., Yin H., Caldwell J.S., Kuhen K.L. UnPAKing human immunodeficiency virus (HIV) replication: using small interfering RNA screening to identify novel cofactors and elucidate the role of group I PAKs in HIV infection. J. Virol. 2006, 80(1):130-137.
    • (2006) J. Virol. , vol.80 , Issue.1 , pp. 130-137
    • Nguyen, D.G.1    Wolff, K.C.2    Yin, H.3    Caldwell, J.S.4    Kuhen, K.L.5
  • 161
    • 70649108820 scopus 로고    scopus 로고
    • Augmentation of reverse transcription by integrase through an interaction with host factor SIP1/Gemin2 is critical for HIV-1 infection
    • Nishitsuji H., Hayashi T., Takahashi T., Miyano M., Kannagi M., Masuda T. Augmentation of reverse transcription by integrase through an interaction with host factor SIP1/Gemin2 is critical for HIV-1 infection. PLoS One 2009, 4(11):e7825.
    • (2009) PLoS One , vol.4 , Issue.11
    • Nishitsuji, H.1    Hayashi, T.2    Takahashi, T.3    Miyano, M.4    Kannagi, M.5    Masuda, T.6
  • 162
    • 0027525103 scopus 로고
    • Friends and family: the role of the Rab GTPases in vesicular traffic
    • Novick P., Brennwald P. Friends and family: the role of the Rab GTPases in vesicular traffic. Cell 1993, 75(4):597-601.
    • (1993) Cell , vol.75 , Issue.4 , pp. 597-601
    • Novick, P.1    Brennwald, P.2
  • 163
    • 80053133140 scopus 로고    scopus 로고
    • Women of color and HIV/AIDS: epidemiology, clinical aspects, and management
    • Springer, New York, NY, V. Stone, B. Ojikutu, M.K. Rawlings, K.Y. Smith (Eds.)
    • Ojikutu B.O., Stone V.E., Bardeguez A. Women of color and HIV/AIDS: epidemiology, clinical aspects, and management. HIV/AIDS in U.S. Communities of Color 2009, 83-101. Springer, New York, NY. V. Stone, B. Ojikutu, M.K. Rawlings, K.Y. Smith (Eds.).
    • (2009) HIV/AIDS in U.S. Communities of Color , pp. 83-101
    • Ojikutu, B.O.1    Stone, V.E.2    Bardeguez, A.3
  • 164
    • 70350433635 scopus 로고    scopus 로고
    • Cooperative-binding and splicing-repressive properties of hnRNP A1
    • Okunola H.L., Krainer A.R. Cooperative-binding and splicing-repressive properties of hnRNP A1. Mol. Cell. Biol. 2009, 29(20):5620-5631.
    • (2009) Mol. Cell. Biol. , vol.29 , Issue.20 , pp. 5620-5631
    • Okunola, H.L.1    Krainer, A.R.2
  • 165
    • 4444246007 scopus 로고    scopus 로고
    • Chemokine receptor CCR5: insights into structure, function, and regulation
    • Oppermann M. Chemokine receptor CCR5: insights into structure, function, and regulation. Cell. Signal. 2004, 16(11):1201-1210.
    • (2004) Cell. Signal. , vol.16 , Issue.11 , pp. 1201-1210
    • Oppermann, M.1
  • 167
    • 15444380346 scopus 로고    scopus 로고
    • Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells
    • Ouellet M., Mercier S., Pelletier I., Bounou S., Roy J., Hirabayashi J., Sato S., Tremblay M.J. Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells. J. Immunol. 2005, 174(7):4120-4126.
    • (2005) J. Immunol. , vol.174 , Issue.7 , pp. 4120-4126
    • Ouellet, M.1    Mercier, S.2    Pelletier, I.3    Bounou, S.4    Roy, J.5    Hirabayashi, J.6    Sato, S.7    Tremblay, M.J.8
  • 168
  • 169
    • 0033168226 scopus 로고    scopus 로고
    • A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription
    • Parada C.A., Roeder R.G. A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 1999, 18(13):3688-3701.
    • (1999) EMBO J. , vol.18 , Issue.13 , pp. 3688-3701
    • Parada, C.A.1    Roeder, R.G.2
  • 170
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik A., Chau V., Wills J.W. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. U. S. A. 2000, 97(24):13069-13074.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.24 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 171
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin M.J., Kadonaga J.T. What's up and down with histone deacetylation and transcription?. Cell 1997, 89(3):325-328.
    • (1997) Cell , vol.89 , Issue.3 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 172
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews A., Kramer B., Marsh M. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 2003, 162(3):443-455.
