메뉴 건너뛰기




Volumn 370, Issue 1, 2008, Pages 45-54

Novel (n)PKC kinases phosphorylate Nef for increased HIV transcription, replication and perinuclear targeting

Author keywords

Nef; Phosphorylation; PKC; Subcellular localization; Transcription

Indexed keywords

NEF PROTEIN; PROTEIN KINASE C DELTA; PROTEIN KINASE C THETA; PROTEIN KINASE LCK; PROTEIN SERINE KINASE;

EID: 36549037151     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.08.015     Document Type: Article
Times cited : (34)

References (55)
  • 1
    • 0029015330 scopus 로고
    • Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis
    • Aiken C., and Trono D. Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis. J. Virol. 69 8 (1995) 5048-5056
    • (1995) J. Virol. , vol.69 , Issue.8 , pp. 5048-5056
    • Aiken, C.1    Trono, D.2
  • 2
    • 0035368515 scopus 로고    scopus 로고
    • Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein
    • Arold S.T., and Baur A.S. Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein. Trends Biochem. Sci. 26 6 (2001) 356-363
    • (2001) Trends Biochem. Sci. , vol.26 , Issue.6 , pp. 356-363
    • Arold, S.T.1    Baur, A.S.2
  • 3
    • 0038701681 scopus 로고    scopus 로고
    • The PKC gene module: molecular biosystematics to resolve its T cell functions
    • Baier G. The PKC gene module: molecular biosystematics to resolve its T cell functions. Immunol. Rev. 192 (2003) 64-79
    • (2003) Immunol. Rev. , vol.192 , pp. 64-79
    • Baier, G.1
  • 4
    • 0028361644 scopus 로고
    • Regulation of human immunodeficiency virus Nef protein by phosphorylation
    • Bandres J.C., Luria S., and Ratner L. Regulation of human immunodeficiency virus Nef protein by phosphorylation. Virology 201 1 (1994) 157-161
    • (1994) Virology , vol.201 , Issue.1 , pp. 157-161
    • Bandres, J.C.1    Luria, S.2    Ratner, L.3
  • 5
    • 0028485232 scopus 로고
    • HIV-1 Nef leads to inhibition or activation of T cells depending on its intracellular localization
    • Baur A.S., Sawai E.T., Dazin P., Fantl W.J., Cheng-Mayer C., and Peterlin B.M. HIV-1 Nef leads to inhibition or activation of T cells depending on its intracellular localization. Immunity 1 5 (1994) 373-384
    • (1994) Immunity , vol.1 , Issue.5 , pp. 373-384
    • Baur, A.S.1    Sawai, E.T.2    Dazin, P.3    Fantl, W.J.4    Cheng-Mayer, C.5    Peterlin, B.M.6
  • 6
    • 0030887932 scopus 로고    scopus 로고
    • The N-terminus of Nef from HIV-1/SIV associates with a protein complex containing Lck and a serine kinase
    • Baur A.S., Sass G., Laffert B., Willbold D., Cheng-Mayer C., and Peterlin B.M. The N-terminus of Nef from HIV-1/SIV associates with a protein complex containing Lck and a serine kinase. Immunity 6 3 (1997) 283-291
    • (1997) Immunity , vol.6 , Issue.3 , pp. 283-291
    • Baur, A.S.1    Sass, G.2    Laffert, B.3    Willbold, D.4    Cheng-Mayer, C.5    Peterlin, B.M.6
  • 7
    • 0029021821 scopus 로고
    • In vitro binding and phosphorylation of human immunodeficiency virus type 1 Nef protein by serine/threonine protein kinase
    • Bodeus M., Marie-Cardine A., Bougeret C., Ramos-Morales F., and Benarous R. In vitro binding and phosphorylation of human immunodeficiency virus type 1 Nef protein by serine/threonine protein kinase. J. Gen. Virol. 76 (1995) 1337-1344
    • (1995) J. Gen. Virol. , vol.76 , pp. 1337-1344
    • Bodeus, M.1    Marie-Cardine, A.2    Bougeret, C.3    Ramos-Morales, F.4    Benarous, R.5
  • 8
    • 0032488027 scopus 로고    scopus 로고
    • A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor
    • Bresnahan P.A., Yonemoto W., Ferrell S., Williams-Herman D., Geleziunas R., and Greene W.C. A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor. Curr. Biol. 8 (1998) 1235-1238
    • (1998) Curr. Biol. , vol.8 , pp. 1235-1238
    • Bresnahan, P.A.1    Yonemoto, W.2    Ferrell, S.3    Williams-Herman, D.4    Geleziunas, R.5    Greene, W.C.6
  • 9
    • 0028968962 scopus 로고
    • The human immunodeficiency virus type 1 Nef protein functions as a protein kinase C substrate in vitro
    • Coates K., and Harris M. The human immunodeficiency virus type 1 Nef protein functions as a protein kinase C substrate in vitro. J. Gen. Virol. 76 (1995) 837-844
    • (1995) J. Gen. Virol. , vol.76 , pp. 837-844
    • Coates, K.1    Harris, M.2
  • 10
    • 0030924947 scopus 로고    scopus 로고
    • Protein kinase C-mediated phosphorylation of HIV-I nef in human cell lines
    • Coates K., Cooke S.J., Mann D.A., and Harris M.P. Protein kinase C-mediated phosphorylation of HIV-I nef in human cell lines. J. Biol. Chem. 272 (1997) 12289-12294
    • (1997) J. Biol. Chem. , vol.272 , pp. 12289-12294
    • Coates, K.1    Cooke, S.J.2    Mann, D.A.3    Harris, M.P.4
  • 11
    • 0029962938 scopus 로고    scopus 로고
    • Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects
    • Collette Y., Dutartre H., Benziane A., Ramos M., Benarous R., Harris M., and Olive D. Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects. J. Biol. Chem. 271 (1996) 6333-6341
    • (1996) J. Biol. Chem. , vol.271 , pp. 6333-6341
    • Collette, Y.1    Dutartre, H.2    Benziane, A.3    Ramos, M.4    Benarous, R.5    Harris, M.6    Olive, D.7
  • 12
    • 0032530773 scopus 로고    scopus 로고
    • Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity
    • Craig H.M., Pandori M.W., and Guatelli J.C. Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity. Proc. Natl. Acad. Sci. USA 95 19 (1998) 11229-11234
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.19 , pp. 11229-11234
    • Craig, H.M.1    Pandori, M.W.2    Guatelli, J.C.3
  • 13
    • 0036230879 scopus 로고    scopus 로고
    • Live and let die: Nef functions beyond HIV replication
    • Fackler O.T., and Baur A.S. Live and let die: Nef functions beyond HIV replication. Immunity 16 (2002) 493-497
    • (2002) Immunity , vol.16 , pp. 493-497
    • Fackler, O.T.1    Baur, A.S.2
  • 14
    • 0033153464 scopus 로고    scopus 로고
    • Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions
    • Fackler O.T., Luo W., Geyer M., Alberts A.S., and Peterlin B.M. Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions. Mol. Cell 3 (1999) 729-739
    • (1999) Mol. Cell , vol.3 , pp. 729-739
    • Fackler, O.T.1    Luo, W.2    Geyer, M.3    Alberts, A.S.4    Peterlin, B.M.5
  • 16
    • 0026083348 scopus 로고
    • Downregulation of protein kinase C-gamma is independent of a functional kinase domain
    • Freisewinkel I., Riethmacher D., and Stabel S. Downregulation of protein kinase C-gamma is independent of a functional kinase domain. FEBS Lett. 280 (1991) 262-266
    • (1991) FEBS Lett. , vol.280 , pp. 262-266
    • Freisewinkel, I.1    Riethmacher, D.2    Stabel, S.3
  • 17
    • 0025733252 scopus 로고
    • Serine phosphorylation-independent downregulation of cell-surface CD4 by nef
    • Garcia J.V., and Miller A.D. Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature 350 (1991) 508-511
    • (1991) Nature , vol.350 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 19
    • 0037047282 scopus 로고    scopus 로고
    • Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery
    • Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.H., Fackler O.T., and Peterlin B.M. Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery. J. Biol. Chem. 277 (2002) 28521-28529
    • (2002) J. Biol. Chem. , vol.277 , pp. 28521-28529
    • Geyer, M.1    Yu, H.2    Mandic, R.3    Linnemann, T.4    Zheng, Y.H.5    Fackler, O.T.6    Peterlin, B.M.7
  • 20
    • 33750614324 scopus 로고    scopus 로고
    • Specific and distinct determinants mediate membrane binding and lipid raft incorporation of HIV-1(SF2) Nef
    • Giese S.I., Woerz I., Homann S., Tibroni N., Geyer M., and Fackler O.T. Specific and distinct determinants mediate membrane binding and lipid raft incorporation of HIV-1(SF2) Nef. Virology 355 (2006) 175-191
    • (2006) Virology , vol.355 , pp. 175-191
    • Giese, S.I.1    Woerz, I.2    Homann, S.3    Tibroni, N.4    Geyer, M.5    Fackler, O.T.6
  • 21
    • 0032488055 scopus 로고    scopus 로고
    • A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4
    • Greenberg M., DeTulleo L., Rapoport I., Skowronski J., and Kirchhausen T. A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4. Curr. Biol. 8 (1998) 1239-1242
    • (1998) Curr. Biol. , vol.8 , pp. 1239-1242
    • Greenberg, M.1    DeTulleo, L.2    Rapoport, I.3    Skowronski, J.4    Kirchhausen, T.5
  • 23
    • 33745835407 scopus 로고    scopus 로고
    • The HIV-1 pathogenicity factor Nef interferes with maturation of stimulatory T-lymphocyte contacts by modulation of N-Wasp activity
    • Haller C., Rauch S., Michel N., Hannemann S., Lehmann M.J., Keppler O.T., and Fackler O.T. The HIV-1 pathogenicity factor Nef interferes with maturation of stimulatory T-lymphocyte contacts by modulation of N-Wasp activity. J. Biol. Chem. 281 (2006) 19618-19630
    • (2006) J. Biol. Chem. , vol.281 , pp. 19618-19630
    • Haller, C.1    Rauch, S.2    Michel, N.3    Hannemann, S.4    Lehmann, M.J.5    Keppler, O.T.6    Fackler, O.T.7
  • 24
    • 85047682875 scopus 로고    scopus 로고
    • Protein kinase C(theta) in T cell activation
    • Isakov N., and Altman A. Protein kinase C(theta) in T cell activation. Annu. Rev. Immunol. 20 (2002) 761-794
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 761-794
    • Isakov, N.1    Altman, A.2
  • 25
    • 19344363916 scopus 로고    scopus 로고
    • HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis
    • Janardhan A., Swigut T., Hill B., Myers M.P., and Skowronski J. HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis. PLoS Biol. 2 (2004) E6
    • (2004) PLoS Biol. , vol.2
    • Janardhan, A.1    Swigut, T.2    Hill, B.3    Myers, M.P.4    Skowronski, J.5
  • 26
    • 12144291075 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts
    • Krautkramer E., Giese S.I., Gasteier J.E., Muranyi W., and Fackler O.T. Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts. J. Virol. 78 (2004) 4085-4097
    • (2004) J. Virol. , vol.78 , pp. 4085-4097
    • Krautkramer, E.1    Giese, S.I.2    Gasteier, J.E.3    Muranyi, W.4    Fackler, O.T.5
  • 27
    • 0032055774 scopus 로고    scopus 로고
    • Nef interacts with the mu subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC I molecules
    • Le Gall S., Erdtmann L., Benichou S., Berlioz-Torrent C., Liu L., Benarous R., Heard J.M., and Schwartz O. Nef interacts with the mu subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC I molecules. Immunity 8 (1998) 483-495
    • (1998) Immunity , vol.8 , pp. 483-495
