메뉴 건너뛰기




Volumn 394, Issue 2, 2009, Pages 329-342

HIV-1 Nef Dimerization Is Required for Nef-Mediated Receptor Downregulation and Viral Replication

Author keywords

bimolecular fluorescence complementation; CD4; dimerization; HIV Nef; HIV replication

Indexed keywords

ANTIRETROVIRUS AGENT; HOMODIMER; NEF PROTEIN; OLIGOMER; VIRUS RECEPTOR;

EID: 70350547756     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.09.047     Document Type: Article
Times cited : (63)

References (71)
  • 3
    • 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., and Jolicoeur P. Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice. Cell 95 (1998) 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
  • 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 270 (1995) 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
  • 6
    • 0030788298 scopus 로고    scopus 로고
    • A role for natural simian immunodeficiency virus and human immunodeficiency virus type 1 Nef alleles in lymphocyte activation
    • Alexander L., Du Z., Rosenzweig M., Jung J.U., and Desrosiers R.C. A role for natural simian immunodeficiency virus and human immunodeficiency virus type 1 Nef alleles in lymphocyte activation. J. Virol. 71 (1997) 6094-6099
    • (1997) J. Virol. , vol.71 , pp. 6094-6099
    • Alexander, L.1    Du, Z.2    Rosenzweig, M.3    Jung, J.U.4    Desrosiers, R.C.5
  • 7
    • 0036230879 scopus 로고    scopus 로고
    • Live and let die: Nef functions beyond HIV replication
    • Fackler O.T., and Baur A.S. Live and let die: Nef functions beyond HIV replication. Immunity 16 (2002) 493-497
    • (2002) Immunity , vol.16 , pp. 493-497
    • Fackler, O.T.1    Baur, A.S.2
  • 8
    • 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., and McMichael A. Nef triggers a transcriptional program in T cells imitating single-signal T cell activation and inducing HIV virulence mediators. Immunity 14 (2001) 763-777
    • (2001) Immunity , vol.14 , pp. 763-777
    • Simmons, A.1    Aluvihare, V.2    McMichael, A.3
  • 9
    • 0028485232 scopus 로고
    • HIV-1 Nef leads to inhibition or activation of T cells depending on its intracellular localization
    • Baur A.S., Sawai E.T., Dazin P., Fantl W.J., Cheng-Mayer C., and Peterlin B.M. HIV-1 Nef leads to inhibition or activation of T cells depending on its intracellular localization. Immunity 1 (1994) 373-384
    • (1994) Immunity , vol.1 , pp. 373-384
    • Baur, A.S.1    Sawai, E.T.2    Dazin, P.3    Fantl, W.J.4    Cheng-Mayer, C.5    Peterlin, B.M.6
  • 10
    • 0031039979 scopus 로고    scopus 로고
    • Separable functions of Nef disrupt two aspects of T cell receptor machinery: CD4 expression and CD3 signaling
    • Iafrate A.J., Bronson S., and Skowronski J. Separable functions of Nef disrupt two aspects of T cell receptor machinery: CD4 expression and CD3 signaling. EMBO J. 16 (1997) 673-684
    • (1997) EMBO J. , vol.16 , pp. 673-684
    • Iafrate, A.J.1    Bronson, S.2    Skowronski, J.3
  • 12
    • 0030835321 scopus 로고    scopus 로고
    • Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A
    • Aiken C. Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A. J. Virol. 71 (1997) 5871-5877
    • (1997) J. Virol. , vol.71 , pp. 5871-5877
    • Aiken, C.1
  • 13
    • 0028302998 scopus 로고
    • Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene
    • Chowers M.Y., Spina C.A., Kwoh T.J., Fitch N.J., Richman D.D., and Guatelli J.C. Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene. J. Virol. 68 (1994) 2906-2914
    • (1994) J. Virol. , vol.68 , pp. 2906-2914
    • Chowers, M.Y.1    Spina, C.A.2    Kwoh, T.J.3    Fitch, N.J.4    Richman, D.D.5    Guatelli, J.C.6
  • 14
    • 0028006247 scopus 로고
