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Volumn 8, Issue 1, 2013, Pages

Down-Regulation of CTLA-4 by HIV-1 Nef Protein

(15)  El Far, Mohamed a,b,i   Isabelle, Catherine a,b   Chomont, Nicolas a,b,c   Bourbonnière, Martin a,b   Fonseca, Simone a,b,c,j   Ancuta, Petronela a   Peretz, Yoav a,b   Chouikh, Younes a,b   Halwani, Rabih d   Schwartz, Olivier e   Madrenas, Joaquín f   Freeman, Gordon J g   Routy, Jean Pierre h   Haddad, Elias K a,b,c   Sékaly, Rafick Pierre a,b,c  


Author keywords

[No Author keywords available]

Indexed keywords

CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; NEF PROTEIN;

EID: 84872804428     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0054295     Document Type: Article
Times cited : (24)

References (63)
  • 1
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins-ensuring viral survival in a hostile environment
    • Malim MH, Emerman M, (2008) HIV-1 accessory proteins-ensuring viral survival in a hostile environment. Cell Host Microbe 3: 388-398.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 2
    • 0028180868 scopus 로고
    • Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain
    • Aiken C, Konner J, Landau NR, Lenburg ME, Trono D, (1994) Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain. Cell 76: 853-864.
    • (1994) Cell , vol.76 , pp. 853-864
    • Aiken, C.1    Konner, J.2    Landau, N.R.3    Lenburg, M.E.4    Trono, D.5
  • 3
    • 0035368515 scopus 로고    scopus 로고
    • Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein
    • Arold ST, Baur AS, (2001) Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein. Trends Biochem Sci 26: 356-363.
    • (2001) Trends Biochem Sci , vol.26 , pp. 356-363
    • Arold, S.T.1    Baur, A.S.2
  • 4
    • 0028062729 scopus 로고
    • Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic
    • Benichou S, Bomsel M, Bodeus M, Durand H, Doute M, et al. (1994) Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic. J Biol Chem 269: 30073-30076.
    • (1994) J Biol Chem , vol.269 , pp. 30073-30076
    • Benichou, S.1    Bomsel, M.2    Bodeus, M.3    Durand, H.4    Doute, M.5
  • 5
    • 0029793620 scopus 로고    scopus 로고
    • CD4 down-modulation during infection of human T cells with human immunodeficiency virus type 1 involves independent activities of vpu, env, and nef
    • Chen BK, Gandhi RT, Baltimore D, (1996) CD4 down-modulation during infection of human T cells with human immunodeficiency virus type 1 involves independent activities of vpu, env, and nef. J Virol 70: 6044-6053.
    • (1996) J Virol , vol.70 , pp. 6044-6053
    • Chen, B.K.1    Gandhi, R.T.2    Baltimore, D.3
  • 6
    • 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 PA, Yonemoto W, Ferrell S, Williams-Herman D, Geleziunas R, et al. (1998) 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: 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
  • 8
    • 0036231461 scopus 로고    scopus 로고
    • Nef-mediated downregulation of CD4 enhances human immunodeficiency virus type 1 replication in primary T lymphocytes
    • Lundquist CA, Tobiume M, Zhou J, Unutmaz D, Aiken C, (2002) Nef-mediated downregulation of CD4 enhances human immunodeficiency virus type 1 replication in primary T lymphocytes. J Virol 76: 4625-4633.
    • (2002) J Virol , vol.76 , pp. 4625-4633
    • Lundquist, C.A.1    Tobiume, M.2    Zhou, J.3    Unutmaz, D.4    Aiken, C.5
  • 9
    • 0032987238 scopus 로고    scopus 로고
    • The Nef protein of primate lentiviruses
    • Piguet V, Trono D, (1999) The Nef protein of primate lentiviruses. Rev Med Virol 9: 111-120.
    • (1999) Rev Med Virol , vol.9 , pp. 111-120
    • Piguet, V.1    Trono, D.2
  • 10
    • 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, Heard JM, (1996) Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat Med 2: 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
  • 11
    • 0036056929 scopus 로고    scopus 로고
    • Interaction between Nef and phosphatidylinositol-3-kinase leads to activation of p21-activated kinase and increased production of HIV
    • Linnemann T, Zheng YH, Mandic R, Peterlin BM, (2002) Interaction between Nef and phosphatidylinositol-3-kinase leads to activation of p21-activated kinase and increased production of HIV. Virology 294: 246-255.