    • (2003) J. Cell Biol. , vol.162 , Issue.3 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 173
    • 66349087418 scopus 로고    scopus 로고
    • Actin-associated hnRNP proteins as transacting factors in the control of mRNA transport and localization
    • Percipalle P., Raju C.S., Fukuda N. Actin-associated hnRNP proteins as transacting factors in the control of mRNA transport and localization. RNA Biol. 2009, 6(2):171-174.
    • (2009) RNA Biol. , vol.6 , Issue.2 , pp. 171-174
    • Percipalle, P.1    Raju, C.S.2    Fukuda, N.3
  • 174
    • 0034142332 scopus 로고    scopus 로고
    • A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter
    • Pereira L.A, Bentley K., Peeters A., Churchill M.J., Deacon N.J. A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter. Nucleic Acids Res. 2000, 28(3):663-668.
    • (2000) Nucleic Acids Res. , vol.28 , Issue.3 , pp. 663-668
    • Pereira, L.A.1    Bentley, K.2    Peeters, A.3    Churchill, M.J.4    Deacon, N.J.5
  • 175
    • 33646410462 scopus 로고    scopus 로고
    • Identification of an intracellular trafficking and assembly pathway for HIV-1 gag
    • Perlman M., Resh M.D. Identification of an intracellular trafficking and assembly pathway for HIV-1 gag. Traffic 2006, 7(6):731-745.
    • (2006) Traffic , vol.7 , Issue.6 , pp. 731-745
    • Perlman, M.1    Resh, M.D.2
  • 176
    • 3242792513 scopus 로고    scopus 로고
    • Reciprocal regulation of the nuclear factor of activated T cells and HIV-1
    • Pessler F., Cron R.Q. Reciprocal regulation of the nuclear factor of activated T cells and HIV-1. Genes Immun. 2004, 5(3):158-167.
    • (2004) Genes Immun. , vol.5 , Issue.3 , pp. 158-167
    • Pessler, F.1    Cron, R.Q.2
  • 177
    • 0033557708 scopus 로고    scopus 로고
    • The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation
    • Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A., Russell W.C., Akusjarvi G. The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation. EMBO J. 1999, 18(4):1014-1024.
    • (1999) EMBO J. , vol.18 , Issue.4 , pp. 1014-1024
    • Petersen-Mahrt, S.K.1    Estmer, C.2    Ohrmalm, C.3    Matthews, D.A.4    Russell, W.C.5    Akusjarvi, G.6
  • 178
    • 77950839509 scopus 로고    scopus 로고
    • The interferon-induced gene ISG15 blocks retrovirus release from cells late in the budding process
    • Pincetic A., Kuang Z., Seo E.J., Leis J. The interferon-induced gene ISG15 blocks retrovirus release from cells late in the budding process. J. Virol. 2010, 84(9):4725-4736.
    • (2010) J. Virol. , vol.84 , Issue.9 , pp. 4725-4736
    • Pincetic, A.1    Kuang, Z.2    Seo, E.J.3    Leis, J.4
  • 179
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper R.C., Katzmann D.J. Biogenesis and function of multivesicular bodies. Annu. Rev. Cell Dev. Biol. 2007, 23:519-547.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 180
    • 0034846497 scopus 로고    scopus 로고
    • Late endosomes: sorting and partitioning in multivesicular bodies
    • Piper R.C., Luzio J.P. Late endosomes: sorting and partitioning in multivesicular bodies. Traffic 2001, 2(9):612-621.
    • (2001) Traffic , vol.2 , Issue.9 , pp. 612-621
    • Piper, R.C.1    Luzio, J.P.2
  • 182
    • 67349263394 scopus 로고    scopus 로고
    • Trafficking and function of the tetraspanin CD63
    • Pols M.S., Klumperman J. Trafficking and function of the tetraspanin CD63. Exp. Cell Res. 2009, 315(9):1584-1592.
    • (2009) Exp. Cell Res. , vol.315 , Issue.9 , pp. 1584-1592
    • Pols, M.S.1    Klumperman, J.2
  • 183
    • 38349174466 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid
    • Popov S., Popova E., Inoue M., Gottlinger H.G. Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid. J. Virol. 2008, 82(3):1389-1398.
    • (2008) J. Virol. , vol.82 , Issue.3 , pp. 1389-1398
    • Popov, S.1    Popova, E.2    Inoue, M.3    Gottlinger, H.G.4
  • 185
    • 0024267430 scopus 로고
    • Fidelity of HIV-1 reverse transcriptase
    • Preston B.D., Poiesz B.J., Loeb L.A. Fidelity of HIV-1 reverse transcriptase. Science 1988, 242(4882):1168-1171.