    • The human immunodeficiency virus-1 nef gene product: a positive factor for viral infection and replication in primary lymphocytes and macrophages
    • Miller M.D., Warmerdam M.T., Gaston I., Greene W.C., and Feinberg M.B. The human immunodeficiency virus-1 nef gene product: a positive factor for viral infection and replication in primary lymphocytes and macrophages. J. Exp. Med. 179 (1994) 101-113
    • (1994) J. Exp. Med. , vol.179 , pp. 101-113
    • Miller, M.D.1    Warmerdam, M.T.2    Gaston, I.3    Greene, W.C.4    Feinberg, M.B.5
  • 16
    • 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., and Thomas G. HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell 111 (2002) 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
  • 17
    • 34147169409 scopus 로고    scopus 로고
    • HIV-1 Nef assembles a Src family kinase-ZAP-70/Syk-PI3K cascade to downregulate cell-surface MHC-I
    • Hung C.H., Thomas L., Ruby C.E., Atkins K.M., Morris N.P., Knight Z.A., et al. HIV-1 Nef assembles a Src family kinase-ZAP-70/Syk-PI3K cascade to downregulate cell-surface MHC-I. Cell Host Microbe 1 (2007) 121-133
    • (2007) Cell Host Microbe , vol.1 , pp. 121-133
    • Hung, C.H.1    Thomas, L.2    Ruby, C.E.3    Atkins, K.M.4    Morris, N.P.5    Knight, Z.A.6
  • 18
    • 0035051976 scopus 로고    scopus 로고
    • Living in oblivion: HIV immune evasion
    • Piguet V., and Trono D. Living in oblivion: HIV immune evasion. Semin. Immunol. 13 (2001) 51-57
    • (2001) Semin. Immunol. , vol.13 , pp. 51-57
    • Piguet, V.1    Trono, D.2
  • 19
    • 0032556872 scopus 로고    scopus 로고
    • HIV-1 Nef protein protects infected primary cells against killing by cytotoxic T lymphocytes
    • Collins K.L., Chen B.K., Kalams S.A., Walker B.D., and Baltimore D. HIV-1 Nef protein protects infected primary cells against killing by cytotoxic T lymphocytes. Nature 391 (1998) 397-401
    • (1998) Nature , vol.391 , pp. 397-401
    • Collins, K.L.1    Chen, B.K.2    Kalams, S.A.3    Walker, B.D.4    Baltimore, D.5
  • 20
    • 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., and 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. 67 (1993) 4923-4931
    • (1993) J. Virol. , vol.67 , pp. 4923-4931
    • Anderson, S.1    Shugars, D.C.2    Swanstrom, R.3    Garcia, J.V.4
  • 21
    • 0027158904 scopus 로고
    • Downregulation of cell-surface CD4 expression by simian immunodeficiency virus Nef prevents viral super infection
    • Benson R.E., Sanfridson A., Ottinger J.S., Doyle C., and Cullen B.R. Downregulation of cell-surface CD4 expression by simian immunodeficiency virus Nef prevents viral super infection. J. Exp. Med. 177 (1993) 1561-1566
    • (1993) J. Exp. Med. , vol.177 , pp. 1561-1566
    • Benson, R.E.1    Sanfridson, A.2    Ottinger, J.S.3    Doyle, C.4    Cullen, B.R.5
  • 22
    • 0025733252 scopus 로고
    • Serine phosphorylation-independent downregulation of cell-surface CD4 by nef
    • Garcia J.V., and Miller A.D. Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature 350 (1991) 508-511
    • (1991) Nature , vol.350 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 23
    • 0027315870 scopus 로고
    • CD4 down-regulation by nef alleles isolated from human immunodeficiency virus type 1-infected individuals
    • Mariani R., and Skowronski J. CD4 down-regulation by nef alleles isolated from human immunodeficiency virus type 1-infected individuals. Proc. Natl Acad. Sci. USA 90 (1993) 5549-5553
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5549-5553
    • Mariani, R.1    Skowronski, J.2
  • 24
    • 0033578072 scopus 로고    scopus 로고