    • Le Gall, S.1    Erdtmann, L.2    Benichou, S.3    Berlioz-Torrent, C.4    Liu, L.5    Benarous, R.6    Heard, J.M.7    Schwartz, O.8
  • 29
    • 0026519632 scopus 로고
    • Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo
    • Liyanage M., Frith D., Livneh E., and Stabel S. Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo. Biochem. J. 283 (1992) 781-787
    • (1992) Biochem. J. , vol.283 , pp. 781-787
    • Liyanage, M.1    Frith, D.2    Livneh, E.3    Stabel, S.4
  • 30
    • 0030475891 scopus 로고    scopus 로고
    • CDC42 and Rac1 are implicated in the activation of the Nef-associated kinase and replication of HIV-1
    • Lu X., Wu X., Plemenitas A., Yu H., Sawai E.T., Abo A., and Peterlin B.M. CDC42 and Rac1 are implicated in the activation of the Nef-associated kinase and replication of HIV-1. Curr. Biol. 6 (1996) 1677-1684
    • (1996) Curr. Biol. , vol.6 , pp. 1677-1684
    • Lu, X.1    Wu, X.2    Plemenitas, A.3    Yu, H.4    Sawai, E.T.5    Abo, A.6    Peterlin, B.M.7
  • 31
    • 0032076086 scopus 로고    scopus 로고
    • Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4
    • Lu X., Yu H., Liu S.H., Brodsky F.M., and Peterlin B.M. Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4. Immunity 8 (1998) 647-656
    • (1998) Immunity , vol.8 , pp. 647-656
    • Lu, X.1    Yu, H.2    Liu, S.H.3    Brodsky, F.M.4    Peterlin, B.M.5
  • 32
    • 0031047976 scopus 로고    scopus 로고
    • Induction of phosphorylation of human immunodeficiency virus type 1 Nef and enhancement of CD4 downregulation by phorbol myristate acetate
    • Luo T., Downing J.R., and Garcia J.V. Induction of phosphorylation of human immunodeficiency virus type 1 Nef and enhancement of CD4 downregulation by phorbol myristate acetate. J. Virol. 71 (1997) 2535-2539
    • (1997) J. Virol. , vol.71 , pp. 2535-2539
    • Luo, T.1    Downing, J.R.2    Garcia, J.V.3
  • 33
    • 0035157781 scopus 로고    scopus 로고
    • Negative factor from SIV binds to the catalytic subunit of the V-ATPase to internalize CD4 and to increase viral infectivity
    • Mandic R., Fackler O.T., Geyer M., Linnemann T., Zheng Y.H., and Peterlin B.M. Negative factor from SIV binds to the catalytic subunit of the V-ATPase to internalize CD4 and to increase viral infectivity. Mol. Biol. Cell 12 (2001) 463-473
    • (2001) Mol. Biol. Cell , vol.12 , pp. 463-473
    • Mandic, R.1    Fackler, O.T.2    Geyer, M.3    Linnemann, T.4    Zheng, Y.H.5    Peterlin, B.M.6
  • 34
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions
    • McLaughlin S., and Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20 (1995) 272-276
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 35
    • 18044378256 scopus 로고    scopus 로고
    • The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4
    • Michel N., Allespach I., Venzke S., Fackler O.T., and Keppler O.T. The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4. Curr. Biol. 15 (2005) 714-723
    • (2005) Curr. Biol. , vol.15 , pp. 714-723
    • Michel, N.1    Allespach, I.2    Venzke, S.3    Fackler, O.T.4    Keppler, O.T.5
  • 36
    • 33746582688 scopus 로고    scopus 로고
    • The Nef protein of human immunodeficiency virus is a broad-spectrum modulator of chemokine receptor cell surface levels that acts independently of classical motifs for receptor endocytosis and Galphai signaling
    • Michel N., Ganter K., Venzke S., Bitzegeio J., Fackler O.T., and Keppler O.T. The Nef protein of human immunodeficiency virus is a broad-spectrum modulator of chemokine receptor cell surface levels that acts independently of classical motifs for receptor endocytosis and Galphai signaling. Mol. Biol. Cell 17 (2006) 3578-3590
