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Volumn 26, Issue 2, 2015, Pages 159-173

Nef, the shuttling molecular adaptor of HIV, influences the cytokine network

Author keywords

Cell to cell transfer; HIV; Nef; TNFalpha; Type I IFN

Indexed keywords

BETA INTERFERON; CD4 ANTIGEN; CD40 ANTIGEN; CELL SURFACE RECEPTOR; COMPLEMENT COMPONENT C3; CYTOKINE; HEMATOPOIETIC CELL KINASE; HLA A ANTIGEN; HLA B ANTIGEN; INTERFERON REGULATORY FACTOR 1; INTERFERON REGULATORY FACTOR 3; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NEF PROTEIN; P21 ACTIVATED KINASE 2; PROTEIN KINASE LCK; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 5; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; VAV PROTEIN; VIF PROTEIN; VPU PROTEIN; INTERFERON;

EID: 84926518716     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.11.010     Document Type: Review
Times cited : (15)

References (179)
  • 1
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins- ensuring viral survival in a hostile environment
    • Malim M.H., Emerman M. HIV-1 accessory proteins- ensuring viral survival in a hostile environment. Cell Host Microbe 2008, 3:388-398.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 2
    • 84894435407 scopus 로고    scopus 로고
    • Dendritic cells in progression and pathology of HIV infection
    • Manches O., Frleta D., Bhardwaj N. Dendritic cells in progression and pathology of HIV infection. Trends Immunol 2014, 35:114-122.
    • (2014) Trends Immunol , vol.35 , pp. 114-122
    • Manches, O.1    Frleta, D.2    Bhardwaj, N.3
  • 3
    • 0027043276 scopus 로고
    • Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene
    • Daniel M.D., Kirchhoff F., Czajak S.C., Sehgal P.K., Desrosiers R.C. Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene. Science 1992, 258:1938-1941.
    • (1992) Science , vol.258 , pp. 1938-1941
    • Daniel, M.D.1    Kirchhoff, F.2    Czajak, S.C.3    Sehgal, P.K.4    Desrosiers, R.C.5
  • 4
    • 0028804160 scopus 로고
    • Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients
    • Deacon N.J., Tsykin A., Solomon A., Smith K., Ludford-Menting M., Hooker D.J., et al. Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients. Science 1995, 270:988-991.
    • (1995) Science , vol.270 , pp. 988-991
    • Deacon, N.J.1    Tsykin, A.2    Solomon, A.3    Smith, K.4    Ludford-Menting, M.5    Hooker, D.J.6
  • 5
    • 0030896502 scopus 로고    scopus 로고
    • Deletion of nef slows but does not prevent CD4-positive T-cell depletion in human immunodeficiency virus type 1-infected human-PBL-SCID mice
    • Gulizia R.J., Collman R.G., Levy J.A., Trono D., Mosier D.E. Deletion of nef slows but does not prevent CD4-positive T-cell depletion in human immunodeficiency virus type 1-infected human-PBL-SCID mice. J Virol 1997, 71:4161-4164.
    • (1997) J Virol , vol.71 , pp. 4161-4164
    • Gulizia, R.J.1    Collman, R.G.2    Levy, J.A.3    Trono, D.4    Mosier, D.E.5
  • 6
    • 0025743306 scopus 로고
    • Importance of the nef gene for maintenance of high virus loads and for development of AIDS
    • Kestler HWr, Ringler D.J., Mori K., Panicali D.L., Sehgal P.K., Daniel M.D., et al. Importance of the nef gene for maintenance of high virus loads and for development of AIDS. Cell 1991, 65:651-662.
    • (1991) Cell , vol.65 , pp. 651-662
    • Kestler, H.W.R1    Ringler, D.J.2    Mori, K.3    Panicali, D.L.4    Sehgal, P.K.5    Daniel, M.D.6
  • 7
    • 0028835788 scopus 로고
    • Brief report: absence of intact nef sequences in a long-term survivor with nonprogressive HIV-1 infection
    • Kirchhoff F., Greenough T.C., Brettler D.B., Sullivan J.L., Desrosiers R.C. Brief report: absence of intact nef sequences in a long-term survivor with nonprogressive HIV-1 infection. N Engl J Med 1995, 332:228-232.
    • (1995) N Engl J Med , vol.332 , pp. 228-232
    • Kirchhoff, F.1    Greenough, T.C.2    Brettler, D.B.3    Sullivan, J.L.4    Desrosiers, R.C.5
  • 8
    • 0032538278 scopus 로고    scopus 로고
    • Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice
    • Hanna Z., Kay D.G., Rebai N., Guimond A., Jothy S., Jolicoeur P. Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice. Cell 1998, 95:163-175.
    • (1998) Cell , vol.95 , pp. 163-175
    • Hanna, Z.1    Kay, D.G.2    Rebai, N.3    Guimond, A.4    Jothy, S.5    Jolicoeur, P.6
  • 9
    • 84856475012 scopus 로고    scopus 로고
    • The CD4C/HIVNef transgenic model of aids
    • Jolicoeur P. The CD4C/HIVNef transgenic model of aids. Curr HIV Res 2011, 9:524-530.
    • (2011) Curr HIV Res , vol.9 , pp. 524-530
    • Jolicoeur, P.1
  • 10
    • 0035943355 scopus 로고    scopus 로고
    • Selective transcription and modulation of resting T cell activity by preintegrated HIV DNA
    • Wu Y., Marsh J.W. Selective transcription and modulation of resting T cell activity by preintegrated HIV DNA. Science 2001, 293:1503-1506.
    • (2001) Science , vol.293 , pp. 1503-1506
    • Wu, Y.1    Marsh, J.W.2
  • 11
    • 0141632798 scopus 로고    scopus 로고
    • Early transcription from nonintegrated DNA in human immunodeficiency virus infection
    • Wu Y., Marsh J.W. Early transcription from nonintegrated DNA in human immunodeficiency virus infection. J Virol 2003, 77:10376-10382.
    • (2003) J Virol , vol.77 , pp. 10376-10382
    • Wu, Y.1    Marsh, J.W.2
  • 12
    • 39449110192 scopus 로고    scopus 로고
    • Human macrophages support persistent transcription from unintegrated HIV-1 DNA
    • Kelly J., Beddall M.H., Yu D., Iyer S.R., Marsh J.W., Wu Y. Human macrophages support persistent transcription from unintegrated HIV-1 DNA. Virology 2008, 372:300-312.
    • (2008) Virology , vol.372 , pp. 300-312
    • Kelly, J.1    Beddall, M.H.2    Yu, D.3    Iyer, S.R.4    Marsh, J.W.5    Wu, Y.6
  • 13
    • 0028018287 scopus 로고
    • Cellular distribution of HIV type 1 Nef protein: identification of domains in Nef required for association with membrane and detergent-insoluble cellular matrix
    • Kaminchik J., Margalit R., Yaish S., Drummer H., Amit B., Sarver N., et al. Cellular distribution of HIV type 1 Nef protein: identification of domains in Nef required for association with membrane and detergent-insoluble cellular matrix. AIDS Res Hum Retroviruses 1994, 10:1003-1010.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 1003-1010
    • Kaminchik, J.1    Margalit, R.2    Yaish, S.3    Drummer, H.4    Amit, B.5    Sarver, N.6
  • 14
    • 33644584737 scopus 로고    scopus 로고
    • Role of myristoylation and N-terminal basic residues in membrane association of the human immunodeficiency virus type 1 Nef protein
    • Bentham M., Mazaleyrat S., Harris M. Role of myristoylation and N-terminal basic residues in membrane association of the human immunodeficiency virus type 1 Nef protein. J Gen Virol 2006, 87:563-571.
    • (2006) J Gen Virol , vol.87 , pp. 563-571
    • Bentham, M.1    Mazaleyrat, S.2    Harris, M.3
  • 15
    • 77950421393 scopus 로고    scopus 로고
    • HIV-1 Nef membrane association depends on charge, curvature, composition and sequence
    • Gerlach H., Laumann V., Martens S., Becker C., Goody R., Geyer M. HIV-1 Nef membrane association depends on charge, curvature, composition and sequence. Nat Chem Biol 2010, 6:46-53.
    • (2010) Nat Chem Biol , vol.6 , pp. 46-53
    • Gerlach, H.1    Laumann, V.2    Martens, S.3    Becker, C.4    Goody, R.5    Geyer, M.6
  • 16
    • 67649403753 scopus 로고    scopus 로고
    • HIV-1 Nef perturbs artificial membranes: investigation of the contribution of the myristoyl anchor
    • Szilluweit R., Boll A., Lukowski S., Gerlach H., Fackler O., Geyer M., et al. HIV-1 Nef perturbs artificial membranes: investigation of the contribution of the myristoyl anchor. Biophys J 2009, 96:3242-3250.
    • (2009) Biophys J , vol.96 , pp. 3242-3250
    • Szilluweit, R.1    Boll, A.2    Lukowski, S.3    Gerlach, H.4    Fackler, O.5    Geyer, M.6
  • 17
    • 0034894379 scopus 로고    scopus 로고
    • Structure-function relationships in HIV-1 Nef
    • Geyer M., Fackler O.T., Peterlin B.M. Structure-function relationships in HIV-1 Nef. EMBO Rep 2001, 2:580-585.
    • (2001) EMBO Rep , vol.2 , pp. 580-585
    • Geyer, M.1    Fackler, O.T.2    Peterlin, B.M.3
  • 18
    • 0027999147 scopus 로고
    • A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease
    • Freund J., Kellner R., Konvalinka J., Wolber V., Krausslich H.G., Kalbitzer H.R. A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease. Eur J Biochem 1994, 223:589-593.
    • (1994) Eur J Biochem , vol.223 , pp. 589-593
    • Freund, J.1    Kellner, R.2    Konvalinka, J.3    Wolber, V.4    Krausslich, H.G.5    Kalbitzer, H.R.6
  • 19
    • 33144469859 scopus 로고    scopus 로고
    • Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef
    • Breuer S., Gerlach H., Kolaric B., Urbanke C., Opitz N., Geyer M. Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef. Biochemistry 2006, 45:2339-2349.
    • (2006) Biochemistry , vol.45 , pp. 2339-2349
    • Breuer, S.1    Gerlach, H.2    Kolaric, B.3    Urbanke, C.4    Opitz, N.5    Geyer, M.6
  • 20
    • 24644466459 scopus 로고    scopus 로고
    • Co-translational myristoylation alters the quaternary structure of HIV-1 Nef in solution
    • Dennis C.A., Baron A., Grossmann J.G., Mazaleyrat S., Harris M., Jaeger J. Co-translational myristoylation alters the quaternary structure of HIV-1 Nef in solution. Proteins 2005, 60:658-669.
    • (2005) Proteins , vol.60 , pp. 658-669
    • Dennis, C.A.1    Baron, A.2    Grossmann, J.G.3    Mazaleyrat, S.4    Harris, M.5    Jaeger, J.6
  • 21
    • 0031572847 scopus 로고    scopus 로고
    • The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling
    • Arold S., Franken P., Strub M.P., Hoh F., Benichou S., Benarous R., et al. The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. Structure 1997, 5:1361-1372.
    • (1997) Structure , vol.5 , pp. 1361-1372
    • Arold, S.1    Franken, P.2    Strub, M.P.3    Hoh, F.4    Benichou, S.5    Benarous, R.6
  • 23
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 1996, 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
  • 24
    • 0033612388 scopus 로고    scopus 로고
    • Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein
    • Geyer M., Munte C.E., Schorr J., Kellner R., Kalbitzer H.R. Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. J Mol Biol 1999, 289:123-138.