    • Cell-surface expression of CD4 reduces HIV-1 infectivity by blocking Env incorporation in a Nef- and Vpu-inhibitable manner
    • Lama J., Mangasarian A., and Trono D. Cell-surface expression of CD4 reduces HIV-1 infectivity by blocking Env incorporation in a Nef- and Vpu-inhibitable manner. Curr. Biol. 9 (1999) 622-631
    • (1999) Curr. Biol. , vol.9 , pp. 622-631
    • Lama, J.1    Mangasarian, A.2    Trono, D.3
  • 25
    • 0033578016 scopus 로고    scopus 로고
    • Inhibition of HIV-1 progeny virion release by cell-surface CD4 is relieved by expression of the viral Nef protein
    • Ross T.M., Oran A.E., and Cullen B.R. Inhibition of HIV-1 progeny virion release by cell-surface CD4 is relieved by expression of the viral Nef protein. Curr. Biol. 9 (1999) 613-621
    • (1999) Curr. Biol. , vol.9 , pp. 613-621
    • Ross, T.M.1    Oran, A.E.2    Cullen, B.R.3
  • 26
    • 0037127303 scopus 로고    scopus 로고
    • Cell surface CD4 interferes with the infectivity of HIV-1 particles released from T cells
    • Cortes M.J., Wong-Staal F., and Lama J. Cell surface CD4 interferes with the infectivity of HIV-1 particles released from T cells. J. Biol. Chem. 277 (2002) 1770-1779
    • (2002) J. Biol. Chem. , vol.277 , pp. 1770-1779
    • Cortes, M.J.1    Wong-Staal, F.2    Lama, J.3
  • 27
    • 0026786630 scopus 로고
    • High level of surface CD4 prevents stable human immunodeficiency virus infection of T-cell transfectants
    • Marshall W.L., Diamond D.C., Kowalski M.M., and Finberg R.W. High level of surface CD4 prevents stable human immunodeficiency virus infection of T-cell transfectants. J. Virol. 66 (1992) 5492-5499
    • (1992) J. Virol. , vol.66 , pp. 5492-5499
    • Marshall, W.L.1    Diamond, D.C.2    Kowalski, M.M.3    Finberg, R.W.4
  • 28
    • 18844363668 scopus 로고    scopus 로고
    • Biology of the HIV Nef protein
    • Das S.R., and Jameel S. Biology of the HIV Nef protein. Indian J. Med. Res. 121 (2005) 315-332
    • (2005) Indian J. Med. Res. , vol.121 , pp. 315-332
    • Das, S.R.1    Jameel, S.2
  • 29
  • 30
    • 0029015330 scopus 로고
    • Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis
    • Aiken C., and Trono D. Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis. J. Virol. 69 (1995) 5048-5056
    • (1995) J. Virol. , vol.69 , pp. 5048-5056
    • Aiken, C.1    Trono, D.2
  • 31
    • 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., and Dumas C. 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 5 (1997) 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    Dumas, C.7
  • 32
    • 0034894379 scopus 로고    scopus 로고
    • Structure-function relationships in HIV-1 Nef
    • Geyer M., Fackler O.T., and Peterlin B.M. Structure-function relationships in HIV-1 Nef. EMBO Rep. 2 (2001) 580-585
    • (2001) EMBO Rep. , vol.2 , pp. 580-585
    • Geyer, M.1    Fackler, O.T.2    Peterlin, B.M.3
  • 33
    • 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., and Kuriyan J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85 (1996) 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
  • 34
    • 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 L.X., Heveker N., Fackler O.T., Arold S., Le Gall S., Janvier K., et al. 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 (2000) 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    Janvier, K.6
  • 35
    • 10644261241 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef domains required for disruption of major histocompatibility complex class I trafficking are also necessary for coprecipitation of Nef with HLA-A2
    • Williams M., Roeth J.F., Kasper M.R., Filzen T.M., and Collins K.L. Human immunodeficiency virus type 1 Nef domains required for disruption of major histocompatibility complex class I trafficking are also necessary for coprecipitation of Nef with HLA-A2. J. Virol. 79 (2005) 632-636