    • (2002) Virology , vol.294 , pp. 246-255
    • Linnemann, T.1    Zheng, Y.H.2    Mandic, R.3    Peterlin, B.M.4
  • 13
    • 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, et al. (2001) HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals. Nat Med 7: 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
  • 14
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee CH, Saksela K, Mirza UA, Chait BT, Kuriyan J, (1996) Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85: 931-942.
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 15
    • 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, et al. (1996) Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects. J Biol Chem 271: 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
  • 16
    • 0028805516 scopus 로고
    • A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    • Lee CH, Leung B, Lemmon MA, Zheng J, Cowburn D, et al. (1995) A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J 14: 5006-5015.
    • (1995) EMBO J , vol.14 , pp. 5006-5015
    • Lee, C.H.1    Leung, B.2    Lemmon, M.A.3    Zheng, J.4    Cowburn, D.5
  • 17
    • 0035943355 scopus 로고    scopus 로고
    • Selective transcription and modulation of resting T cell activity by preintegrated HIV DNA
    • Wu Y, Marsh JW, (2001) Selective transcription and modulation of resting T cell activity by preintegrated HIV DNA. Science 293: 1503-1506.
    • (2001) Science , vol.293 , pp. 1503-1506
    • Wu, Y.1    Marsh, J.W.2
  • 18
    • 0033529258 scopus 로고    scopus 로고
    • HIV-1 Nef increases T cell activation in a stimulus-dependent manner
    • Schrager JA, Marsh JW, (1999) HIV-1 Nef increases T cell activation in a stimulus-dependent manner. Proc Natl Acad Sci U S A 96: 8167-8172.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8167-8172
    • Schrager, J.A.1    Marsh, J.W.2
  • 20
    • 0028791059 scopus 로고
    • Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4
    • Waterhouse P, Penninger JM, Timms E, Wakeham A, Shahinian A, et al. (1995) Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4. Science 270: 985-988.
    • (1995) Science , vol.270 , pp. 985-988
    • Waterhouse, P.1    Penninger, J.M.2    Timms, E.3    Wakeham, A.4    Shahinian, A.5
  • 21
    • 0034254301 scopus 로고    scopus 로고
    • CTLA-4 (CD152) can inhibit T cell activation by two different mechanisms depending on its level of cell surface expression
    • Carreno BM, Bennett F, Chau TA, Ling V, Luxenberg D, et al. (2000) CTLA-4 (CD152) can inhibit T cell activation by two different mechanisms depending on its level of cell surface expression. J Immunol 165: 1352-1356.
    • (2000) J Immunol , vol.165 , pp. 1352-1356
    • Carreno, B.M.1    Bennett, F.2    Chau, T.A.3    Ling, V.4    Luxenberg, D.5
  • 23
    • 1642396607 scopus 로고    scopus 로고
    • Ligation of B7-1/B7-2 by human CD4+ T cells triggers indoleamine 2,3-dioxygenase activity in dendritic cells
    • Munn DH, Sharma MD, Mellor AL, (2004) Ligation of B7-1/B7-2 by human CD4+ T cells triggers indoleamine 2,3-dioxygenase activity in dendritic cells. J Immunol 172: 4100-4110.
    • (2004) J Immunol , vol.172 , pp. 4100-4110
    • Munn, D.H.1    Sharma, M.D.2    Mellor, A.L.3
  • 24
    • 0028852073 scopus 로고
    • Cytotoxic T lymphocyte-associated molecule-4, a high-avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail
    • Leung HT, Bradshaw J, Cleaveland JS, Linsley PS, (1995) Cytotoxic T lymphocyte-associated molecule-4, a high-avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail. J Biol Chem 270: 25107-25114.
    • (1995) J Biol Chem , vol.270 , pp. 25107-25114
    • Leung, H.T.1    Bradshaw, J.2    Cleaveland, J.S.3    Linsley, P.S.4
  • 25
    • 0030176371 scopus 로고    scopus 로고
    • Intracellular trafficking of CTLA-4 and focal localization towards sites of TCR engagement
    • Linsley PS, Bradshaw J, Greene J, Peach R, Bennett KL, et al. (1996) Intracellular trafficking of CTLA-4 and focal localization towards sites of TCR engagement. Immunity 4: 535-543.