    • (1999) J Mol Biol , vol.289 , pp. 123-138
    • Geyer, M.1    Munte, C.E.2    Schorr, J.3    Kellner, R.4    Kalbitzer, H.R.5
  • 25
    • 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., Baur A.S. Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein. Trends Biochem Sci 2001, 26:356-363.
    • (2001) Trends Biochem Sci , vol.26 , pp. 356-363
    • Arold, S.T.1    Baur, A.S.2
  • 26
    • 84901008609 scopus 로고    scopus 로고
    • Heterologous Src homology 4 domains support membrane anchoring and biological activity of HIV-1 Nef
    • Geist M.M., Pan X., Bender S., Bartenschlager R., Nickel W., Fackler O.T. Heterologous Src homology 4 domains support membrane anchoring and biological activity of HIV-1 Nef. J Biol Chem 2014, 289:14030-14044.
    • (2014) J Biol Chem , vol.289 , pp. 14030-14044
    • Geist, M.M.1    Pan, X.2    Bender, S.3    Bartenschlager, R.4    Nickel, W.5    Fackler, O.T.6
  • 27
    • 10744228109 scopus 로고    scopus 로고
    • HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane
    • Witte V., Laffert B., Rosorius O., Lischka P., Blume K., Galler G., et al. HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane. Mol Cell 2004, 13:179-190.
    • (2004) Mol Cell , vol.13 , pp. 179-190
    • Witte, V.1    Laffert, B.2    Rosorius, O.3    Lischka, P.4    Blume, K.5    Galler, G.6
  • 28
    • 0034948709 scopus 로고    scopus 로고
    • Nef triggers a transcriptional program in T cells imitating single-signal T cell activation and inducing HIV virulence mediators
    • Simmons A., Aluvihare V., McMichael A. Nef triggers a transcriptional program in T cells imitating single-signal T cell activation and inducing HIV virulence mediators. Immunity 2001, 14:763-777.
    • (2001) Immunity , vol.14 , pp. 763-777
    • Simmons, A.1    Aluvihare, V.2    McMichael, A.3
  • 29
    • 18844363668 scopus 로고    scopus 로고
    • Biology of the HIV Nef protein
    • Das S.R., Jameel S. Biology of the HIV Nef protein. Indian J Med Res 2005, 121:315-332.
    • (2005) Indian J Med Res , vol.121 , pp. 315-332
    • Das, S.R.1    Jameel, S.2
  • 30
    • 79958770579 scopus 로고    scopus 로고
    • Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly
    • Horenkamp F.A., Breuer S., Schulte A., Lülf S., Weyand M., Saksela K., et al. Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. Traffic 2011, 12(7):867-877.
    • (2011) Traffic , vol.12 , Issue.7 , pp. 867-877
    • Horenkamp, F.A.1    Breuer, S.2    Schulte, A.3    Lülf, S.4    Weyand, M.5    Saksela, K.6
  • 31
    • 84898733948 scopus 로고    scopus 로고
    • How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4
    • Ren X., Park S.Y., Bonifacino J.S., Hurley J.H. How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4. eLife 2014, 3:e01754.
    • (2014) eLife , vol.3 , pp. e01754
    • Ren, X.1    Park, S.Y.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 32
    • 0037074008 scopus 로고    scopus 로고
    • HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway
    • Blagoveshchenskaya A.D., Thomas L., Feliciangeli S.F., Hung C.H., Thomas G. HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell 2002, 111:853-866.
    • (2002) Cell , vol.111 , pp. 853-866
    • Blagoveshchenskaya, A.D.1    Thomas, L.2    Feliciangeli, S.F.3    Hung, C.H.4    Thomas, G.5
  • 33
    • 0034312298 scopus 로고    scopus 로고
    • The plasma membrane as a combat zone in the HIV battlefield
    • Doms R.W., Trono D. The plasma membrane as a combat zone in the HIV battlefield. Genes Dev 2000, 14:2677-2688.
    • (2000) Genes Dev , vol.14 , pp. 2677-2688
    • Doms, R.W.1    Trono, D.2
  • 34
    • 84856499935 scopus 로고    scopus 로고
    • One protein to rule them all: modulation of cell surface receptors and molecules by HIV Nef
    • Landi A., Iannucci V., Nuffel A.V., Meuwissen P., Verhasselt B. One protein to rule them all: modulation of cell surface receptors and molecules by HIV Nef. Curr HIV Res 2011, 9:496-504.
    • (2011) Curr HIV Res , vol.9 , pp. 496-504
    • Landi, A.1    Iannucci, V.2    Nuffel, A.V.3    Meuwissen, P.4    Verhasselt, B.5
  • 35
    • 84911497235 scopus 로고    scopus 로고
    • HIV-1 Nef and Vpu are functionally redundant broad-spectrum modulators of cell surface receptors including tetraspanins
    • Haller C., Müller B., Fritz J.V., Lamas-Murua M., Stolp B., Pujol F., et al. HIV-1 Nef and Vpu are functionally redundant broad-spectrum modulators of cell surface receptors including tetraspanins. J Virol 2014, 88:14241-14257.
    • (2014) J Virol , vol.88 , pp. 14241-14257
    • Haller, C.1    Müller, B.2    Fritz, J.V.3    Lamas-Murua, M.4    Stolp, B.5    Pujol, F.6
  • 36
    • 0027209701 scopus 로고
    • Nef from primary isolates of human immunodeficiency virus type 1 suppresses surface CD4 expression in human and mouse T cells
    • Anderson S., Shugars D.C., Swanstrom R., Garcia J.V. Nef from primary isolates of human immunodeficiency virus type 1 suppresses surface CD4 expression in human and mouse T cells. J Virol 1993, 67:4923-4931.
    • (1993) J Virol , vol.67 , pp. 4923-4931
    • Anderson, S.1    Shugars, D.C.2    Swanstrom, R.3    Garcia, J.V.4
  • 37
    • 25444510358 scopus 로고    scopus 로고
    • The Nef protein of HIV-1 induces loss of cell surface costimulatory molecules CD80 and CD86 in APCs
    • Chaudhry A., Das S.R., Hussain A., Mayor S., George A., Bal V., et al. The Nef protein of HIV-1 induces loss of cell surface costimulatory molecules CD80 and CD86 in APCs. J Immunol 2005, 175:4566-4574.
    • (2005) J Immunol , vol.175 , pp. 4566-4574
    • Chaudhry, A.1    Das, S.R.2    Hussain, A.3    Mayor, S.4    George, A.5    Bal, V.6
  • 38
    • 0033819615 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef mediates sustained membrane expression of tumor necrosis factor and the related cytokine LIGHT on activated T cells
    • Lama J., Ware C.F. Human immunodeficiency virus type 1 Nef mediates sustained membrane expression of tumor necrosis factor and the related cytokine LIGHT on activated T cells. J Virol 2000, 74:9396-9402.
    • (2000) J Virol , vol.74 , pp. 9396-9402
    • Lama, J.1    Ware, C.F.2
  • 39
    • 20044362379 scopus 로고    scopus 로고
    • Nef-induced alteration of the early/recycling endosomal compartment correlates with enhancement of HIV-1 infectivity
    • Madrid R., Janvier K., Hitchin D., Day J., Coleman S., Noviello C., et al. Nef-induced alteration of the early/recycling endosomal compartment correlates with enhancement of HIV-1 infectivity. J Biol Chem 2005, 280:5032-5044.
    • (2005) J Biol Chem , vol.280 , pp. 5032-5044
    • Madrid, R.1    Janvier, K.2    Hitchin, D.3    Day, J.4    Coleman, S.5    Noviello, C.6
  • 40
    • 0141521574 scopus 로고    scopus 로고
    • Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles
    • Schindler M., Würfl S., Benaroch P., Greenough T.C., Daniels R., Easterbrook P., et al. Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles. J Virol 2003, 77:10548-10556.
    • (2003) J Virol , vol.77 , pp. 10548-10556
    • Schindler, M.1    Würfl, S.2    Benaroch, P.3    Greenough, T.C.4    Daniels, R.5    Easterbrook, P.6
  • 41
    • 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 J.M. Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat Med 1996, 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
  • 42
    • 0036169006 scopus 로고    scopus 로고
    • HIV-1 Nef-induced upregulation of DC-SIGN in dendritic cells promotes lymphocyte clustering and viral spread
    • Sol-Foulon N., Moris A., Nobile C., Boccaccio C., Engering A., Abastado J.P., et al. HIV-1 Nef-induced upregulation of DC-SIGN in dendritic cells promotes lymphocyte clustering and viral spread. Immunity 2002, 16:145-155.
    • (2002) Immunity , vol.16 , pp. 145-155
    • Sol-Foulon, N.1    Moris, A.2    Nobile, C.3    Boccaccio, C.4    Engering, A.5    Abastado, J.P.6
  • 43
    • 23844471509 scopus 로고    scopus 로고
    • Human immunodeficiency virus Nef induces rapid internalization of the T-cell coreceptor CD8alphabeta
    • Stove V., Van de Walle I., Naessens E., Coene E., Stove C., Plum J., et al. Human immunodeficiency virus Nef induces rapid internalization of the T-cell coreceptor CD8alphabeta. J Virol 2005, 79:11422-11433.
    • (2005) J Virol , vol.79 , pp. 11422-11433
    • Stove, V.1    Van de Walle, I.2    Naessens, E.3    Coene, E.4    Stove, C.5    Plum, J.6
  • 45
    • 33845513921 scopus 로고    scopus 로고
    • Dynamic interaction of HIV-1 Nef with the clathrin-mediated endocytic pathway at the plasma membrane
    • Burtey A., Rappoport J.Z., Bouchet J., Basmaciogullari S., Guatelli J., Simon S.M., et al. Dynamic interaction of HIV-1 Nef with the clathrin-mediated endocytic pathway at the plasma membrane. Traffic 2007, 8:61-76.
    • (2007) Traffic , vol.8 , pp. 61-76
    • Burtey, A.1    Rappoport, J.Z.2    Bouchet, J.3    Basmaciogullari, S.4    Guatelli, J.5    Simon, S.M.6
  • 46
    • 33745122662 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways
    • Roeth J.F., Collins K.L. Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways. Microbiol Mol Biol Rev 2006, 70:548-563.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 548-563
    • Roeth, J.F.1    Collins, K.L.2
  • 47
    • 0034134113 scopus 로고    scopus 로고
    • Interactions of HIV-1 NEF with cellular signal transducing proteins
    • Renkema G.H., Saksela K. Interactions of HIV-1 NEF with cellular signal transducing proteins. Front Biosci 2000, 5:D268-D283.
    • (2000) Front Biosci , vol.5 , pp. D268-D283
    • Renkema, G.H.1    Saksela, K.2
  • 48
    • 84871795476 scopus 로고    scopus 로고
    • HIV-1 Nef: a multifaceted modulator of T cell receptor signaling
    • Abraham L., Fackler O.T. HIV-1 Nef: a multifaceted modulator of T cell receptor signaling. Cell Commun Signal 2012, 10:39.
    • (2012) Cell Commun Signal , vol.10 , pp. 39
    • Abraham, L.1    Fackler, O.T.2
  • 49
    • 2942555187 scopus 로고    scopus 로고
    • A novel role for p21-activated protein kinase 2 in T cell activation
    • Chu P.C., Wu J., Liao X.C., Pardo J., Zhao H., Li C., et al. A novel role for p21-activated protein kinase 2 in T cell activation. J Immunol 2004, 172:7324-7334.