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3578-3590
    • Michel, N.1    Ganter, K.2    Venzke, S.3    Bitzegeio, J.4    Fackler, O.T.5    Keppler, O.T.6
  • 37
    • 0027956402 scopus 로고
    • The HIV-1 nef gene acts as a positive viral infectivity factor
    • Miller M.D., Feinberg M.B., and Greene W.C. The HIV-1 nef gene acts as a positive viral infectivity factor. Trends Microbiol. 2 (1994) 294-298
    • (1994) Trends Microbiol. , vol.2 , pp. 294-298
    • Miller, M.D.1    Feinberg, M.B.2    Greene, W.C.3
  • 38
    • 0024991898 scopus 로고
    • pEF-BOS, a powerful mammalian expression vector
    • Mizushima S., and Nagata S. pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 18 (1990) 5322
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2
  • 39
    • 8644224930 scopus 로고    scopus 로고
    • Nef associates with p21-activated kinase 2 in a p21-GTPase-dependent dynamic activation complex within lipid rafts
    • Pulkkinen K., Renkema G.H., Kirchhoff F., and Saksela K. Nef associates with p21-activated kinase 2 in a p21-GTPase-dependent dynamic activation complex within lipid rafts. J. Virol. 78 (2004) 12773-12780
    • (2004) J. Virol. , vol.78 , pp. 12773-12780
    • Pulkkinen, K.1    Renkema, G.H.2    Kirchhoff, F.3    Saksela, K.4
  • 40
    • 0033518291 scopus 로고    scopus 로고
    • Identification of the Nef-associated kinase as p21-activated kinase 2
    • Renkema G.H., Manninen A., Mann D.A., Harris M., and Saksela K. Identification of the Nef-associated kinase as p21-activated kinase 2. Curr. Biol. 9 (1999) 1407-1410
    • (1999) Curr. Biol. , vol.9 , pp. 1407-1410
    • Renkema, G.H.1    Manninen, A.2    Mann, D.A.3    Harris, M.4    Saksela, K.5
  • 41
    • 0036785568 scopus 로고    scopus 로고
    • Cdc42/Rac1-mediated activation primes PAK2 for superactivation by tyrosine phosphorylation
    • Renkema G.H., Pulkkinen K., and Saksela K. Cdc42/Rac1-mediated activation primes PAK2 for superactivation by tyrosine phosphorylation. Mol. Cell. Biol. 22 (2002) 6719-6725
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6719-6725
    • Renkema, G.H.1    Pulkkinen, K.2    Saksela, K.3
  • 42
    • 33745122662 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways
    • Roeth J.F., and Collins K.L. Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways. Microbiol. Mol. Biol. Rev. 70 (2006) 548-563
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 548-563
    • Roeth, J.F.1    Collins, K.L.2
  • 43
    • 0028878783 scopus 로고
    • Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4
    • Saksela K., Cheng G., and Baltimore D. Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4. EMBO J. 14 (1995) 484-491
    • (1995) EMBO J. , vol.14 , pp. 484-491
    • Saksela, K.1    Cheng, G.2    Baltimore, D.3
  • 44
    • 0029045360 scopus 로고
    • Human immunodeficiency virus type 1 Nef increases the efficiency of reverse transcription in the infected cell
    • Schwartz O., Marechal V., Danos O., and Heard J.M. Human immunodeficiency virus type 1 Nef increases the efficiency of reverse transcription in the infected cell. J. Virol. 69 (1995) 4053-4059
    • (1995) J. Virol. , vol.69 , pp. 4053-4059
    • Schwartz, O.1    Marechal, V.2    Danos, O.3    Heard, J.M.4
  • 45
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein
    • Schwartz O., Marechal V., Le Gall S., Lemonnier F., and Heard J.M. Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat. Med. 2 (1996) 338-342