    • (1996) Immunity , vol.4 , pp. 535-543
    • Linsley, P.S.1    Bradshaw, J.2    Greene, J.3    Peach, R.4    Bennett, K.L.5
  • 26
    • 0033083788 scopus 로고    scopus 로고
    • Regulation of cytotoxic T lymphocyte-associated molecule-4 by Src kinases
    • Chuang E, Lee KM, Robbins MD, Duerr JM, Alegre ML, et al. (1999) Regulation of cytotoxic T lymphocyte-associated molecule-4 by Src kinases. J Immunol 162: 1270-1277.
    • (1999) J Immunol , vol.162 , pp. 1270-1277
    • Chuang, E.1    Lee, K.M.2    Robbins, M.D.3    Duerr, J.M.4    Alegre, M.L.5
  • 27
    • 0029899783 scopus 로고    scopus 로고
    • CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells
    • Krummel MF, Allison JP, (1996) CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells. J Exp Med 183: 2533-2540.
    • (1996) J Exp Med , vol.183 , pp. 2533-2540
    • Krummel, M.F.1    Allison, J.P.2
  • 28
    • 0036569236 scopus 로고    scopus 로고
    • CTLA-4 suppresses proximal TCR signaling in resting human CD4(+) T cells by inhibiting ZAP-70 Tyr(319) phosphorylation: a potential role for tyrosine phosphatases
    • Guntermann C, Alexander DR, (2002) CTLA-4 suppresses proximal TCR signaling in resting human CD4(+) T cells by inhibiting ZAP-70 Tyr(319) phosphorylation: a potential role for tyrosine phosphatases. J Immunol 168: 4420-4429.
    • (2002) J Immunol , vol.168 , pp. 4420-4429
    • Guntermann, C.1    Alexander, D.R.2
  • 30
    • 0025353408 scopus 로고
    • Constitutive expression of human immunodeficiency virus (HIV) nef protein in human astrocytes does not influence basal or induced HIV long terminal repeat activity
    • Bachelerie F, Alcami J, Hazan U, Israel N, Goud B, et al. (1990) Constitutive expression of human immunodeficiency virus (HIV) nef protein in human astrocytes does not influence basal or induced HIV long terminal repeat activity. J Virol 64: 3059-3062.
    • (1990) J Virol , vol.64 , pp. 3059-3062
    • Bachelerie, F.1    Alcami, J.2    Hazan, U.3    Israel, N.4    Goud, B.5
  • 31
    • 0029991350 scopus 로고    scopus 로고
    • Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation
    • Jordan M, Schallhorn A, Wurm FM, (1996) Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res 24: 596-601.
    • (1996) Nucleic Acids Res , vol.24 , pp. 596-601
    • Jordan, M.1    Schallhorn, A.2    Wurm, F.M.3
  • 32
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders EM, Stap J, Brakenhoff GJ, van Driel R, Aten JA, (1992) Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J Cell Sci 103 (Pt 3):: 857-862.
    • (1992) J Cell Sci , vol.103 , Issue.Pt 3 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.J.3    van Driel, R.4    Aten, J.A.5
  • 33
    • 58149280838 scopus 로고    scopus 로고
    • T cell-dendritic cell immunological synapses contain TCR-dependent CD28-CD80 clusters that recruit protein kinase C theta
    • Tseng SY, Waite JC, Liu M, Vardhana S, Dustin ML, (2008) T cell-dendritic cell immunological synapses contain TCR-dependent CD28-CD80 clusters that recruit protein kinase C theta. J Immunol 181: 4852-4863.
    • (2008) J Immunol , vol.181 , pp. 4852-4863
    • Tseng, S.Y.1    Waite, J.C.2    Liu, M.3    Vardhana, S.4    Dustin, M.L.5
  • 34
    • 1542332582 scopus 로고    scopus 로고
    • Two different forms of human CTLA-4 proteins following peripheral T cell activation
    • Chun T, Choi HJ, Chung YH, (2004) Two different forms of human CTLA-4 proteins following peripheral T cell activation. Immunol Lett 91: 213-220.
    • (2004) Immunol Lett , vol.91 , pp. 213-220
    • Chun, T.1    Choi, H.J.2    Chung, Y.H.3
  • 35
    • 0030917081 scopus 로고    scopus 로고
    • Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2
    • Shiratori T, Miyatake S, Ohno H, Nakaseko C, Isono K, et al. (1997) Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2. Immunity 6: 583-589.