    • (2004) J Immunol , vol.172 , pp. 7324-7334
    • Chu, P.C.1    Wu, J.2    Liao, X.C.3    Pardo, J.4    Zhao, H.5    Li, C.6
  • 51
    • 0035128420 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef selectively associates with a catalytically active subpopulation of p21-activated kinase 2 (PAK2) independently of PAK2 binding to Nck or beta-PIX
    • Renkema G.H., Manninen A., Saksela K. Human immunodeficiency virus type 1 Nef selectively associates with a catalytically active subpopulation of p21-activated kinase 2 (PAK2) independently of PAK2 binding to Nck or beta-PIX. J Virol 2001, 75:2154-2160.
    • (2001) J Virol , vol.75 , pp. 2154-2160
    • Renkema, G.H.1    Manninen, A.2    Saksela, K.3
  • 52
    • 12144291075 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts
    • Krautkrämer E., Giese S.I., Gasteier J.E., Muranyi W., Fackler O.T. Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts. J Virol 2004, 78:4085-4097.
    • (2004) J Virol , vol.78 , pp. 4085-4097
    • Krautkrämer, E.1    Giese, S.I.2    Gasteier, J.E.3    Muranyi, W.4    Fackler, O.T.5
  • 53
    • 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., Saksela K. Nef associates with p21-activated kinase 2 in a p21-GTPase-dependent dynamic activation complex within lipid rafts. J Virol 2004, 78:12773-12780.
    • (2004) J Virol , vol.78 , pp. 12773-12780
    • Pulkkinen, K.1    Renkema, G.H.2    Kirchhoff, F.3    Saksela, K.4
  • 54
    • 79961104556 scopus 로고    scopus 로고
    • Nef-mediated enhancement of cellular activation and human immunodeficiency virus type 1 replication in primary T cells is dependent on association with p21-activated kinase 2
    • Olivieri K.C., Mukerji J., Gabuzda D. Nef-mediated enhancement of cellular activation and human immunodeficiency virus type 1 replication in primary T cells is dependent on association with p21-activated kinase 2. Retrovirology 2011, 8:64.
    • (2011) Retrovirology , vol.8 , pp. 64
    • Olivieri, K.C.1    Mukerji, J.2    Gabuzda, D.3
  • 55
    • 0032750417 scopus 로고    scopus 로고
    • Activation of the PAK-related kinase by human immunodeficiency virus type 1 Nef in primary human peripheral blood lymphocytes and macrophages leads to phosphorylation of a PIX-p95 complex
    • Brown A., Wang X., Sawai E., Cheng-Mayer C. Activation of the PAK-related kinase by human immunodeficiency virus type 1 Nef in primary human peripheral blood lymphocytes and macrophages leads to phosphorylation of a PIX-p95 complex. J Virol 1999, 73:9899-9907.
    • (1999) J Virol , vol.73 , pp. 9899-9907
    • Brown, A.1    Wang, X.2    Sawai, E.3    Cheng-Mayer, C.4
  • 56
    • 0036533633 scopus 로고    scopus 로고
    • TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/zeta complex
    • Blanchard N., Lankar D., Faure F., Regnault A., Dumont C., Raposo G., et al. TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/zeta complex. J Immunol 2002, 168:3235-3241.
    • (2002) J Immunol , vol.168 , pp. 3235-3241
    • Blanchard, N.1    Lankar, D.2    Faure, F.3    Regnault, A.4    Dumont, C.5    Raposo, G.6
  • 57
    • 84856482631 scopus 로고    scopus 로고
    • Interactions of the HIV/SIV pathogenicity factor Nef with SH3 domain-containing host cell proteins
    • Saksela K. Interactions of the HIV/SIV pathogenicity factor Nef with SH3 domain-containing host cell proteins. Curr HIV Res 2011, 9:531-542.
    • (2011) Curr HIV Res , vol.9 , pp. 531-542
    • Saksela, K.1
  • 58
    • 0033519235 scopus 로고    scopus 로고
    • Induction of Fas ligand expression by HIV involves the interaction of Nef with the T cell receptor zeta chain
    • Xu X.N., Laffert B., Screaton G.R., Kraft M., Wolf D., Kolanus W., et al. Induction of Fas ligand expression by HIV involves the interaction of Nef with the T cell receptor zeta chain. J Exp Med 1999, 189:1489-1496.
    • (1999) J Exp Med , vol.189 , pp. 1489-1496
    • Xu, X.N.1    Laffert, B.2    Screaton, G.R.3    Kraft, M.4    Wolf, D.5    Kolanus, W.6
  • 59
    • 0030744349 scopus 로고    scopus 로고
    • Evasion of cytotoxic T lymphocyte (CTL) responses by nef-dependent induction of Fas ligand (CD95L) expression on simian immunodeficiency virus-infected cells
    • Xu X.N., Screaton G.R., Gotch F.M., Dong T., Tan R., Almond N., et al. Evasion of cytotoxic T lymphocyte (CTL) responses by nef-dependent induction of Fas ligand (CD95L) expression on simian immunodeficiency virus-infected cells. J Exp Med 1997, 186:7-16.
    • (1997) J Exp Med , vol.186 , pp. 7-16
    • Xu, X.N.1    Screaton, G.R.2    Gotch, F.M.3    Dong, T.4    Tan, R.5    Almond, N.6
  • 61
    • 0035848864 scopus 로고    scopus 로고
    • HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell
    • Geleziunas R., Xu W., Takeda K., Ichijo H., Greene W.C. HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell. Nature 2001, 410:834-838.
    • (2001) Nature , vol.410 , pp. 834-838
    • Geleziunas, R.1    Xu, W.2    Takeda, K.3    Ichijo, H.4    Greene, W.C.5
  • 62
    • 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., et al. HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals. Nat Med 2001, 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    Trapp, S.6
  • 63
    • 0036187980 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis
    • Greenway A.L., McPhee D.A., Allen K., Johnstone R., Holloway G., Mills J., et al. Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis. J Virol 2002, 76:2692-2702.
    • (2002) J Virol , vol.76 , pp. 2692-2702
    • Greenway, A.L.1    McPhee, D.A.2    Allen, K.3    Johnstone, R.4    Holloway, G.5    Mills, J.6
  • 64
    • 33745070227 scopus 로고    scopus 로고
    • Nef-mediated suppression of T cell activation was lost in a lentiviral lineage that gave rise to HIV-1
    • Schindler M., Münch J., Kutsch O., Li H., Santiago M.L., Bibollet-Ruche F., et al. Nef-mediated suppression of T cell activation was lost in a lentiviral lineage that gave rise to HIV-1. Cell 2006, 125:1055-1067.
    • (2006) Cell , vol.125 , pp. 1055-1067
    • Schindler, M.1    Münch, J.2    Kutsch, O.3    Li, H.4    Santiago, M.L.5    Bibollet-Ruche, F.6
  • 67
    • 84896715854 scopus 로고    scopus 로고
    • HIV Nef expression favors the relative preservation of CD4+ T regulatory cells that retain some important suppressive functions
    • Chrobak P., Afkhami S., Priceputu E., Poudrier J., Meunier C., Hanna Z., et al. HIV Nef expression favors the relative preservation of CD4+ T regulatory cells that retain some important suppressive functions. J Immunol 2014, 192:1681-1692.
    • (2014) J Immunol , vol.192 , pp. 1681-1692
    • Chrobak, P.1    Afkhami, S.2    Priceputu, E.3    Poudrier, J.4    Meunier, C.5    Hanna, Z.6
  • 68
    • 84859577716 scopus 로고    scopus 로고
    • HIV-1 Nef transfer and intracellular signalling in uninfected cells
    • InTech Open Access Publisher, Rijeka, Croatia, T.L. Chang (Ed.)
    • Percario Z., Mangino G., Gallo G., Chiantore M., Fiorucci G., Romeo G., et al. HIV-1 Nef transfer and intracellular signalling in uninfected cells. HIV-host interactions 2011, 61-78. InTech Open Access Publisher, Rijeka, Croatia. T.L. Chang (Ed.).
    • (2011) HIV-host interactions , pp. 61-78
    • Percario, Z.1    Mangino, G.2    Gallo, G.3    Chiantore, M.4    Fiorucci, G.5    Romeo, G.6
  • 69
    • 33947390903 scopus 로고    scopus 로고
    • In vitro treatment of human monocytes/macrophages with myristoylated recombinant Nef of human immunodeficiency virus type 1 leads to the activation of mitogen-activated protein kinases, IkappaB kinases, and interferon regulatory factor 3 and to the release of beta interferon
    • Mangino G., Percario Z., Fiorucci G., Vaccari G., Manrique S., Romeo G., et al. In vitro treatment of human monocytes/macrophages with myristoylated recombinant Nef of human immunodeficiency virus type 1 leads to the activation of mitogen-activated protein kinases, IkappaB kinases, and interferon regulatory factor 3 and to the release of beta interferon. J Virol 2007, 81:2777-2791.
    • (2007) J Virol , vol.81 , pp. 2777-2791
    • Mangino, G.1    Percario, Z.2    Fiorucci, G.3    Vaccari, G.4    Manrique, S.5    Romeo, G.6
  • 70
    • 0037441996 scopus 로고    scopus 로고
    • HIV-1 Nef induces the release of inflammatory factors from human monocyte/macrophages: involvement of Nef endocytotic signals and NF-kappaB activation
    • Olivetta E., Percario Z., Fiorucci G., Mattia G., Schiavoni I., Dennis C., et al. HIV-1 Nef induces the release of inflammatory factors from human monocyte/macrophages: involvement of Nef endocytotic signals and NF-kappaB activation. J Immunol 2003, 170:1716-1727.
    • (2003) J Immunol , vol.170 , pp. 1716-1727
    • Olivetta, E.1    Percario, Z.2    Fiorucci, G.3    Mattia, G.4    Schiavoni, I.5    Dennis, C.6
  • 71
    • 0036118228 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus-induced complement expression in astrocytes and neurons
    • Speth C., Schabetsberger T., Mohsenipour I., Stöckl G., Würzner R., Stoiber H., et al. Mechanism of human immunodeficiency virus-induced complement expression in astrocytes and neurons. J Virol 2002, 76:3179-3188.
    • (2002) J Virol , vol.76 , pp. 3179-3188
    • Speth, C.1    Schabetsberger, T.2    Mohsenipour, I.3    Stöckl, G.4    Würzner, R.5    Stoiber, H.6
  • 72
    • 0030577001 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef protein on the cell surface is cytocidal for human CD4+ T cells
    • Fujii Y., Otake K., Tashiro M., Adachi A. Human immunodeficiency virus type 1 Nef protein on the cell surface is cytocidal for human CD4+ T cells. FEBS Lett 1996, 393:105-108.
    • (1996) FEBS Lett , vol.393 , pp. 105-108
    • Fujii, Y.1    Otake, K.2    Tashiro, M.3    Adachi, A.4
  • 73
    • 0030480115 scopus 로고    scopus 로고
    • In vitro cytocidal effects of human immunodeficiency virus type 1 Nef on unprimed human CD4+ T cells without MHC restriction
    • Fujii Y., Otake K., Tashiro M., Adachi A. In vitro cytocidal effects of human immunodeficiency virus type 1 Nef on unprimed human CD4+ T cells without MHC restriction. J Gen Virol 1996, 77(Pt 12):2943-2951.