    • (1988) Science , vol.242 , Issue.4882 , pp. 1168-1171
    • Preston, B.D.1    Poiesz, B.J.2    Loeb, L.A.3
  • 186
    • 0032525046 scopus 로고    scopus 로고
    • Activated rat macrophages produce a galectin-1-like protein that induces apoptosis of T cells: biochemical and functional characterization
    • Rabinovich G.A., Iglesias M.M., Modesti N.M., Castagna L.F., Wolfenstein-Todel C., Riera C.M., Sotomayor C.E. Activated rat macrophages produce a galectin-1-like protein that induces apoptosis of T cells: biochemical and functional characterization. J. Immunol. 1998, 160(10):4831-4840.
    • (1998) J. Immunol. , vol.160 , Issue.10 , pp. 4831-4840
    • Rabinovich, G.A.1    Iglesias, M.M.2    Modesti, N.M.3    Castagna, L.F.4    Wolfenstein-Todel, C.5    Riera, C.M.6    Sotomayor, C.E.7
  • 187
    • 77956799975 scopus 로고    scopus 로고
    • Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell type-dependent role in regulating infectivity
    • Rai T., Mosoian A., Resh M.D. Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell type-dependent role in regulating infectivity. J. Virol. 2010, 84(19):9783-9792.
    • (2010) J. Virol. , vol.84 , Issue.19 , pp. 9783-9792
    • Rai, T.1    Mosoian, A.2    Resh, M.D.3
  • 188
  • 189
    • 0037005404 scopus 로고    scopus 로고
    • Hrs and endocytic sorting of ubiquitinated membrane proteins
    • Raiborg C., Stenmark H. Hrs and endocytic sorting of ubiquitinated membrane proteins. Cell Struct. Funct. 2002, 27(6):403-408.
    • (2002) Cell Struct. Funct. , vol.27 , Issue.6 , pp. 403-408
    • Raiborg, C.1    Stenmark, H.2
  • 192
    • 0037189506 scopus 로고    scopus 로고
    • Nuclear factor of activated T cells is a driving force for preferential productive HIV-1 infection of CD45RO-expressing CD4+ T cells
    • Robichaud G.A., Barbeau B., Fortin J.F., Rothstein D.M., Tremblay M.J. Nuclear factor of activated T cells is a driving force for preferential productive HIV-1 infection of CD45RO-expressing CD4+ T cells. J. Biol. Chem. 2002, 277(26):23733-23741.
    • (2002) J. Biol. Chem. , vol.277 , Issue.26 , pp. 23733-23741
    • Robichaud, G.A.1    Barbeau, B.2    Fortin, J.F.3    Rothstein, D.M.4    Tremblay, M.J.5
  • 193
    • 57349170148 scopus 로고    scopus 로고
    • Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases
    • Romano G., Giordano A. Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases. Cell Cycle 2008, 7(23):3664-3668.
    • (2008) Cell Cycle , vol.7 , Issue.23 , pp. 3664-3668
    • Romano, G.1    Giordano, A.2
  • 195
    • 33644768131 scopus 로고    scopus 로고
    • Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages
    • Ryzhova E.V., Vos R.M., Albright A.V., Harrist A.V., Harvey T., Gonzalez-Scarano F. Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages. J. Virol. 2006, 80(6):2694-2704.
    • (2006) J. Virol. , vol.80 , Issue.6 , pp. 2694-2704
    • Ryzhova, E.V.1    Vos, R.M.2    Albright, A.V.3    Harrist, A.V.4    Harvey, T.5    Gonzalez-Scarano, F.6
  • 196
    • 35549010295 scopus 로고    scopus 로고
    • Direct inhibition of CDK9 blocks HIV-1 replication without preventing T-cell activation in primary human peripheral blood lymphocytes
    • Salerno D., Hasham M.G., Marshall R., Garriga J., Tsygankov A.Y., Grana X. Direct inhibition of CDK9 blocks HIV-1 replication without preventing T-cell activation in primary human peripheral blood lymphocytes. Gene 2007, 405(1-2):65-78.
    • (2007) Gene , vol.405 , Issue.1-2 , pp. 65-78
    • Salerno, D.1    Hasham, M.G.2    Marshall, R.3    Garriga, J.4    Tsygankov, A.Y.5    Grana, X.6
  • 198
    • 0037770587 scopus 로고    scopus 로고
    • Cyclins that don't cycle-cyclin T/cyclin-dependent kinase-9 determines cardiac muscle cell size
    • Sano M., Schneider M.D. Cyclins that don't cycle-cyclin T/cyclin-dependent kinase-9 determines cardiac muscle cell size. Cell Cycle 2003, 2(2):99-104.
    • (2003) Cell Cycle , vol.2 , Issue.2 , pp. 99-104
    • Sano, M.1    Schneider, M.D.2
  • 199
    • 37849037354 scopus 로고    scopus 로고
    • Modulation of human immunodeficiency virus type 1 infectivity through incorporation of tetraspanin proteins
    • Sato K., Aoki J., Misawa N., Daikoku E., Sano K., Tanaka Y., Koyanagi Y. Modulation of human immunodeficiency virus type 1 infectivity through incorporation of tetraspanin proteins. J. Virol. 2008, 82(2):1021-1033.