    • (2005) J. Virol. , vol.79 , pp. 632-636
    • Williams, M.1    Roeth, J.F.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 36
    • 10844282788 scopus 로고    scopus 로고
    • Oligomerization is required for HIV-1 Nef-induced activation of the Src family protein-tyrosine kinase, Hck
    • Ye H., Choi H.J., Poe J., and Smithgall T.E. Oligomerization is required for HIV-1 Nef-induced activation of the Src family protein-tyrosine kinase, Hck. Biochemistry 43 (2004) 15775-15784
    • (2004) Biochemistry , vol.43 , pp. 15775-15784
    • Ye, H.1    Choi, H.J.2    Poe, J.3    Smithgall, T.E.4
  • 37
    • 6344276677 scopus 로고    scopus 로고
    • Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase
    • Choi H.J., and Smithgall T.E. Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase. J. Mol. Biol. 343 (2004) 1255-1268
    • (2004) J. Mol. Biol. , vol.343 , pp. 1255-1268
    • Choi, H.J.1    Smithgall, T.E.2
  • 38
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • Shyu Y.J., Liu H., Deng X., and Hu C.D. Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. BioTechniques 40 (2006) 61-66
    • (2006) BioTechniques , vol.40 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.D.4
  • 39
    • 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., and Geyer M. Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef. Biochemistry 45 (2006) 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
  • 40
    • 0035844009 scopus 로고    scopus 로고
    • Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef
    • Geyer M., and Peterlin B.M. Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef. FEBS Lett. 496 (2001) 91-95
    • (2001) FEBS Lett. , vol.496 , pp. 91-95
    • Geyer, M.1    Peterlin, B.M.2
  • 41
    • 0032553012 scopus 로고    scopus 로고
    • RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef
    • Arold S., O'Brien R., Franken P., Strub M.P., Hoh F., Dumas C., and Ladbury J.E. RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef. Biochemistry 37 (1998) 14683-14691
    • (1998) Biochemistry , vol.37 , pp. 14683-14691
    • Arold, S.1    O'Brien, R.2    Franken, P.3    Strub, M.P.4    Hoh, F.5    Dumas, C.6    Ladbury, J.E.7
  • 42
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek S., Bax A., Clore G.M., Gronenborn A.M., Hu J.-S., Kaufman J., et al. The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nat. Struct. Biol. 3 (1996) 340-345
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.-S.5    Kaufman, J.6
  • 43
    • 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., and Trono D. HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes. Nat. Cell Biol. 2 (2000) 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    Trono, D.7
  • 44
    • 0036889125 scopus 로고    scopus 로고
    • Direct binding of human immunodeficiency virus type 1 Nef to the major histocompatibility complex class I (MHC-I) cytoplasmic tail disrupts MHC-I trafficking
    • Williams M., Roeth J.F., Kasper M.R., Fleis R.I., Przybycin C.G., and Collins K.L. Direct binding of human immunodeficiency virus type 1 Nef to the major histocompatibility complex class I (MHC-I) cytoplasmic tail disrupts MHC-I trafficking. J. Virol. 76 (2002) 12173-12184
    • (2002) J. Virol. , vol.76 , pp. 12173-12184
    • Williams, M.1    Roeth, J.F.2    Kasper, M.R.3    Fleis, R.I.4    Przybycin, C.G.5    Collins, K.L.6
  • 45
    • 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., and 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. 87 (2006) 563-571
    • (2006) J. Gen. Virol. , vol.87 , pp. 563-571