    • (1996) J Gen Virol , vol.77 , pp. 2943-2951
    • Fujii, Y.1    Otake, K.2    Tashiro, M.3    Adachi, A.4
  • 74
    • 0030576919 scopus 로고    scopus 로고
    • Soluble Nef antigen of HIV-1 is cytotoxic for human CD4+ T cells
    • Fujii Y., Otake K., Tashiro M., Adachi A. Soluble Nef antigen of HIV-1 is cytotoxic for human CD4+ T cells. FEBS Lett 1996, 393:93-96.
    • (1996) FEBS Lett , vol.393 , pp. 93-96
    • Fujii, Y.1    Otake, K.2    Tashiro, M.3    Adachi, A.4
  • 75
    • 4644289971 scopus 로고    scopus 로고
    • Characterization of Nef-CXCR4 interactions important for apoptosis induction
    • Huang M.B., Jin L.L., James C.O., Khan M., Powell M.D., Bond V.C. Characterization of Nef-CXCR4 interactions important for apoptosis induction. J Virol 2004, 78:11084-11096.
    • (2004) J Virol , vol.78 , pp. 11084-11096
    • Huang, M.B.1    Jin, L.L.2    James, C.O.3    Khan, M.4    Powell, M.D.5    Bond, V.C.6
  • 76
    • 1542317632 scopus 로고    scopus 로고
    • Extracellular Nef protein targets CD4+ T cells for apoptosis by interacting with CXCR4 surface receptors
    • James C.O., Huang M.B., Khan M., Garcia-Barrio M., Powell M.D., Bond V.C. Extracellular Nef protein targets CD4+ T cells for apoptosis by interacting with CXCR4 surface receptors. J Virol 2004, 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    Bond, V.C.6
  • 77
    • 0034537667 scopus 로고    scopus 로고
    • T-tropic human immunodeficiency virus (HIV) type 1 Nef protein enters human monocyte-macrophages and induces resistance to HIV replication: a possible mechanism of HIV T-tropic emergence in AIDS
    • Alessandrini L., Santarcangelo A.C., Olivetta E., Ferrantelli F., d'Aloja P., Pugliese K., et al. T-tropic human immunodeficiency virus (HIV) type 1 Nef protein enters human monocyte-macrophages and induces resistance to HIV replication: a possible mechanism of HIV T-tropic emergence in AIDS. J Gen Virol 2000, 81:2905-2917.
    • (2000) J Gen Virol , vol.81 , pp. 2905-2917
    • Alessandrini, L.1    Santarcangelo, A.C.2    Olivetta, E.3    Ferrantelli, F.4    d'Aloja, P.5    Pugliese, K.6
  • 78
    • 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 D.M., Chadburn A., Cerutti A. Human immunodeficiency virus 1 Nef suppresses CD40-dependent immunoglobulin class switching in bystander B cells. Nat Immunol 2006, 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    Cerutti, A.6
  • 79
    • 0036351906 scopus 로고    scopus 로고
    • HIV-1 Nef induces dendritic cell differentiation: a possible mechanism of uninfected CD4(+) T cell activation
    • Quaranta M.G., Tritarelli E., Giordani L., Viora M. HIV-1 Nef induces dendritic cell differentiation: a possible mechanism of uninfected CD4(+) T cell activation. Exp Cell Res 2002, 275:243-254.
    • (2002) Exp Cell Res , vol.275 , pp. 243-254
    • Quaranta, M.G.1    Tritarelli, E.2    Giordani, L.3    Viora, M.4
  • 80
    • 0242526806 scopus 로고    scopus 로고
    • HIV-1 Nef triggers Vav-mediated signaling pathway leading to functional and morphological differentiation of dendritic cells
    • Quaranta M.G., Mattioli B., Spadaro F., Straface E., Giordani L., Ramoni C., et al. HIV-1 Nef triggers Vav-mediated signaling pathway leading to functional and morphological differentiation of dendritic cells. FASEB J 2003, 17:2025-2036.
    • (2003) FASEB J , vol.17 , pp. 2025-2036
    • Quaranta, M.G.1    Mattioli, B.2    Spadaro, F.3    Straface, E.4    Giordani, L.5    Ramoni, C.6
  • 81
    • 0035525793 scopus 로고    scopus 로고
    • HIV-1 Nef activates STAT1 in human monocytes/macrophages through the release of soluble factors
    • Federico M., Percario Z., Olivetta E., Fiorucci G., Muratori C., Micheli A., et al. HIV-1 Nef activates STAT1 in human monocytes/macrophages through the release of soluble factors. Blood 2001, 98:2752-2761.
    • (2001) Blood , vol.98 , pp. 2752-2761
    • Federico, M.1    Percario, Z.2    Olivetta, E.3    Fiorucci, G.4    Muratori, C.5    Micheli, A.6
  • 82
    • 0347991985 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) Nef activates STAT3 in primary human monocyte/macrophages through the release of soluble factors: involvement of Nef domains interacting with the cell endocytotic machinery
    • Percario Z., Olivetta E., Fiorucci G., Mangino G., Peretti S., Romeo G., et al. Human immunodeficiency virus type 1 (HIV-1) Nef activates STAT3 in primary human monocyte/macrophages through the release of soluble factors: involvement of Nef domains interacting with the cell endocytotic machinery. J Leukoc Biol 2003, 74:821-832.
    • (2003) J Leukoc Biol , vol.74 , pp. 821-832
    • Percario, Z.1    Olivetta, E.2    Fiorucci, G.3    Mangino, G.4    Peretti, S.5    Romeo, G.6
  • 83
    • 80051998389 scopus 로고    scopus 로고
    • HIV-1 Nef induces proinflammatory state in macrophages through its acidic cluster domain: involvement of TNF alpha receptor associated factor 2
    • Mangino G., Percario Z.A., Fiorucci G., Vaccari G., Acconcia F., Chiarabelli C., et al. HIV-1 Nef induces proinflammatory state in macrophages through its acidic cluster domain: involvement of TNF alpha receptor associated factor 2. PLoS One 2011, 6:e22982.
    • (2011) PLoS One , vol.6 , pp. e22982
    • Mangino, G.1    Percario, Z.A.2    Fiorucci, G.3    Vaccari, G.4    Acconcia, F.5    Chiarabelli, C.6
  • 84
    • 0030684068 scopus 로고    scopus 로고
    • Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation
    • Greenberg M.E., Bronson S., Lock M., Neumann M., Pavlakis G.N., Skowronski J. Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation. EMBO J 1997, 16:6964-6976.
    • (1997) EMBO J , vol.16 , pp. 6964-6976
    • Greenberg, M.E.1    Bronson, S.2    Lock, M.3    Neumann, M.4    Pavlakis, G.N.5    Skowronski, J.6
  • 85
    • 0037462825 scopus 로고    scopus 로고
    • Exogenous Nef protein activates NF-kappa B, AP-1, and c-Jun N-terminal kinase and stimulates HIV transcription in promonocytic cells. Role in AIDS pathogenesis
    • Varin A., Manna S.K., Quivy V., Decrion A.Z., Van Lint C., Herbein G., et al. Exogenous Nef protein activates NF-kappa B, AP-1, and c-Jun N-terminal kinase and stimulates HIV transcription in promonocytic cells. Role in AIDS pathogenesis. J Biol Chem 2003, 278:2219-2227.
    • (2003) J Biol Chem , vol.278 , pp. 2219-2227
    • Varin, A.1    Manna, S.K.2    Quivy, V.3    Decrion, A.Z.4    Van Lint, C.5    Herbein, G.6
  • 86
    • 33645910194 scopus 로고    scopus 로고
    • Nef: out and in?
    • Peterlin B. Nef: out and in?. Nat Immunol 2006, 7:229-230.
    • (2006) Nat Immunol , vol.7 , pp. 229-230
    • Peterlin, B.1
  • 87
    • 0024389879 scopus 로고
    • Antibodies to the nef protein and to nef peptides in HIV-1-infected seronegative individuals
    • Ameisen J., Guy B., Chamaret S., Loche M., Mouton Y., Neyrinck J., et al. Antibodies to the nef protein and to nef peptides in HIV-1-infected seronegative individuals. AIDS Res Hum Retroviruses 1989, 5:279-291.
    • (1989) AIDS Res Hum Retroviruses , vol.5 , pp. 279-291
    • Ameisen, J.1    Guy, B.2    Chamaret, S.3    Loche, M.4    Mouton, Y.5    Neyrinck, J.6
  • 88
    • 38849168755 scopus 로고    scopus 로고
    • Membrane nanotubes physically connect T cells over long distances presenting a novel route for HIV-1 transmission
    • Sowinski S., Jolly C., Berninghausen O., Purbhoo M.A., Chauveau A., Köhler K., et al. Membrane nanotubes physically connect T cells over long distances presenting a novel route for HIV-1 transmission. Nat Cell Biol 2008, 10:211-219.
    • (2008) Nat Cell Biol , vol.10 , pp. 211-219
    • Sowinski, S.1    Jolly, C.2    Berninghausen, O.3    Purbhoo, M.A.4    Chauveau, A.5    Köhler, K.6
  • 89
    • 52149109150 scopus 로고    scopus 로고
    • HIV-1 Nef protein is secreted into vesicles that can fuse with target cells and virions
    • S2-S14-9
    • Campbell T.D., Khan M., Huang M.B., Bond V.C., Powell M.D. HIV-1 Nef protein is secreted into vesicles that can fuse with target cells and virions. Ethn Dis 2008, 18. S2-S14-9.
    • (2008) Ethn Dis , vol.18
    • Campbell, T.D.1    Khan, M.2    Huang, M.B.3    Bond, V.C.4    Powell, M.D.5
  • 91
    • 69049119032 scopus 로고    scopus 로고
    • HIV-1 evades virus-specific IgG2 and IgA responses by targeting systemic and intestinal B cells via long-range intercellular conduits
    • Xu W., Santini P.A., Sullivan J.S., He B., Shan M., Ball S.C., et al. HIV-1 evades virus-specific IgG2 and IgA responses by targeting systemic and intestinal B cells via long-range intercellular conduits. Nat Immunol 2009, 10:1008-1017.
    • (2009) Nat Immunol , vol.10 , pp. 1008-1017
    • Xu, W.1    Santini, P.A.2    Sullivan, J.S.3    He, B.4    Shan, M.5    Ball, S.C.6
  • 92
    • 69949128211 scopus 로고    scopus 로고
    • Massive secretion by T cells is caused by HIV Nef in infected cells and by Nef transfer to bystander cells
    • Muratori C., Cavallin L.E., Krätzel K., Tinari A., De Milito A., Fais S., et al. Massive secretion by T cells is caused by HIV Nef in infected cells and by Nef transfer to bystander cells. Cell Host Microbe 2009, 6:218-230.
    • (2009) Cell Host Microbe , vol.6 , pp. 218-230
    • Muratori, C.1    Cavallin, L.E.2    Krätzel, K.3    Tinari, A.4    De Milito, A.5    Fais, S.6
  • 93
    • 80052161955 scopus 로고    scopus 로고
    • HIV-Nef and AIDS pathogenesis: are we barking up the wrong tree?
    • Baur A.S. HIV-Nef and AIDS pathogenesis: are we barking up the wrong tree?. Trends Microbiol 2011, 19(9):435-440.