    • (2008) J. Virol. , vol.82 , Issue.2 , pp. 1021-1033
    • Sato, K.1    Aoki, J.2    Misawa, N.3    Daikoku, E.4    Sano, K.5    Tanaka, Y.6    Koyanagi, Y.7
  • 200
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • Schnell J.D., Hicke L. Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J. Biol. Chem. 2003, 278(38):35857-35860.
    • (2003) J. Biol. Chem. , vol.278 , Issue.38 , pp. 35857-35860
    • Schnell, J.D.1    Hicke, L.2
  • 201
    • 70449674212 scopus 로고    scopus 로고
    • Human DEAD-box protein 3 has multiple functions in gene regulation and cell cycle control and is a prime target for viral manipulation
    • Schroder M. Human DEAD-box protein 3 has multiple functions in gene regulation and cell cycle control and is a prime target for viral manipulation. Biochem. Pharmacol. 2010, 79(3):297-306.
    • (2010) Biochem. Pharmacol. , vol.79 , Issue.3 , pp. 297-306
    • Schroder, M.1
  • 202
    • 78751705243 scopus 로고    scopus 로고
    • Coordination of intracellular transport steps by GTPases
    • Segev N. Coordination of intracellular transport steps by GTPases. Semin. Cell Dev. Biol. 2010, 22(1):33-38.
    • (2010) Semin. Cell Dev. Biol. , vol.22 , Issue.1 , pp. 33-38
    • Segev, N.1
  • 205
    • 33845788704 scopus 로고    scopus 로고
    • Wild-type levels of human immunodeficiency virus type 1 infectivity in the absence of cellular emerin protein
    • Shun M.C., Daigle J.E., Vandegraaff N., Engelman A. Wild-type levels of human immunodeficiency virus type 1 infectivity in the absence of cellular emerin protein. J. Virol. 2007, 81(1):166-172.
    • (2007) J. Virol. , vol.81 , Issue.1 , pp. 166-172
    • Shun, M.C.1    Daigle, J.E.2    Vandegraaff, N.3    Engelman, A.4
  • 206
  • 207
    • 33744985540 scopus 로고    scopus 로고
    • Endosomal and non-endosomal functions of ESCRT proteins
    • Slagsvold T., Pattni K., Malerod L., Stenmark H. Endosomal and non-endosomal functions of ESCRT proteins. Trends Cell Biol. 2006, 16(6):317-326.
    • (2006) Trends Cell Biol. , vol.16 , Issue.6 , pp. 317-326
    • Slagsvold, T.1    Pattni, K.2    Malerod, L.3    Stenmark, H.4
  • 209
    • 33644758276 scopus 로고    scopus 로고
    • Cyclophilin A and TRIM5alpha independently regulate human immunodeficiency virus type 1 infectivity in human cells
    • Sokolskaja E., Berthoux L., Luban J. Cyclophilin A and TRIM5alpha independently regulate human immunodeficiency virus type 1 infectivity in human cells. J. Virol. 2006, 80(6):2855-2862.
    • (2006) J. Virol. , vol.80 , Issue.6 , pp. 2855-2862
    • Sokolskaja, E.1    Berthoux, L.2    Luban, J.3
  • 211
    • 38449113053 scopus 로고    scopus 로고
    • Gp340 expressed on human genital epithelia binds HIV-1 envelope protein and facilitates viral transmission
    • Stoddard E., Cannon G., Ni H., Kariko K., Capodici J., Malamud D., Weissman D. gp340 expressed on human genital epithelia binds HIV-1 envelope protein and facilitates viral transmission. J. Immunol. 2007, 179(5):3126-3132.
    • (2007) J. Immunol. , vol.179 , Issue.5 , pp. 3126-3132
    • Stoddard, E.1    Cannon, G.2    Ni, H.3    Kariko, K.4    Capodici, J.5    Malamud, D.6    Weissman, D.7
  • 212
    • 69249217928 scopus 로고    scopus 로고
    • Gp340 promotes transcytosis of human immunodeficiency virus type 1 in genital tract-derived cell lines and primary endocervical tissue
    • Stoddard E., Ni H., Cannon G., Zhou C., Kallenbach N., Malamud D., Weissman D. gp340 promotes transcytosis of human immunodeficiency virus type 1 in genital tract-derived cell lines and primary endocervical tissue. J. Virol. 2009, 83(17):8596-8603.