    • (1997) Immunity , vol.6 , pp. 583-589
    • Shiratori, T.1    Miyatake, S.2    Ohno, H.3    Nakaseko, C.4    Isono, K.5
  • 36
    • 0030611358 scopus 로고    scopus 로고
    • Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor protein
    • Zhang Y, Allison JP, (1997) Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor protein. Proc Natl Acad Sci U S A 94: 9273-9278.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9273-9278
    • Zhang, Y.1    Allison, J.P.2
  • 37
    • 17044429848 scopus 로고    scopus 로고
    • Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during activation of regulatory T cells
    • Mead KI, Zheng Y, Manzotti CN, Perry LC, Liu MK, et al. (2005) Exocytosis of CTLA-4 is dependent on phospholipase D and ADP ribosylation factor-1 and stimulated during activation of regulatory T cells. J Immunol 174: 4803-4811.
    • (2005) J Immunol , vol.174 , pp. 4803-4811
    • Mead, K.I.1    Zheng, Y.2    Manzotti, C.N.3    Perry, L.C.4    Liu, M.K.5
  • 38
    • 33746322762 scopus 로고    scopus 로고
    • Functional characterization of HIV-1 Nef mutants in the context of viral infection
    • Fackler OT, Moris A, Tibroni N, Giese SI, Glass B, et al. (2006) Functional characterization of HIV-1 Nef mutants in the context of viral infection. Virology 351: 322-339.
    • (2006) Virology , vol.351 , pp. 322-339
    • Fackler, O.T.1    Moris, A.2    Tibroni, N.3    Giese, S.I.4    Glass, B.5
  • 39
    • 0031452168 scopus 로고    scopus 로고
    • Structure, function and regulation of the vacuolar (H+)-ATPase
    • Stevens TH, Forgac M, (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13: 779-808.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 779-808
    • Stevens, T.H.1    Forgac, M.2
  • 40
    • 0027165412 scopus 로고
    • Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro
    • Peter F, Plutner H, Zhu H, Kreis TE, Balch WE, (1993) Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J Cell Biol 122: 1155-1167.
    • (1993) J Cell Biol , vol.122 , pp. 1155-1167
    • Peter, F.1    Plutner, H.2    Zhu, H.3    Kreis, T.E.4    Balch, W.E.5
  • 41
    • 84857260144 scopus 로고    scopus 로고
    • Lysosomal acidification mechanisms
    • Mindell JA, (2012) Lysosomal acidification mechanisms. Annu Rev Physiol 74: 69-86.
    • (2012) Annu Rev Physiol , vol.74 , pp. 69-86
    • Mindell, J.A.1
  • 42
    • 0037175008 scopus 로고    scopus 로고
    • Concanamycin A, the specific inhibitor of V-ATPases, binds to the V(o) subunit c
    • Huss M, Ingenhorst G, Konig S, Gassel M, Drose S, et al. (2002) Concanamycin A, the specific inhibitor of V-ATPases, binds to the V(o) subunit c. J Biol Chem 277: 40544-40548.
    • (2002) J Biol Chem , vol.277 , pp. 40544-40548
    • Huss, M.1    Ingenhorst, G.2    Konig, S.3    Gassel, M.4    Drose, S.5
  • 43
    • 0020352681 scopus 로고
    • Weak bases and ionophores rapidly and reversibly raise the pH of endocytic vesicles in cultured mouse fibroblasts
    • Maxfield FR, (1982) Weak bases and ionophores rapidly and reversibly raise the pH of endocytic vesicles in cultured mouse fibroblasts. J Cell Biol 95: 676-681.
    • (1982) J Cell Biol , vol.95 , pp. 676-681
    • Maxfield, F.R.1
  • 44
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B, (1978) Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci U S A 75: 3327-3331.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 45
    • 0036162115 scopus 로고    scopus 로고
    • Chloroquine decreases cell-surface expression of tumour necrosis factor receptors in human histiocytic U-937 cells
    • Jeong JY, Choi JW, Jeon KI, Jue DM, (2002) Chloroquine decreases cell-surface expression of tumour necrosis factor receptors in human histiocytic U-937 cells. Immunology 105: 83-91.
    • (2002) Immunology , vol.105 , pp. 83-91
    • Jeong, J.Y.1    Choi, J.W.2    Jeon, K.I.3    Jue, D.M.4
  • 46
    • 0030051240 scopus 로고    scopus 로고
    • Inhibition of Nef- and phorbol ester-induced CD4 degradation by macrolide antibiotics
    • Luo T, Anderson SJ, Garcia JV, (1996) Inhibition of Nef- and phorbol ester-induced CD4 degradation by macrolide antibiotics. J Virol 70: 1527-1534.