    • (2011) Trends Microbiol , vol.19 , Issue.9 , pp. 435-440
    • Baur, A.S.1
  • 94
    • 0242333900 scopus 로고    scopus 로고
    • Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells
    • Fomina A.F., Deerinck T.J., Ellisman M.H., Cahalan M.D. Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells. Exp Cell Res 2003, 291:150-166.
    • (2003) Exp Cell Res , vol.291 , pp. 150-166
    • Fomina, A.F.1    Deerinck, T.J.2    Ellisman, M.H.3    Cahalan, M.D.4
  • 95
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev D., Datta S., Ackema K., Zerial M., Spang A. Identification of the switch in early-to-late endosome transition. Cell 2010, 141:497-508.
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3    Zerial, M.4    Spang, A.5
  • 96
    • 36048947746 scopus 로고    scopus 로고
    • Regulated secretion from CD4+ T cells
    • Jolly C., Sattentau Q.J. Regulated secretion from CD4+ T cells. Trends Immunol 2007, 28:474-481.
    • (2007) Trends Immunol , vol.28 , pp. 474-481
    • Jolly, C.1    Sattentau, Q.J.2
  • 97
    • 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., Cheng Y., et al. HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4+ T cells. Traffic 2010, 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    Cheng, Y.6
  • 98
    • 79951687153 scopus 로고    scopus 로고
    • HIV type 1 Nef is released from infected cells in CD45(+) microvesicles and is present in the plasma of HIV-infected individuals
    • Raymond A.D., Campbell-Sims T.C., Khan M., Lang M., Huang M.B., Bond V.C., et al. HIV type 1 Nef is released from infected cells in CD45(+) microvesicles and is present in the plasma of HIV-infected individuals. AIDS Res Hum Retroviruses 2011, 27:167-178.
    • (2011) AIDS Res Hum Retroviruses , vol.27 , pp. 167-178
    • Raymond, A.D.1    Campbell-Sims, T.C.2    Khan, M.3    Lang, M.4    Huang, M.B.5    Bond, V.C.6
  • 99
    • 84887291770 scopus 로고    scopus 로고
    • The microvesicle component of HIV-1 inocula modulates dendritic cell infection and maturation and enhances adhesion to and activation of T lymphocytes
    • Mercier S.K., Donaghy H., Botting R.A., Turville S.G., Harman A.N., Nasr N., et al. The microvesicle component of HIV-1 inocula modulates dendritic cell infection and maturation and enhances adhesion to and activation of T lymphocytes. PLoS Pathog 2013, 9:e1003700.
    • (2013) PLoS Pathog , vol.9 , pp. e1003700
    • Mercier, S.K.1    Donaghy, H.2    Botting, R.A.3    Turville, S.G.4    Harman, A.N.5    Nasr, N.6
  • 100
    • 84862197035 scopus 로고    scopus 로고
    • Proteomic analysis of HIV-1 Nef cellular binding partners reveals a role for exocyst complex proteins in mediating enhancement of intercellular nanotube formation
    • Mukerji J., Olivieri K.C., Misra V., Agopian K.A., Gabuzda D. Proteomic analysis of HIV-1 Nef cellular binding partners reveals a role for exocyst complex proteins in mediating enhancement of intercellular nanotube formation. Retrovirology 2012, 9:33.
    • (2012) Retrovirology , vol.9 , pp. 33
    • Mukerji, J.1    Olivieri, K.C.2    Misra, V.3    Agopian, K.A.4    Gabuzda, D.5
  • 101
    • 84897417062 scopus 로고    scopus 로고
    • Transfer of intracellular HIV Nef to endothelium causes endothelial dysfunction
    • Wang T., Green L.A., Gupta S.K., Kim C., Wang L., Almodovar S., et al. Transfer of intracellular HIV Nef to endothelium causes endothelial dysfunction. PLoS One 2014, 9:e91063.
    • (2014) PLoS One , vol.9 , pp. e91063
    • Wang, T.1    Green, L.A.2    Gupta, S.K.3    Kim, C.4    Wang, L.5    Almodovar, S.6
  • 102
    • 84923222270 scopus 로고    scopus 로고
    • Intracellular Nef detected in peripheral blood mononuclear cells from HIV patients
    • [ahead of print]
    • Wang T., Green L.A., Gupta S.K., Amet T., Byrd D.J., Yu Q., et al. Intracellular Nef detected in peripheral blood mononuclear cells from HIV patients. AIDS Res Hum Retroviruses 2014, [ahead of print].
    • (2014) AIDS Res Hum Retroviruses
    • Wang, T.1    Green, L.A.2    Gupta, S.K.3    Amet, T.4    Byrd, D.J.5    Yu, Q.6
  • 103
    • 64049116643 scopus 로고    scopus 로고
    • Induction of a striking systemic cytokine cascade prior to peak viremia in acute human immunodeficiency virus type 1 infection, in contrast to more modest and delayed responses in acute hepatitis B and C virus infections
    • Stacey A.R., Norris P.J., Qin L., Haygreen E.A., Taylor E., Heitman J., et al. Induction of a striking systemic cytokine cascade prior to peak viremia in acute human immunodeficiency virus type 1 infection, in contrast to more modest and delayed responses in acute hepatitis B and C virus infections. J Virol 2009, 83:3719-3733.
    • (2009) J Virol , vol.83 , pp. 3719-3733
    • Stacey, A.R.1    Norris, P.J.2    Qin, L.3    Haygreen, E.A.4    Taylor, E.5    Heitman, J.6
  • 104
    • 38949102301 scopus 로고    scopus 로고
    • Chronic innate immune activation as a cause of HIV-1 immunopathogenesis
    • Boasso A., Shearer G.M. Chronic innate immune activation as a cause of HIV-1 immunopathogenesis. Clin Immunol 2008, 126:235-242.
    • (2008) Clin Immunol , vol.126 , pp. 235-242
    • Boasso, A.1    Shearer, G.M.2
  • 105
    • 0032845027 scopus 로고    scopus 로고
    • HIV-1 Nef mediates lymphocyte chemotaxis and activation by infected macrophages
    • Swingler S., Mann A., Jacque J., Brichacek B., Sasseville V.G., Williams K., et al. HIV-1 Nef mediates lymphocyte chemotaxis and activation by infected macrophages. Nat Med 1999, 5:997-1003.
    • (1999) Nat Med , vol.5 , pp. 997-1003
    • Swingler, S.1    Mann, A.2    Jacque, J.3    Brichacek, B.4    Sasseville, V.G.5    Williams, K.6
  • 106
    • 0038342442 scopus 로고    scopus 로고
    • HIV-1 Nef intersects the macrophage CD40L signalling pathway to promote resting-cell infection
    • Swingler S., Brichacek B., Jacque J.M., Ulich C., Zhou J., Stevenson M. HIV-1 Nef intersects the macrophage CD40L signalling pathway to promote resting-cell infection. Nature 2003, 424:213-219.
    • (2003) Nature , vol.424 , pp. 213-219
    • Swingler, S.1    Brichacek, B.2    Jacque, J.M.3    Ulich, C.4    Zhou, J.5    Stevenson, M.6
  • 107
    • 0032563306 scopus 로고    scopus 로고
    • PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization
    • Wan L., Molloy S.S., Thomas L., Liu G., Xiang Y., Rybak S.L., et al. PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. Cell 1998, 94:205-216.
    • (1998) Cell , vol.94 , pp. 205-216
    • Wan, L.1    Molloy, S.S.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Rybak, S.L.6
  • 108
    • 84861708657 scopus 로고    scopus 로고
    • An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I
    • Dikeakos J.D., Thomas L., Kwon G., Elferich J., Shinde U., Thomas G. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I. Mol Biol Cell 2012, 23:2184-2197.
    • (2012) Mol Biol Cell , vol.23 , pp. 2184-2197
    • Dikeakos, J.D.1    Thomas, L.2    Kwon, G.3    Elferich, J.4    Shinde, U.5    Thomas, G.6
  • 109
    • 52649095981 scopus 로고    scopus 로고
    • Functional characterization of the human immunodeficiency virus type 1 Nef acidic domain
    • Baugh L.L., Garcia J.V., Foster J.L. Functional characterization of the human immunodeficiency virus type 1 Nef acidic domain. J Virol 2008, 82:9657-9667.
    • (2008) J Virol , vol.82 , pp. 9657-9667
    • Baugh, L.L.1    Garcia, J.V.2    Foster, J.L.3
  • 110
    • 34548510349 scopus 로고    scopus 로고
    • HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2
    • Lubben N.B., Sahlender D.A., Motley A.M., Lehner P.J., Benaroch P., Robinson M.S. HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2. Mol Biol Cell 2007, 18:3351-3365.
    • (2007) Mol Biol Cell , vol.18 , pp. 3351-3365
    • Lubben, N.B.1    Sahlender, D.A.2    Motley, A.M.3    Lehner, P.J.4    Benaroch, P.5    Robinson, M.S.6
  • 111
    • 0038632363 scopus 로고    scopus 로고
    • Effects of HIV-1 Nef on retrograde transport from the plasma membrane to the endoplasmic reticulum
    • Johannes L., Pezo V., Mallard F., Tenza D., Wiltz A., Saint-Pol A., et al. Effects of HIV-1 Nef on retrograde transport from the plasma membrane to the endoplasmic reticulum. Traffic 2003, 4:323-332.
    • (2003) Traffic , vol.4 , pp. 323-332
    • Johannes, L.1    Pezo, V.2    Mallard, F.3    Tenza, D.4    Wiltz, A.5    Saint-Pol, A.6
  • 112
    • 84888308190 scopus 로고    scopus 로고
    • HIV-1 Nef interacts with HCV core, recruits TRAF2, TRAF5 and TRAF6, and stimulates HIV-1 replication in macrophages
    • Khan K.A., Abbas W., Varin A., Kumar A., Di Martino V., Dichamp I., et al. HIV-1 Nef interacts with HCV core, recruits TRAF2, TRAF5 and TRAF6, and stimulates HIV-1 replication in macrophages. J Innate Immun 2013, 5:639-656.
    • (2013) J Innate Immun , vol.5 , pp. 639-656
    • Khan, K.A.1    Abbas, W.2    Varin, A.3    Kumar, A.4    Di Martino, V.5    Dichamp, I.6
  • 113
    • 0030925641 scopus 로고    scopus 로고
    • Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3
    • Sandberg M., Hammerschmidt W., Sugden B. Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3. J Virol 1997, 71:4649-4656.
    • (1997) J Virol , vol.71 , pp. 4649-4656
    • Sandberg, M.1    Hammerschmidt, W.2    Sugden, B.3
  • 114
    • 0041387452 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase and NF-kappaB pathways by a Kaposi's sarcoma-associated herpesvirus K15 membrane protein
    • Brinkmann M., Glenn M., Rainbow L., Kieser A., Henke-Gendo C., Schulz T. Activation of mitogen-activated protein kinase and NF-kappaB pathways by a Kaposi's sarcoma-associated herpesvirus K15 membrane protein. J Virol 2003, 77:9346-9358.
    • (2003) J Virol , vol.77 , pp. 9346-9358
    • Brinkmann, M.1    Glenn, M.2    Rainbow, L.3    Kieser, A.4    Henke-Gendo, C.5    Schulz, T.6
  • 115
    • 33947418102 scopus 로고    scopus 로고
    • Herpesvirus saimiri STP-A oncoprotein utilizes Src family protein tyrosine kinase and tumor necrosis factor receptor-associated factors to elicit cellular signal transduction
    • Garcia M., Kaserman J., Chung Y., Jung J., Lee S. Herpesvirus saimiri STP-A oncoprotein utilizes Src family protein tyrosine kinase and tumor necrosis factor receptor-associated factors to elicit cellular signal transduction. J Virol 2007, 81:2663-2674.