    • (2009) J. Virol. , vol.83 , Issue.17 , pp. 8596-8603
    • Stoddard, E.1    Ni, H.2    Cannon, G.3    Zhou, C.4    Kallenbach, N.5    Malamud, D.6    Weissman, D.7
  • 213
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B., Calistri A., Craig S., Popova E., Gottlinger H.G. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 2003, 114(6):689-699.
    • (2003) Cell , vol.114 , Issue.6 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 214
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M., Owens C.M., Perron M.J., Kiessling M., Autissier P., Sodroski J. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 2004, 427(6977):848-853.
    • (2004) Nature , vol.427 , Issue.6977 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 215
    • 33745861280 scopus 로고    scopus 로고
    • Cyclophilin A: an auxiliary but not necessary cofactor for TRIM5alpha restriction of HIV-1
    • Stremlau M., Song B., Javanbakht H., Perron M., Sodroski J. Cyclophilin A: an auxiliary but not necessary cofactor for TRIM5alpha restriction of HIV-1. Virology 2006, 351(1):112-120.
    • (2006) Virology , vol.351 , Issue.1 , pp. 112-120
    • Stremlau, M.1    Song, B.2    Javanbakht, H.3    Perron, M.4    Sodroski, J.5
  • 216
    • 0029923982 scopus 로고    scopus 로고
    • A role for nucleoporin FG repeat domains in export of human immunodeficiency virus type 1 Rev protein and RNA from the nucleus
    • Stutz F., Izaurralde E., Mattaj I.W., Rosbash M. A role for nucleoporin FG repeat domains in export of human immunodeficiency virus type 1 Rev protein and RNA from the nucleus. Mol. Cell. Biol. 1996, 16(12):7144-7150.
    • (1996) Mol. Cell. Biol. , vol.16 , Issue.12 , pp. 7144-7150
    • Stutz, F.1    Izaurralde, E.2    Mattaj, I.W.3    Rosbash, M.4
  • 217
    • 0029132031 scopus 로고
    • Sp1 transcription factor is required for in vitro basal and Tat-activated transcription from the human immunodeficiency virus type 1 long terminal repeat
    • Sune C., Garcia-Blanco M.A. Sp1 transcription factor is required for in vitro basal and Tat-activated transcription from the human immunodeficiency virus type 1 long terminal repeat. J. Virol. 1995, 69(10):6572-6576.
    • (1995) J. Virol. , vol.69 , Issue.10 , pp. 6572-6576
    • Sune, C.1    Garcia-Blanco, M.A.2
  • 218
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin-nuclear entry of retroviruses
    • Suzuki Y., Craigie R. The road to chromatin-nuclear entry of retroviruses. Nat. Rev. Microbiol. 2007, 5(3):187-196.
    • (2007) Nat. Rev. Microbiol. , vol.5 , Issue.3 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 219
    • 38949155149 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease
    • Takahashi K., Uchida C., Shin R.W., Shimazaki K., Uchida T. Prolyl isomerase Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease. Cell. Mol. Life Sci. 2008, 65(3):359-375.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.3 , pp. 359-375
    • Takahashi, K.1    Uchida, C.2    Shin, R.W.3    Shimazaki, K.4    Uchida, T.5
  • 220
    • 18144378465 scopus 로고    scopus 로고
    • Structural bases of the annealing of primer tRNA(3Lys) to the HIV-1 viral RNA
    • Tisne C. Structural bases of the annealing of primer tRNA(3Lys) to the HIV-1 viral RNA. Curr. HIV Res. 2005, 3(2):147-156.
    • (2005) Curr. HIV Res. , vol.3 , Issue.2 , pp. 147-156
    • Tisne, C.1
  • 221
    • 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., Benkirane M., Emiliani S. Requirement for SWI/SNF chromatin-remodeling complex in Tat-mediated activation of the HIV-1 promoter. EMBO J. 2006, 25(8):1690-1699.
    • (2006) EMBO J. , vol.25 , Issue.8 , pp. 1690-1699
    • Treand, C.1    du Chene, I.2    Bres, V.3    Kiernan, R.4    Benarous, R.5    Benkirane, M.6    Emiliani, S.7
  • 222
    • 53849136952 scopus 로고    scopus 로고
    • Impact of human immunodeficiency virus type 1 reverse transcriptase inhibitor drug resistance mutation interactions on phenotypic susceptibility
    • Trivedi V., Von Lindern J., Montes-Walters M., Rojo D.R., Shell E.J., Parkin N., O'Brien W.A., Ferguson M.R. Impact of human immunodeficiency virus type 1 reverse transcriptase inhibitor drug resistance mutation interactions on phenotypic susceptibility. AIDS Res. Hum. Retroviruses 2008, 24(10):1291-1300.