    • (1996) J Virol , vol.70 , pp. 1527-1534
    • Luo, T.1    Anderson, S.J.2    Garcia, J.V.3
  • 47
    • 0028341239 scopus 로고
    • Trafficking of interleukin 2 and transferrin in endosomal fractions of T lymphocytes
    • Duprez V, Smoljanovic M, Lieb M, Dautry-Varsat A, (1994) Trafficking of interleukin 2 and transferrin in endosomal fractions of T lymphocytes. J Cell Sci 107 (Pt 5):: 1289-1295.
    • (1994) J Cell Sci , vol.107 , Issue.Pt 5 , pp. 1289-1295
    • Duprez, V.1    Smoljanovic, M.2    Lieb, M.3    Dautry-Varsat, A.4
  • 48
    • 0030443168 scopus 로고    scopus 로고
    • Regulation of surface and intracellular expression of CTLA4 on mouse T cells
    • Alegre ML, Noel PJ, Eisfelder BJ, Chuang E, Clark MR, et al. (1996) Regulation of surface and intracellular expression of CTLA4 on mouse T cells. J Immunol 157: 4762-4770.
    • (1996) J Immunol , vol.157 , pp. 4762-4770
    • Alegre, M.L.1    Noel, P.J.2    Eisfelder, B.J.3    Chuang, E.4    Clark, M.R.5
  • 49
    • 20744447725 scopus 로고    scopus 로고
    • Detection of human immunodeficiency virus type 1 Nef and CD4 physical interaction in living human cells by using bioluminescence resonance energy transfer
    • Cluet D, Bertsch C, Beyer C, Gloeckler L, Erhardt M, et al. (2005) Detection of human immunodeficiency virus type 1 Nef and CD4 physical interaction in living human cells by using bioluminescence resonance energy transfer. J Virol 79: 8629-8636.
    • (2005) J Virol , vol.79 , pp. 8629-8636
    • Cluet, D.1    Bertsch, C.2    Beyer, C.3    Gloeckler, L.4    Erhardt, M.5
  • 50
    • 34548680261 scopus 로고    scopus 로고
    • Upregulation of CTLA-4 by HIV-specific CD4+ T cells correlates with disease progression and defines a reversible immune dysfunction
    • Kaufmann DE, Kavanagh DG, Pereyra F, Zaunders JJ, Mackey EW, et al. (2007) Upregulation of CTLA-4 by HIV-specific CD4+ T cells correlates with disease progression and defines a reversible immune dysfunction. Nat Immunol 8: 1246-1254.
    • (2007) Nat Immunol , vol.8 , pp. 1246-1254
    • Kaufmann, D.E.1    Kavanagh, D.G.2    Pereyra, F.3    Zaunders, J.J.4    Mackey, E.W.5
  • 51
    • 0037040351 scopus 로고    scopus 로고
    • CTLA-4 upregulation during HIV infection: association with anergy and possible target for therapeutic intervention
    • Leng Q, Bentwich Z, Magen E, Kalinkovich A, Borkow G, (2002) CTLA-4 upregulation during HIV infection: association with anergy and possible target for therapeutic intervention. AIDS 16: 519-529.
    • (2002) AIDS , vol.16 , pp. 519-529
    • Leng, Q.1    Bentwich, Z.2    Magen, E.3    Kalinkovich, A.4    Borkow, G.5
  • 52
    • 0025733252 scopus 로고
    • Serine phosphorylation-independent downregulation of cell-surface CD4 by nef
    • Garcia JV, Miller AD, (1991) Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature 350: 508-511.
    • (1991) Nature , vol.350 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 53
    • 0028128822 scopus 로고
    • Myristoylation-dependent binding of HIV-1 Nef to CD4
    • Harris MP, Neil JC, (1994) Myristoylation-dependent binding of HIV-1 Nef to CD4. J Mol Biol 241: 136-142.
    • (1994) J Mol Biol , vol.241 , pp. 136-142
    • Harris, M.P.1    Neil, J.C.2
  • 54
    • 0030958508 scopus 로고    scopus 로고
    • Identification of regions in HIV-1 Nef required for efficient downregulation of cell surface CD4
    • Hua J, Blair W, Truant R, Cullen BR, (1997) Identification of regions in HIV-1 Nef required for efficient downregulation of cell surface CD4. Virology 231: 231-238.