    • (2007) J Virol , vol.81 , pp. 2663-2674
    • Garcia, M.1    Kaserman, J.2    Chung, Y.3    Jung, J.4    Lee, S.5
  • 116
    • 0042733392 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein modulates c-Jun N-terminal kinase through interaction with tumor necrosis factor receptor-associated factor 2
    • Park K., Choi S., Choi D., Park J., Yie S., Lee S., et al. Hepatitis C virus NS5A protein modulates c-Jun N-terminal kinase through interaction with tumor necrosis factor receptor-associated factor 2. J Biol Chem 2003, 278:30711-30718.
    • (2003) J Biol Chem , vol.278 , pp. 30711-30718
    • Park, K.1    Choi, S.2    Choi, D.3    Park, J.4    Yie, S.5    Lee, S.6
  • 117
    • 84874238349 scopus 로고    scopus 로고
    • HIV Nef, paxillin, and Pak1/2 regulate activation and secretion of TACE/ADAM10 proteases
    • Lee J.H., Wittki S., Bräu T., Dreyer F.S., Krätzel K., Dindorf J., et al. HIV Nef, paxillin, and Pak1/2 regulate activation and secretion of TACE/ADAM10 proteases. Mol Cell 2013, 49:668-679.
    • (2013) Mol Cell , vol.49 , pp. 668-679
    • Lee, J.H.1    Wittki, S.2    Bräu, T.3    Dreyer, F.S.4    Krätzel, K.5    Dindorf, J.6
  • 118
  • 119
    • 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 Y.H., Mandic R., Peterlin B.M. Interaction between Nef and phosphatidylinositol-3-kinase leads to activation of p21-activated kinase and increased production of HIV. Virology 2002, 294:246-255.
    • (2002) Virology , vol.294 , pp. 246-255
    • Linnemann, T.1    Zheng, Y.H.2    Mandic, R.3    Peterlin, B.M.4
  • 120
    • 40149097137 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef recruits the guanine exchange factor Vav1 via an unexpected interface into plasma membrane microdomains for association with p21-activated kinase 2 activity
    • Rauch S., Pulkkinen K., Saksela K., Fackler O.T. Human immunodeficiency virus type 1 Nef recruits the guanine exchange factor Vav1 via an unexpected interface into plasma membrane microdomains for association with p21-activated kinase 2 activity. J Virol 2008, 82:2918-2929.
    • (2008) J Virol , vol.82 , pp. 2918-2929
    • Rauch, S.1    Pulkkinen, K.2    Saksela, K.3    Fackler, O.T.4
  • 121
    • 84862962823 scopus 로고    scopus 로고
    • Historical perspectives on tumor necrosis factor and its superfamily: 25 years later, a golden journey
    • Aggarwal B.B., Gupta S.C., Kim J.H. Historical perspectives on tumor necrosis factor and its superfamily: 25 years later, a golden journey. Blood 2012, 119:651-665.
    • (2012) Blood , vol.119 , pp. 651-665
    • Aggarwal, B.B.1    Gupta, S.C.2    Kim, J.H.3
  • 122
    • 84902215040 scopus 로고    scopus 로고
    • Soluble, but not transmembrane, TNF-α is required during influenza infection to limit the magnitude of immune responses and the extent of immunopathology
    • DeBerge M.P., Ely K.H., Enelow R.I. Soluble, but not transmembrane, TNF-α is required during influenza infection to limit the magnitude of immune responses and the extent of immunopathology. J Immunol 2014, 192:5839-5851.
    • (2014) J Immunol , vol.192 , pp. 5839-5851
    • DeBerge, M.P.1    Ely, K.H.2    Enelow, R.I.3
  • 123
    • 84893381289 scopus 로고    scopus 로고
    • Transmembrane TNF-α promotes suppressive activities of myeloid-derived suppressor cells via TNFR2
    • Hu X., Li B., Li X., Zhao X., Wan L., Lin G., et al. Transmembrane TNF-α promotes suppressive activities of myeloid-derived suppressor cells via TNFR2. J Immunol 2014, 192:1320-1331.
    • (2014) J Immunol , vol.192 , pp. 1320-1331
    • Hu, X.1    Li, B.2    Li, X.3    Zhao, X.4    Wan, L.5    Lin, G.6
  • 124
    • 84893829335 scopus 로고    scopus 로고
    • TNF and TNF receptor superfamily members in HIV infection: new cellular targets for therapy?
    • Kumar A., Abbas W., Herbein G. TNF and TNF receptor superfamily members in HIV infection: new cellular targets for therapy?. Mediators Inflamm 2013, 2013:484378.
    • (2013) Mediators Inflamm , vol.2013 , pp. 484378
    • Kumar, A.1    Abbas, W.2    Herbein, G.3
  • 125
    • 84906968837 scopus 로고    scopus 로고
    • Exosomes from human immunodeficiency virus type 1 (HIV-1)-infected cells license quiescent CD4+ T lymphocytes to replicate HIV-1 through a Nef- and ADAM17-dependent mechanism
    • Arenaccio C., Chiozzini C., Columba-Cabezas S., Manfredi F., Affabris E., Baur A., et al. Exosomes from human immunodeficiency virus type 1 (HIV-1)-infected cells license quiescent CD4+ T lymphocytes to replicate HIV-1 through a Nef- and ADAM17-dependent mechanism. J Virol 2014, 88:11529-11539.
    • (2014) J Virol , vol.88 , pp. 11529-11539
    • Arenaccio, C.1    Chiozzini, C.2    Columba-Cabezas, S.3    Manfredi, F.4    Affabris, E.5    Baur, A.6
  • 126
    • 0033776709 scopus 로고    scopus 로고
    • HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes
    • Piguet V., Wan L., Borel C., Mangasarian A., Demaurex N., Thomas G., et al. HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes. Nat Cell Biol 2000, 2:163-167.
    • (2000) Nat Cell Biol , vol.2 , pp. 163-167
    • Piguet, V.1    Wan, L.2    Borel, C.3    Mangasarian, A.4    Demaurex, N.5    Thomas, G.6
  • 127
    • 77949558495 scopus 로고    scopus 로고
    • ADAM-17: the enzyme that does it all
    • Gooz M. ADAM-17: the enzyme that does it all. Crit Rev Biochem Mol Biol 2010, 45:146-169.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 146-169
    • Gooz, M.1
  • 128
    • 0031048979 scopus 로고    scopus 로고
    • Accumulation of defective viral genomes in peripheral blood mononuclear cells of human immunodeficiency virus type 1-infected individuals
    • Sanchez G., Xu X., Chermann J.C., Hirsch I. Accumulation of defective viral genomes in peripheral blood mononuclear cells of human immunodeficiency virus type 1-infected individuals. J Virol 1997, 71:2233-2240.
    • (1997) J Virol , vol.71 , pp. 2233-2240
    • Sanchez, G.1    Xu, X.2    Chermann, J.C.3    Hirsch, I.4
  • 129
    • 0034878971 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 DNA sequences genetically damaged by hypermutation are often abundant in patient peripheral blood mononuclear cells and may be generated during near-simultaneous infection and activation of CD4(+) T cells
    • Janini M., Rogers M., Birx D.R., McCutchan F.E. Human immunodeficiency virus type 1 DNA sequences genetically damaged by hypermutation are often abundant in patient peripheral blood mononuclear cells and may be generated during near-simultaneous infection and activation of CD4(+) T cells. J Virol 2001, 75:7973-7986.
    • (2001) J Virol , vol.75 , pp. 7973-7986
    • Janini, M.1    Rogers, M.2    Birx, D.R.3    McCutchan, F.E.4
  • 130
    • 84895067799 scopus 로고    scopus 로고
    • Differential impact of APOBEC3-driven mutagenesis on HIV evolution in diverse anatomical compartments
    • Fourati S., Lambert-Niclot S., Soulie C., Wirden M., Malet I., Valantin M.A., et al. Differential impact of APOBEC3-driven mutagenesis on HIV evolution in diverse anatomical compartments. AIDS 2014, 28:487-491.
    • (2014) AIDS , vol.28 , pp. 487-491
    • Fourati, S.1    Lambert-Niclot, S.2    Soulie, C.3    Wirden, M.4    Malet, I.5    Valantin, M.A.6
  • 131
    • 84904615306 scopus 로고    scopus 로고
    • Cell activation and HIV-1 replication in unstimulated CD4+ T lymphocytes ingesting exosomes from cells expressing defective HIV-1
    • Arenaccio C., Chiozzini C., Columba-Cabezas S., Manfredi F., Federico M. Cell activation and HIV-1 replication in unstimulated CD4+ T lymphocytes ingesting exosomes from cells expressing defective HIV-1. Retrovirology 2014, 11:46.
    • (2014) Retrovirology , vol.11 , pp. 46
    • Arenaccio, C.1    Chiozzini, C.2    Columba-Cabezas, S.3    Manfredi, F.4    Federico, M.5
  • 132
    • 0024402875 scopus 로고
    • Biologic and molecular characterization of producer and nonproducer clones from HUT-78 cells infected with a patient HIV isolate
    • Federico M., Titti F., Buttó S., Orecchia A., Carlini F., Taddeo B., et al. Biologic and molecular characterization of producer and nonproducer clones from HUT-78 cells infected with a patient HIV isolate. AIDS Res Hum Retroviruses 1989, 5:385-396.
    • (1989) AIDS Res Hum Retroviruses , vol.5 , pp. 385-396
    • Federico, M.1    Titti, F.2    Buttó, S.3    Orecchia, A.4    Carlini, F.5    Taddeo, B.6
  • 133
    • 0031958099 scopus 로고    scopus 로고
    • Gag, vif, and nef genes contribute to the homologous viral interference induced by a nonproducer human immunodeficiency virus type 1 (HIV-1) variant: identification of novel HIV-1-inhibiting viral protein mutants
    • D'Aloja P., Olivetta E., Bona R., Nappi F., Pedacchia D., Pugliese K., et al. gag, vif, and nef genes contribute to the homologous viral interference induced by a nonproducer human immunodeficiency virus type 1 (HIV-1) variant: identification of novel HIV-1-inhibiting viral protein mutants. J Virol 1998, 72:4308-4319.
    • (1998) J Virol , vol.72 , pp. 4308-4319
    • D'Aloja, P.1    Olivetta, E.2    Bona, R.3    Nappi, F.4    Pedacchia, D.5    Pugliese, K.6
  • 134
    • 0034782579 scopus 로고    scopus 로고
    • Genetic and functional analysis of the human immunodeficiency virus (HIV) type 1-inhibiting F12-HIVnef allele
    • D'Aloja P., Santarcangelo A.C., Arold S., Baur A., Federico M. Genetic and functional analysis of the human immunodeficiency virus (HIV) type 1-inhibiting F12-HIVnef allele. J Gen Virol 2001, 82:2735-2745.
    • (2001) J Gen Virol , vol.82 , pp. 2735-2745
    • D'Aloja, P.1    Santarcangelo, A.C.2    Arold, S.3    Baur, A.4    Federico, M.5
  • 135
    • 39049155167 scopus 로고    scopus 로고
    • Is HIV infection a TNF receptor signalling-driven disease
    • Herbein G., Khan K.A. Is HIV infection a TNF receptor signalling-driven disease. Trends Immunol 2008, 29:61-67.