    • (2008) AIDS Res. Hum. Retroviruses , vol.24 , Issue.10 , pp. 1291-1300
    • Trivedi, V.1    Von Lindern, J.2    Montes-Walters, M.3    Rojo, D.R.4    Shell, E.J.5    Parkin, N.6    O'Brien, W.A.7    Ferguson, M.R.8
  • 224
    • 37149031062 scopus 로고    scopus 로고
    • CBF-1 promotes transcriptional silencing during the establishment of HIV-1 latency
    • Tyagi M., Karn J. CBF-1 promotes transcriptional silencing during the establishment of HIV-1 latency. EMBO J. 2007, 26(24):4985-4995.
    • (2007) EMBO J. , vol.26 , Issue.24 , pp. 4985-4995
    • Tyagi, M.1    Karn, J.2
  • 225
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells
    • Urbe S., Huber L.A., Zerial M., Tooze S.A., Parton R.G. Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells. FEBS Lett. 1993, 334(2):175-182.
    • (1993) FEBS Lett. , vol.334 , Issue.2 , pp. 175-182
    • Urbe, S.1    Huber, L.A.2    Zerial, M.3    Tooze, S.A.4    Parton, R.G.5
  • 226
    • 33644831457 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of integrase-interacting proteins lens epithelium-derived growth factor (LEDGF)/p75 and hepatoma-derived growth factor related protein 2 (HRP2) in preintegration complex function and HIV-1 replication
    • Vandegraaff N., Devroe E., Turlure F., Silver P.A., Engelman A. Biochemical and genetic analyses of integrase-interacting proteins lens epithelium-derived growth factor (LEDGF)/p75 and hepatoma-derived growth factor related protein 2 (HRP2) in preintegration complex function and HIV-1 replication. Virology 2006, 346(2):415-426.
    • (2006) Virology , vol.346 , Issue.2 , pp. 415-426
    • Vandegraaff, N.1    Devroe, E.2    Turlure, F.3    Silver, P.A.4    Engelman, A.5
  • 227
    • 18844429520 scopus 로고    scopus 로고
    • Identification of the LEDGF/p75 HIV-1 integrase-interaction domain and NLS reveals NLS-independent chromatin tethering
    • Vanegas M., Llano M., Delgado S., Thompson D., Peretz M., Poeschla E. Identification of the LEDGF/p75 HIV-1 integrase-interaction domain and NLS reveals NLS-independent chromatin tethering. J. Cell Sci. 2005, 118(Pt. 8):1733-1743.
    • (2005) J. Cell Sci. , vol.118 , Issue.PART. 8 , pp. 1733-1743
    • Vanegas, M.1    Llano, M.2    Delgado, S.3    Thompson, D.4    Peretz, M.5    Poeschla, E.6
  • 228
    • 16344373391 scopus 로고    scopus 로고
    • The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr
    • Varadarajan P., Mahalingam S., Liu P., Ng S.B., Gandotra S., Dorairajoo D.S., Balasundaram D. The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr. Mol. Biol. Cell 2005, 16(4):1823-1838.
    • (2005) Mol. Biol. Cell , vol.16 , Issue.4 , pp. 1823-1838
    • Varadarajan, P.1    Mahalingam, S.2    Liu, P.3    Ng, S.B.4    Gandotra, S.5    Dorairajoo, D.S.6    Balasundaram, D.7
  • 229
    • 0027258123 scopus 로고
    • Chromatin disruption in the promoter of human immunodeficiency virus type 1 during transcriptional activation
    • Verdin E., Paras P., Van Lint C. Chromatin disruption in the promoter of human immunodeficiency virus type 1 during transcriptional activation. EMBO J. 1993, 12(8):3249-3259.
    • (1993) EMBO J. , vol.12 , Issue.8 , pp. 3249-3259
    • Verdin, E.1    Paras, P.2    Van Lint, C.3
  • 232
    • 78149301835 scopus 로고    scopus 로고
    • Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag
    • Weiss E.R., Popova E., Yamanaka H., Kim H.C., Huibregtse J.M., Gottlinger H. Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag. PLoS Pathog. 2010, 6(9).
    • (2010) PLoS Pathog. , vol.6 , Issue.9
    • Weiss, E.R.1    Popova, E.2    Yamanaka, H.3    Kim, H.C.4    Huibregtse, J.M.5    Gottlinger, H.6
  • 233
    • 0035991688 scopus 로고    scopus 로고
    • HIV receptors and cellular tropism
    • Weiss R.A. HIV receptors and cellular tropism. IUBMB Life 2002, 53(4-5):201-205.
    • (2002) IUBMB Life , vol.53 , Issue.4-5 , pp. 201-205
    • Weiss, R.A.1
  • 235
    • 59449092121 scopus 로고    scopus 로고
    • Multiple roles for Puralpha in cellular and viral regulation
    • White M.K., Johnson E.M., Khalili K. Multiple roles for Puralpha in cellular and viral regulation. Cell Cycle 2009, 8(3):1-7.