    • (1997) Virology , vol.231 , pp. 231-238
    • Hua, J.1    Blair, W.2    Truant, R.3    Cullen, B.R.4
  • 55
    • 0032076086 scopus 로고    scopus 로고
    • Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4
    • Lu X, Yu H, Liu SH, Brodsky FM, Peterlin BM, (1998) Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4. Immunity 8: 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
  • 56
    • 19244382596 scopus 로고    scopus 로고
    • Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions
    • Liu LX, Heveker N, Fackler OT, Arold S, Le Gall S, et al. (2000) Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions. J Virol 74: 5310-5319.
    • (2000) J Virol , vol.74 , pp. 5310-5319
    • Liu, L.X.1    Heveker, N.2    Fackler, O.T.3    Arold, S.4    Le Gall, S.5
  • 57
    • 0033515427 scopus 로고    scopus 로고
    • Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes
    • Piguet V, Gu F, Foti M, Demaurex N, Gruenberg J, et al. (1999) Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes. Cell 97: 63-73.
    • (1999) Cell , vol.97 , pp. 63-73
    • Piguet, V.1    Gu, F.2    Foti, M.3    Demaurex, N.4    Gruenberg, J.5
  • 58
    • 0027450321 scopus 로고
    • The negative effect of human immunodeficiency virus type 1 Nef on cell surface CD4 expression is not species specific and requires the cytoplasmic domain of CD4
    • Garcia JV, Alfano J, Miller AD, (1993) The negative effect of human immunodeficiency virus type 1 Nef on cell surface CD4 expression is not species specific and requires the cytoplasmic domain of CD4. J Virol 67: 1511-1516.
    • (1993) J Virol , vol.67 , pp. 1511-1516
    • Garcia, J.V.1    Alfano, J.2    Miller, A.D.3
  • 59
    • 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 YH, et al. (2002) 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: 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
  • 60
    • 71849085384 scopus 로고    scopus 로고
    • HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4+ T cells
    • Lenassi M, Cagney G, Liao M, Vaupotic T, Bartholomeeusen K, et al. (2010) HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4+ T cells. Traffic 11: 110-122.
    • (2010) Traffic , vol.11 , pp. 110-122
    • Lenassi, M.1    Cagney, G.2    Liao, M.3    Vaupotic, T.4    Bartholomeeusen, K.5
  • 61
    • 1542317632 scopus 로고    scopus 로고
    • Extracellular Nef protein targets CD4+ T cells for apoptosis by interacting with CXCR4 surface receptors
    • James CO, Huang MB, Khan M, Garcia-Barrio M, Powell MD, et al. (2004) Extracellular Nef protein targets CD4+ T cells for apoptosis by interacting with CXCR4 surface receptors. J Virol 78: 3099-3109.
    • (2004) J Virol , vol.78 , pp. 3099-3109
    • James, C.O.1    Huang, M.B.2    Khan, M.3    Garcia-Barrio, M.4    Powell, M.D.5
  • 62
    • 33645288761 scopus 로고    scopus 로고
    • Human immunodeficiency virus 1 Nef suppresses CD40-dependent immunoglobulin class switching in bystander B cells
    • Qiao X, He B, Chiu A, Knowles DM, Chadburn A, et al. (2006) Human immunodeficiency virus 1 Nef suppresses CD40-dependent immunoglobulin class switching in bystander B cells. Nat Immunol 7: 302-310.
    • (2006) Nat Immunol , vol.7 , pp. 302-310
    • Qiao, X.1    He, B.2    Chiu, A.3    Knowles, D.M.4    Chadburn, A.5
  • 63
    • 45949087129 scopus 로고    scopus 로고
    • Immune activation driven by CTLA-4 blockade augments viral replication at mucosal sites in simian immunodeficiency virus infection
    • Cecchinato V, Tryniszewska E, Ma ZM, Vaccari M, Boasso A, et al. (2008) Immune activation driven by CTLA-4 blockade augments viral replication at mucosal sites in simian immunodeficiency virus infection. J Immunol 180: 5439-5447.
    • (2008) J Immunol , vol.180 , pp. 5439-5447
    • Cecchinato, V.1    Tryniszewska, E.2    Ma, Z.M.3    Vaccari, M.4    Boasso, A.5


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