    • (2008) Trends Immunol , vol.29 , pp. 61-67
    • Herbein, G.1    Khan, K.A.2
  • 136
    • 33750601327 scopus 로고    scopus 로고
    • Replicating Ad-recombinants encoding non-myristoylated rather than wild-type HIV Nef elicit enhanced cellular immunity
    • Peng B., Voltan R., Cristillo A.D., Alvord W.G., Davis-Warren A., Zhou Q., et al. Replicating Ad-recombinants encoding non-myristoylated rather than wild-type HIV Nef elicit enhanced cellular immunity. AIDS 2006, 20:2149-2157.
    • (2006) AIDS , vol.20 , pp. 2149-2157
    • Peng, B.1    Voltan, R.2    Cristillo, A.D.3    Alvord, W.G.4    Davis-Warren, A.5    Zhou, Q.6
  • 137
    • 34548129591 scopus 로고    scopus 로고
    • Viral defense, carcinogenesis and ISG15: novel roles for an old ISG
    • Pitha-Rowe I.F., Pitha P.M. Viral defense, carcinogenesis and ISG15: novel roles for an old ISG. Cytokine Growth Factor Rev 2007, 18:409-417.
    • (2007) Cytokine Growth Factor Rev , vol.18 , pp. 409-417
    • Pitha-Rowe, I.F.1    Pitha, P.M.2
  • 138
    • 70349748582 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 mediates global disruption of innate antiviral signaling and immune defenses within infected cells
    • Doehle B.P., Hladik F., McNevin J.P., McElrath M.J., Gale M. Human immunodeficiency virus type 1 mediates global disruption of innate antiviral signaling and immune defenses within infected cells. J Virol 2009, 83:10395-10405.
    • (2009) J Virol , vol.83 , pp. 10395-10405
    • Doehle, B.P.1    Hladik, F.2    McNevin, J.P.3    McElrath, M.J.4    Gale, M.5
  • 139
    • 84865106370 scopus 로고    scopus 로고
    • Vpu mediates depletion of interferon regulatory factor 3 during HIV infection by a lysosome-dependent mechanism
    • Doehle B.P., Chang K., Rustagi A., McNevin J., McElrath M.J., Gale M. Vpu mediates depletion of interferon regulatory factor 3 during HIV infection by a lysosome-dependent mechanism. J Virol 2012, 86:8367-8374.
    • (2012) J Virol , vol.86 , pp. 8367-8374
    • Doehle, B.P.1    Chang, K.2    Rustagi, A.3    McNevin, J.4    McElrath, M.J.5    Gale, M.6
  • 140
    • 84878553328 scopus 로고    scopus 로고
    • HIV-1 Vpu does not degrade interferon regulatory factor 3
    • Hotter D., Kirchhoff F., Sauter D. HIV-1 Vpu does not degrade interferon regulatory factor 3. J Virol 2013, 87:7160-7165.
    • (2013) J Virol , vol.87 , pp. 7160-7165
    • Hotter, D.1    Kirchhoff, F.2    Sauter, D.3
  • 141
    • 84865069404 scopus 로고    scopus 로고
    • Vpu-deficient HIV strains stimulate innate immune signaling responses in target cells
    • Doehle B.P., Chang K., Fleming L., McNevin J., Hladik F., McElrath M.J., et al. Vpu-deficient HIV strains stimulate innate immune signaling responses in target cells. J Virol 2012, 86:8499-8506.
    • (2012) J Virol , vol.86 , pp. 8499-8506
    • Doehle, B.P.1    Chang, K.2    Fleming, L.3    McNevin, J.4    Hladik, F.5    McElrath, M.J.6
  • 142
    • 41149122048 scopus 로고    scopus 로고
    • IRF-1 is required for full NF-kappaB transcriptional activity at the human immunodeficiency virus type 1 long terminal repeat enhancer
    • Sgarbanti M., Remoli A.L., Marsili G., Ridolfi B., Borsetti A., Perrotti E., et al. IRF-1 is required for full NF-kappaB transcriptional activity at the human immunodeficiency virus type 1 long terminal repeat enhancer. J Virol 2008, 82:3632-3641.
    • (2008) J Virol , vol.82 , pp. 3632-3641
    • Sgarbanti, M.1    Remoli, A.L.2    Marsili, G.3    Ridolfi, B.4    Borsetti, A.5    Perrotti, E.6
  • 144
    • 79955377543 scopus 로고    scopus 로고
    • TRIM5 is an innate immune sensor for the retrovirus capsid lattice
    • Pertel T., Hausmann S., Morger D., Züger S., Guerra J., Lascano J., et al. TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature 2011, 472:361-365.
    • (2011) Nature , vol.472 , pp. 361-365
    • Pertel, T.1    Hausmann, S.2    Morger, D.3    Züger, S.4    Guerra, J.5    Lascano, J.6
  • 145
    • 84869194198 scopus 로고    scopus 로고
    • Innate sensing of HIV-1 assembly by Tetherin induces NFκB-dependent proinflammatory responses
    • Galão R.P., Le Tortorec A., Pickering S., Kueck T., Neil S.J. Innate sensing of HIV-1 assembly by Tetherin induces NFκB-dependent proinflammatory responses. Cell Host Microbe 2012, 12:633-644.
    • (2012) Cell Host Microbe , vol.12 , pp. 633-644
    • Galão, R.P.1    Le Tortorec, A.2    Pickering, S.3    Kueck, T.4    Neil, S.J.5
  • 146
    • 84887989681 scopus 로고    scopus 로고
    • Emerging role of the host restriction factor tetherin in viral immune sensing
    • Hotter D., Sauter D., Kirchhoff F. Emerging role of the host restriction factor tetherin in viral immune sensing. J Mol Biol 2013, 425:4956-4964.
    • (2013) J Mol Biol , vol.425 , pp. 4956-4964
    • Hotter, D.1    Sauter, D.2    Kirchhoff, F.3
  • 147
    • 0028035271 scopus 로고
    • Interferon induction by HIV glycoprotein 120: role of the V3 loop
    • Ankel H., Capobianchi M.R., Castilletti C., Dianzani F. Interferon induction by HIV glycoprotein 120: role of the V3 loop. Virology 1994, 205:34-43.
    • (1994) Virology , vol.205 , pp. 34-43
    • Ankel, H.1    Capobianchi, M.R.2    Castilletti, C.3    Dianzani, F.4
  • 150
    • 0028123780 scopus 로고
    • Induction of beta interferon by human immunodeficiency virus type 1 and its gp120 protein in human monocytes-macrophages: role of beta interferon in restriction of virus replication
    • Gessani S., Puddu P., Varano B., Borghi P., Conti L., Fantuzzi L., et al. Induction of beta interferon by human immunodeficiency virus type 1 and its gp120 protein in human monocytes-macrophages: role of beta interferon in restriction of virus replication. J Virol 1994, 68:1983-1986.
    • (1994) J Virol , vol.68 , pp. 1983-1986
    • Gessani, S.1    Puddu, P.2    Varano, B.3    Borghi, P.4    Conti, L.5    Fantuzzi, L.6
  • 151
    • 0026044408 scopus 로고
    • Induction of alpha interferon by human immunodeficiency virus type 1 in human monocyte-macrophage cultures
    • Szebeni J., Dieffenbach C., Wahl S.M., Venkateshan C.N., Yeh A., Popovic M., et al. Induction of alpha interferon by human immunodeficiency virus type 1 in human monocyte-macrophage cultures. J Virol 1991, 65:6362-6364.
    • (1991) J Virol , vol.65 , pp. 6362-6364
    • Szebeni, J.1    Dieffenbach, C.2    Wahl, S.M.3    Venkateshan, C.N.4    Yeh, A.5    Popovic, M.6
  • 152
    • 0025823898 scopus 로고
    • Interferon-alpha and tumor necrosis factor-alpha in serum of patients in various stages of HIV-1 infection
    • von Sydow M., Sönnerborg A., Gaines H., Strannegård O. Interferon-alpha and tumor necrosis factor-alpha in serum of patients in various stages of HIV-1 infection. AIDS Res Hum Retroviruses 1991, 7:375-380.
    • (1991) AIDS Res Hum Retroviruses , vol.7 , pp. 375-380
    • von Sydow, M.1    Sönnerborg, A.2    Gaines, H.3    Strannegård, O.4
  • 153
    • 33646468496 scopus 로고    scopus 로고
    • Differential expression of IFN-alpha and TRAIL/DR5 in lymphoid tissue of progressor versus nonprogressor HIV-1-infected patients
    • Herbeuval J.P., Nilsson J., Boasso A., Hardy A.W., Kruhlak M.J., Anderson S.A., et al. Differential expression of IFN-alpha and TRAIL/DR5 in lymphoid tissue of progressor versus nonprogressor HIV-1-infected patients. Proc Natl Acad Sci USA 2006, 103:7000-7005.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7000-7005
    • Herbeuval, J.P.1    Nilsson, J.2    Boasso, A.3    Hardy, A.W.4    Kruhlak, M.J.5    Anderson, S.A.6
  • 154
    • 72849132344 scopus 로고    scopus 로고
    • Global genomic analysis reveals rapid control of a robust innate response in SIV-infected sooty mangabeys
    • Bosinger S.E., Li Q., Gordon S.N., Klatt N.R., Duan L., Xu L., et al. Global genomic analysis reveals rapid control of a robust innate response in SIV-infected sooty mangabeys. J Clin Invest 2009, 119:3556-3572.
    • (2009) J Clin Invest , vol.119 , pp. 3556-3572
    • Bosinger, S.E.1    Li, Q.2    Gordon, S.N.3    Klatt, N.R.4    Duan, L.5    Xu, L.6
  • 155
    • 72849136282 scopus 로고    scopus 로고
    • Nonpathogenic SIV infection of African green monkeys induces a strong but rapidly controlled type I IFN response
    • Jacquelin B., Mayau V., Targat B., Liovat A.S., Kunkel D., Petitjean G., et al. Nonpathogenic SIV infection of African green monkeys induces a strong but rapidly controlled type I IFN response. J Clin Invest 2009, 119:3544-3555.
    • (2009) J Clin Invest , vol.119 , pp. 3544-3555
    • Jacquelin, B.1    Mayau, V.2    Targat, B.3    Liovat, A.S.4    Kunkel, D.5    Petitjean, G.6
  • 156
    • 80051801187 scopus 로고    scopus 로고
    • HIV-1 infection and induction of interferon alpha in plasmacytoid dendritic cells
    • Benlahrech A., Patterson S. HIV-1 infection and induction of interferon alpha in plasmacytoid dendritic cells. Curr Opin HIV AIDS 2011, 6:373-378.
    • (2011) Curr Opin HIV AIDS , vol.6 , pp. 373-378
    • Benlahrech, A.1    Patterson, S.2
  • 157
    • 27644513772 scopus 로고    scopus 로고
    • Endocytosis of HIV-1 activates plasmacytoid dendritic cells via Toll-like receptor-viral RNA interactions
    • Beignon A.S., McKenna K., Skoberne M., Manches O., DaSilva I., Kavanagh D.G., et al. Endocytosis of HIV-1 activates plasmacytoid dendritic cells via Toll-like receptor-viral RNA interactions. J Clin Invest 2005, 115:3265-3275.