    • (2009) Cell Cycle , vol.8 , Issue.3 , pp. 1-7
    • White, M.K.1    Johnson, E.M.2    Khalili, K.3
  • 236
    • 30444431914 scopus 로고    scopus 로고
    • NF-kappaB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation
    • Williams S.A., Chen L.F., Kwon H., Ruiz-Jarabo C.M., Verdin E., Greene W.C. NF-kappaB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation. EMBO J. 2006, 25(1):139-149.
    • (2006) EMBO J. , vol.25 , Issue.1 , pp. 139-149
    • Williams, S.A.1    Chen, L.F.2    Kwon, H.3    Ruiz-Jarabo, C.M.4    Verdin, E.5    Greene, W.C.6
  • 237
    • 67349288596 scopus 로고    scopus 로고
    • Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1
    • Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A. Integrase interacts with nucleoporin NUP153 to mediate the nuclear import of human immunodeficiency virus type 1. J. Virol. 2009, 83(13):6522-6533.
    • (2009) J. Virol. , vol.83 , Issue.13 , pp. 6522-6533
    • Woodward, C.L.1    Prakobwanakit, S.2    Mosessian, S.3    Chow, S.A.4
  • 239
    • 4344634285 scopus 로고    scopus 로고
    • HIV-1 gene expression: lessons from provirus and non-integrated DNA
    • Wu Y. HIV-1 gene expression: lessons from provirus and non-integrated DNA. Retrovirology 2004, 1:13.
    • (2004) Retrovirology , vol.1 , pp. 13
    • Wu, Y.1
  • 241
    • 0035116375 scopus 로고    scopus 로고
    • SPT genes: key players in the regulation of transcription, chromatin structure and other cellular processes
    • Yamaguchi Y., Narita T., Inukai N., Wada T., Handa H. SPT genes: key players in the regulation of transcription, chromatin structure and other cellular processes. J. Biochem. 2001, 129(2):185-191.
    • (2001) J. Biochem. , vol.129 , Issue.2 , pp. 185-191
    • Yamaguchi, Y.1    Narita, T.2    Inukai, N.3    Wada, T.4    Handa, H.5
  • 242
    • 70749143560 scopus 로고    scopus 로고
    • Cell context-dependent involvement of ATR in early stages of retroviral replication
    • Yang Y.X., Guen V., Richard J., Cohen E.A., Berthoux L. Cell context-dependent involvement of ATR in early stages of retroviral replication. Virology 2010, 396(2):272-279.
    • (2010) Virology , vol.396 , Issue.2 , pp. 272-279
    • Yang, Y.X.1    Guen, V.2    Richard, J.3    Cohen, E.A.4    Berthoux, L.5
  • 243
    • 3242720240 scopus 로고    scopus 로고
    • Trim5alpha protein restricts both HIV-1 and murine leukemia virus
    • Yap M.W., Nisole S., Lynch C., Stoye J.P. Trim5alpha protein restricts both HIV-1 and murine leukemia virus. Proc. Natl. Acad. Sci. U. S. A. 2004, 101(29):10786-10791.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.29 , pp. 10786-10791
    • Yap, M.W.1    Nisole, S.2    Lynch, C.3    Stoye, J.P.4
  • 244
    • 7044253474 scopus 로고    scopus 로고
    • Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function
    • Yedavalli V.S., Neuveut C., Chi Y.H., Kleiman L., Jeang K.T. Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function. Cell 2004, 119(3):381-392.
    • (2004) Cell , vol.119 , Issue.3 , pp. 381-392
    • Yedavalli, V.S.1    Neuveut, C.2    Chi, Y.H.3    Kleiman, L.4    Jeang, K.T.5
  • 245
    • 67749148923 scopus 로고    scopus 로고
    • A genome-wide short hairpin RNA screening of jurkat T-cells for human proteins contributing to productive HIV-1 replication
    • Yeung M.L., Houzet L., Yedavalli V.S., Jeang K.T. A genome-wide short hairpin RNA screening of jurkat T-cells for human proteins contributing to productive HIV-1 replication. J. Biol. Chem. 2009, 284(29):19463-19473.
    • (2009) J. Biol. Chem. , vol.284 , Issue.29 , pp. 19463-19473
    • Yeung, M.L.1    Houzet, L.2    Yedavalli, V.S.3    Jeang, K.T.4
  • 246
    • 52149093714 scopus 로고    scopus 로고
    • Cyclin T1-dependent genes in activated CD4 T and macrophage cell lines appear enriched in HIV-1 co-factors
    • Yu W., Ramakrishnan R., Wang Y., Chiang K., Sung T.L., Rice A.P. Cyclin T1-dependent genes in activated CD4 T and macrophage cell lines appear enriched in HIV-1 co-factors. PLoS One 2008, 3(9):e3146.