    • (1996) Nat. Med. , vol.2 , pp. 338-342
    • Schwartz, O.1    Marechal, V.2    Le Gall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 48
    • 0027952787 scopus 로고
    • The importance of nef in the induction of human immunodeficiency virus type 1 replication from primary quiescent CD4 lymphocytes
    • Spina C.A., Kwoh T.J., Chowers M.Y., Guatelli J.C., and Richman D.D. The importance of nef in the induction of human immunodeficiency virus type 1 replication from primary quiescent CD4 lymphocytes. J. Exp. Med. 179 (1994) 115-123
    • (1994) J. Exp. Med. , vol.179 , pp. 115-123
    • Spina, C.A.1    Kwoh, T.J.2    Chowers, M.Y.3    Guatelli, J.C.4    Richman, D.D.5
  • 49
    • 0344875506 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Nef expression induces intracellular accumulation of multivesicular bodies and major histocompatibility complex class II complexes: potential role of phosphatidylinositol 3-kinase
    • Stumptner-Cuvelette P., Jouve M., Helft J., Dugast M., Glouzman A.S., Jooss K., Raposo G., and Benaroch P. Human immunodeficiency virus-1 Nef expression induces intracellular accumulation of multivesicular bodies and major histocompatibility complex class II complexes: potential role of phosphatidylinositol 3-kinase. Mol. Biol. Cell 14 (2003) 4857-4870
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4857-4870
    • Stumptner-Cuvelette, P.1    Jouve, M.2    Helft, J.3    Dugast, M.4    Glouzman, A.S.5    Jooss, K.6    Raposo, G.7    Benaroch, P.8
  • 50
    • 33646552033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type-1 infection impairs the formation of the immunological synapse
    • Thoulouze M.I., Sol-Foulon N., Blanchet F., Dautry-Varsat A., Schwartz O., and Alcover A. Human immunodeficiency virus type-1 infection impairs the formation of the immunological synapse. Immunity 24 (2006) 547-561
    • (2006) Immunity , vol.24 , pp. 547-561
    • Thoulouze, M.I.1    Sol-Foulon, N.2    Blanchet, F.3    Dautry-Varsat, A.4    Schwartz, O.5    Alcover, A.6
  • 51
    • 0034602776 scopus 로고    scopus 로고
    • The Nef protein of HIV-1 associates with rafts and primes T cells for activation
    • Wang J.K., Kiyokawa E., Verdin E., and Trono D. The Nef protein of HIV-1 associates with rafts and primes T cells for activation. Proc. Natl. Acad. Sci. USA 97 (2000) 394-399
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 394-399
    • Wang, J.K.1    Kiyokawa, E.2    Verdin, E.3    Trono, D.4
  • 52
    • 0030273317 scopus 로고    scopus 로고
    • HIV-1 Nef association with cellular serine kinase correlates with enhanced virion infectivity and efficient proviral DNA synthesis
    • Wiskerchen M., and Cheng-Mayer C. HIV-1 Nef association with cellular serine kinase correlates with enhanced virion infectivity and efficient proviral DNA synthesis. Virology 224 (1996) 292-301
    • (1996) Virology , vol.224 , pp. 292-301
    • Wiskerchen, M.1    Cheng-Mayer, C.2
  • 54
    • 0035173735 scopus 로고    scopus 로고
    • HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals
    • Wolf D., Witte V., Laffert B., Blume K., Stromer E., Trapp S., d'Aloja P., Schurmann A., and Baur A.S. HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals. Nat. Med. 7 (2001) 1217-1224
    • (2001) Nat. Med. , vol.7 , pp. 1217-1224
    • Wolf, D.1    Witte, V.2    Laffert, B.3    Blume, K.4    Stromer, E.5    Trapp, S.6    d'Aloja, P.7    Schurmann, A.8    Baur, A.S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.