    • (2005) J Clin Invest , vol.115 , pp. 3265-3275
    • Beignon, A.S.1    McKenna, K.2    Skoberne, M.3    Manches, O.4    DaSilva, I.5    Kavanagh, D.G.6
  • 158
    • 79952234401 scopus 로고    scopus 로고
    • Spatiotemporal trafficking of HIV in human plasmacytoid dendritic cells defines a persistently IFN-α-producing and partially matured phenotype
    • O'Brien M., Manches O., Sabado R.L., Baranda S.J., Wang Y., Marie I., et al. Spatiotemporal trafficking of HIV in human plasmacytoid dendritic cells defines a persistently IFN-α-producing and partially matured phenotype. J Clin Invest 2011, 121:1088-1101.
    • (2011) J Clin Invest , vol.121 , pp. 1088-1101
    • O'Brien, M.1    Manches, O.2    Sabado, R.L.3    Baranda, S.J.4    Wang, Y.5    Marie, I.6
  • 159
    • 84879654670 scopus 로고    scopus 로고
    • Human plasmacytoid dendritic cells efficiently capture HIV-1 envelope glycoproteins via CD4 for antigen presentation
    • Sandgren K.J., Smed-Sörensen A., Forsell M.N., Soldemo M., Adams W.C., Liang F., et al. Human plasmacytoid dendritic cells efficiently capture HIV-1 envelope glycoproteins via CD4 for antigen presentation. J Immunol 2013, 191:60-69.
    • (2013) J Immunol , vol.191 , pp. 60-69
    • Sandgren, K.J.1    Smed-Sörensen, A.2    Forsell, M.N.3    Soldemo, M.4    Adams, W.C.5    Liang, F.6
  • 160
    • 77956689533 scopus 로고    scopus 로고
    • Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3
    • Sasai M., Linehan M.M., Iwasaki A. Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3. Science 2010, 329:1530-1534.
    • (2010) Science , vol.329 , pp. 1530-1534
    • Sasai, M.1    Linehan, M.M.2    Iwasaki, A.3
  • 161
    • 77957582392 scopus 로고    scopus 로고
    • Innate immune activation in primary HIV-1 infection
    • Chang J.J., Altfeld M. Innate immune activation in primary HIV-1 infection. J Infect Dis 2010, 202(Suppl 2):S297-S301.
    • (2010) J Infect Dis , vol.202 , pp. S297-S301
    • Chang, J.J.1    Altfeld, M.2
  • 162
    • 58149184316 scopus 로고    scopus 로고
    • Reversible blockade of thymic output: an inherent part of TLR ligand-mediated immune response
    • Démoulins T., Abdallah A., Kettaf N., Baron M.L., Gerarduzzi C., Gauchat D., et al. Reversible blockade of thymic output: an inherent part of TLR ligand-mediated immune response. J Immunol 2008, 181:6757-6769.
    • (2008) J Immunol , vol.181 , pp. 6757-6769
    • Démoulins, T.1    Abdallah, A.2    Kettaf, N.3    Baron, M.L.4    Gerarduzzi, C.5    Gauchat, D.6
  • 163
    • 0030036342 scopus 로고    scopus 로고
    • Induction of bystander T cell proliferation by viruses and type I interferon in vivo
    • Tough D.F., Borrow P., Sprent J. Induction of bystander T cell proliferation by viruses and type I interferon in vivo. Science 1996, 272:1947-1950.
    • (1996) Science , vol.272 , pp. 1947-1950
    • Tough, D.F.1    Borrow, P.2    Sprent, J.3
  • 164
    • 2542481852 scopus 로고    scopus 로고
    • Telomere erosion in memory T cells induced by telomerase inhibition at the site of antigenic challenge in vivo
    • Reed J.R., Vukmanovic-Stejic M., Fletcher J.M., Soares M.V., Cook J.E., Orteu C.H., et al. Telomere erosion in memory T cells induced by telomerase inhibition at the site of antigenic challenge in vivo. J Exp Med 2004, 199:1433-1443.
    • (2004) J Exp Med , vol.199 , pp. 1433-1443
    • Reed, J.R.1    Vukmanovic-Stejic, M.2    Fletcher, J.M.3    Soares, M.V.4    Cook, J.E.5    Orteu, C.H.6
  • 165
    • 38849134878 scopus 로고    scopus 로고
    • Chronic CD4+ T-cell activation and depletion in human immunodeficiency virus type 1 infection: type I interferon-mediated disruption of T-cell dynamics
    • Sedaghat A.R., German J., Teslovich T.M., Cofrancesco J., Jie C.C., Talbot C.C., et al. Chronic CD4+ T-cell activation and depletion in human immunodeficiency virus type 1 infection: type I interferon-mediated disruption of T-cell dynamics. J Virol 2008, 82:1870-1883.
    • (2008) J Virol , vol.82 , pp. 1870-1883
    • Sedaghat, A.R.1    German, J.2    Teslovich, T.M.3    Cofrancesco, J.4    Jie, C.C.5    Talbot, C.C.6
  • 166
    • 84876299371 scopus 로고    scopus 로고
    • Blockade of chronic type I interferon signaling to control persistent LCMV infection
    • Wilson E.B., Yamada D.H., Elsaesser H., Herskovitz J., Deng J., Cheng G., et al. Blockade of chronic type I interferon signaling to control persistent LCMV infection. Science 2013, 340:202-207.
    • (2013) Science , vol.340 , pp. 202-207
    • Wilson, E.B.1    Yamada, D.H.2    Elsaesser, H.3    Herskovitz, J.4    Deng, J.5    Cheng, G.6
  • 167
    • 84876311772 scopus 로고    scopus 로고
    • Persistent LCMV infection is controlled by blockade of type I interferon signaling
    • Teijaro J.R., Ng C., Lee A.M., Sullivan B.M., Sheehan K.C., Welch M., et al. Persistent LCMV infection is controlled by blockade of type I interferon signaling. Science 2013, 340:207-211.
    • (2013) Science , vol.340 , pp. 207-211
    • Teijaro, J.R.1    Ng, C.2    Lee, A.M.3    Sullivan, B.M.4    Sheehan, K.C.5    Welch, M.6
  • 168
    • 34247170486 scopus 로고    scopus 로고
    • HIV-1 immunopathogenesis: how good interferon turns bad
    • Herbeuval J.P., Shearer G.M. HIV-1 immunopathogenesis: how good interferon turns bad. Clin Immunol 2007, 123:121-128.
    • (2007) Clin Immunol , vol.123 , pp. 121-128
    • Herbeuval, J.P.1    Shearer, G.M.2
  • 169
    • 80755150060 scopus 로고    scopus 로고
    • Humanized mouse models of HIV infection
    • Denton P.W., García J.V. Humanized mouse models of HIV infection. AIDS Rev 2011, 13:135-148.
    • (2011) AIDS Rev , vol.13 , pp. 135-148
    • Denton, P.W.1    García, J.V.2
  • 170
    • 84904426496 scopus 로고    scopus 로고
    • Adding new dimensions: towards an integrative understanding of HIV-1 spread
    • Fackler O.T., Murooka T.T., Imle A., Mempel T.R. Adding new dimensions: towards an integrative understanding of HIV-1 spread. Nat Rev Microbiol 2014, 12:563-574.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 563-574
    • Fackler, O.T.1    Murooka, T.T.2    Imle, A.3    Mempel, T.R.4
  • 171
    • 57049103401 scopus 로고    scopus 로고
    • Glioblastoma microvesicles transport RNA and proteins that promote tumour growth and provide diagnostic biomarkers
    • Skog J., Würdinger T., van Rijn S., Meijer D.H., Gainche L., Sena-Esteves M., et al. Glioblastoma microvesicles transport RNA and proteins that promote tumour growth and provide diagnostic biomarkers. Nat Cell Biol 2008, 10:1470-1476.
    • (2008) Nat Cell Biol , vol.10 , pp. 1470-1476
    • Skog, J.1    Würdinger, T.2    van Rijn, S.3    Meijer, D.H.4    Gainche, L.5    Sena-Esteves, M.6
  • 172
    • 34250325547 scopus 로고    scopus 로고
    • Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes
    • Fang Y., Wu N., Gan X., Yan W., Morrell J.C., Gould S.J. Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes. PLoS Biol 2007, 5:e158.
    • (2007) PLoS Biol , vol.5 , pp. e158
    • Fang, Y.1    Wu, N.2    Gan, X.3    Yan, W.4    Morrell, J.C.5    Gould, S.J.6
  • 173
    • 84897449430 scopus 로고    scopus 로고
    • HIV-1 matrix protein p17 promotes lymphangiogenesis and activates the endothelin-1/endothelin B receptor axis
    • Caccuri F., Rueckert C., Giagulli C., Schulze K., Basta D., Zicari S., et al. HIV-1 matrix protein p17 promotes lymphangiogenesis and activates the endothelin-1/endothelin B receptor axis. Arterioscler Thromb Vasc Biol 2014, 34:846-856.
    • (2014) Arterioscler Thromb Vasc Biol , vol.34 , pp. 846-856
    • Caccuri, F.1    Rueckert, C.2    Giagulli, C.3    Schulze, K.4    Basta, D.5    Zicari, S.6
  • 174
    • 84899069315 scopus 로고    scopus 로고
    • Simian immunodeficiency virus and human immunodeficiency virus type 1 matrix proteins specify different capabilities to modulate B cell growth
    • Caccuri F., Giagulli C., Reichelt J., Martorelli D., Marsico S., Bugatti A., et al. Simian immunodeficiency virus and human immunodeficiency virus type 1 matrix proteins specify different capabilities to modulate B cell growth. J Virol 2014, 88:5706-5717.
    • (2014) J Virol , vol.88 , pp. 5706-5717
    • Caccuri, F.1    Giagulli, C.2    Reichelt, J.3    Martorelli, D.4    Marsico, S.5    Bugatti, A.6
  • 176
    • 84922391873 scopus 로고    scopus 로고
    • Detection of HIV-1 matrix protein p17 quasispecies variants in plasma of chronic HIV-1-infected patients by ultra-deep pyrosequencing
    • Giombini E., Dolcetti R., Caccuri F., Selleri M., Rozera G., Abbate I., et al. Detection of HIV-1 matrix protein p17 quasispecies variants in plasma of chronic HIV-1-infected patients by ultra-deep pyrosequencing. J Acquir Immune Defic Syndr 2014, 66:332-339.
    • (2014) J Acquir Immune Defic Syndr , vol.66 , pp. 332-339
    • Giombini, E.1    Dolcetti, R.2    Caccuri, F.3    Selleri, M.4    Rozera, G.5    Abbate, I.6
  • 177
    • 84886903090 scopus 로고    scopus 로고
    • Contributions of HIV-1 Nef to immune dysregulation in HIV-infected patients: a therapeutic target
    • Witkowski W., Verhasselt B. Contributions of HIV-1 Nef to immune dysregulation in HIV-infected patients: a therapeutic target. Expert Opin Ther Targets 2013, 17:1345-1356.
    • (2013) Expert Opin Ther Targets , vol.17 , pp. 1345-1356
    • Witkowski, W.1    Verhasselt, B.2
  • 179
    • 84899047095 scopus 로고    scopus 로고
    • Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody
    • Lülf S., Matz J., Rouyez M.C., Järviluoma A., Saksela K., Benichou S., et al. Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology 2014, 11:24.
    • (2014) Retrovirology , vol.11 , pp. 24
    • Lülf, S.1    Matz, J.2    Rouyez, M.C.3    Järviluoma, A.4    Saksela, K.5    Benichou, S.6


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