    • (2008) PLoS One , vol.3 , Issue.9
    • Yu, W.1    Ramakrishnan, R.2    Wang, Y.3    Chiang, K.4    Sung, T.L.5    Rice, A.P.6
  • 248
    • 37849024338 scopus 로고    scopus 로고
    • Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV
    • Zhai Q., Fisher R.D., Chung H.Y., Myszka D.G., Sundquist W.I., Hill C.P. Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV. Nat. Struct. Mol. Biol. 2008, 15(1):43-49.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.1 , pp. 43-49
    • Zhai, Q.1    Fisher, R.D.2    Chung, H.Y.3    Myszka, D.G.4    Sundquist, W.I.5    Hill, C.P.6
  • 249
    • 16044364731 scopus 로고    scopus 로고
    • HIV-1 subtype and second-receptor use
    • Zhang L., Huang Y., He T., Cao Y., Ho D.D. HIV-1 subtype and second-receptor use. Nature 1996, 383(6603):768.
    • (1996) Nature , vol.383 , Issue.6603 , pp. 768
    • Zhang, L.1    Huang, Y.2    He, T.3    Cao, Y.4    Ho, D.D.5
  • 250
    • 0033927570 scopus 로고    scopus 로고
    • Use of inhibitors to evaluate coreceptor usage by simian and simian/human immunodeficiency viruses and human immunodeficiency virus type 2 in primary cells
    • Zhang Y., Lou B., Lal R.B., Gettie A., Marx P.A., Moore J.P. Use of inhibitors to evaluate coreceptor usage by simian and simian/human immunodeficiency viruses and human immunodeficiency virus type 2 in primary cells. J. Virol. 2000, 74(15):6893-6910.
    • (2000) J. Virol. , vol.74 , Issue.15 , pp. 6893-6910
    • Zhang, Y.1    Lou, B.2    Lal, R.B.3    Gettie, A.4    Marx, P.A.5    Moore, J.P.6
  • 252
    • 10044266854 scopus 로고    scopus 로고
    • Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription
    • Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F., Brady J.N., Kumar A. Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription. J. Virol. 2004, 78(24):13522-13533.
    • (2004) J. Virol. , vol.78 , Issue.24 , pp. 13522-13533
    • Zhou, M.1    Deng, L.2    Lacoste, V.3    Park, H.U.4    Pumfery, A.5    Kashanchi, F.6    Brady, J.N.7    Kumar, A.8
  • 253
    • 58149487612 scopus 로고    scopus 로고
    • Bromodomain protein Brd4 regulates human immunodeficiency virus transcription through phosphorylation of CDK9 at threonine 29
    • Zhou M., Huang K., Jung K.J., Cho W.K., Klase Z., Kashanchi F., Pise-Masison C.A., Brady J.N. Bromodomain protein Brd4 regulates human immunodeficiency virus transcription through phosphorylation of CDK9 at threonine 29. J. Virol. 2009, 83(2):1036-1044.
    • (2009) J. Virol. , vol.83 , Issue.2 , pp. 1036-1044
    • Zhou, M.1    Huang, K.2    Jung, K.J.3    Cho, W.K.4    Klase, Z.5    Kashanchi, F.6    Pise-Masison, C.A.7    Brady, J.N.8
  • 254
    • 0032127436 scopus 로고    scopus 로고
    • Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages
    • Zhou Q., Chen D., Pierstorff E., Luo K. Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages. EMBO J. 1998, 17(13):3681-3691.
    • (1998) EMBO J. , vol.17 , Issue.13 , pp. 3681-3691
    • Zhou, Q.1    Chen, D.2    Pierstorff, E.3    Luo, K.4
  • 255
    • 0029834383 scopus 로고    scopus 로고
    • Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat
    • Zhou Q., Sharp P.A. Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. Science 1996, 274(5287):605-610.
    • (1996) Science , vol.274 , Issue.5287 , pp. 605-610
    • Zhou, Q.1    Sharp, P.A.2
  • 257
    • 0030890404 scopus 로고    scopus 로고
    • Mutations in the nuclear export signal of human ran-binding protein RanBP1 block the Rev-mediated posttranscriptional regulation of human immunodeficiency virus type 1
    • Zolotukhin A.S., Felber B.K. Mutations in the nuclear export signal of human ran-binding protein RanBP1 block the Rev-mediated posttranscriptional regulation of human immunodeficiency virus type 1. J. Biol. Chem. 1997, 272(17):11356-11360.
    • (1997) J. Biol. Chem. , vol.272 , Issue.17 , pp. 11356-11360
    • Zolotukhin, A.S.1    Felber, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.