    • Bentham, M.1    Mazaleyrat, S.2    Harris, M.3
  • 46
    • 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 C.-H., Leung B., Lemmon M.A., Zheng J., Cowburn D., Kuriyan J., and Saksela K. 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 (1995) 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    Kuriyan, J.6    Saksela, K.7
  • 47
    • 0035907306 scopus 로고    scopus 로고
    • The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein
    • Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D., et al. The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein. J. Biol. Chem. 276 (2001) 16885-16893
    • (2001) J. Biol. Chem. , vol.276 , pp. 16885-16893
    • Hassaine, G.1    Courcoul, M.2    Bessou, G.3    Barthalay, Y.4    Picard, C.5    Olive, D.6
  • 48
    • 0037160057 scopus 로고    scopus 로고
    • Activation of Stat3 by the Src family kinase Hck requires a functional SH3 domain
    • Schreiner S.J., Schiavone A.P., and Smithgall T.E. Activation of Stat3 by the Src family kinase Hck requires a functional SH3 domain. J. Biol. Chem. 277 (2002) 45680-45687
    • (2002) J. Biol. Chem. , vol.277 , pp. 45680-45687
    • Schreiner, S.J.1    Schiavone, A.P.2    Smithgall, T.E.3
  • 49
    • 0034795885 scopus 로고    scopus 로고
    • CD4 down-modulation by human immunodeficiency virus type 1 Nef correlates with the efficiency of viral replication and with CD4(+) T-cell depletion in human lymphoid tissue ex vivo
    • Glushakova S., Munch J., Carl S., Greenough T.C., Sullivan J.L., Margolis L., and Kirchhoff F. CD4 down-modulation by human immunodeficiency virus type 1 Nef correlates with the efficiency of viral replication and with CD4(+) T-cell depletion in human lymphoid tissue ex vivo. J. Virol. 75 (2001) 10113-10117
    • (2001) J. Virol. , vol.75 , pp. 10113-10117
    • Glushakova, S.1    Munch, J.2    Carl, S.3    Greenough, T.C.4    Sullivan, J.L.5    Margolis, L.6    Kirchhoff, F.7
  • 50
    • 0036231461 scopus 로고    scopus 로고
    • Nef-mediated downregulation of CD4 enhances human immunodeficiency virus type 1 replication in primary T lymphocytes
    • Lundquist C.A., Tobiume M., Zhou J., Unutmaz D., and Aiken C. Nef-mediated downregulation of CD4 enhances human immunodeficiency virus type 1 replication in primary T lymphocytes. J. Virol. 76 (2002) 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
  • 51
    • 67649410579 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: a non-pathogenic Nef mutant-based anti-HIV strategy
    • Green L.A., Liu Y., and He J.J. Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: a non-pathogenic Nef mutant-based anti-HIV strategy. J. Biol. Chem. 284 (2009) 13363-13372
    • (2009) J. Biol. Chem. , vol.284 , pp. 13363-13372
    • Green, L.A.1    Liu, Y.2    He, J.J.3
  • 52
    • 0034820906 scopus 로고    scopus 로고
    • HIV type 1 chemokine receptor usage in mother-to-child transmission
    • Salvatori F., and Scarlatti G. HIV type 1 chemokine receptor usage in mother-to-child transmission. AIDS Res. Hum. Retroviruses 17 (2001) 925-935
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 925-935
    • Salvatori, F.1    Scarlatti, G.2
  • 53
    • 0031936306 scopus 로고    scopus 로고
    • Neutralization sensitivity of human immunodeficiency virus type 1 primary isolates to antibodies and CD4-based reagents is independent of coreceptor usage
    • Trkola A., Ketas T., Kewalramani V.N., Endorf F., Binley J.M., Katinger H., et al. Neutralization sensitivity of human immunodeficiency virus type 1 primary isolates to antibodies and CD4-based reagents is independent of coreceptor usage. J. Virol. 72 (1998) 1876-1885
    • (1998) J. Virol. , vol.72 , pp. 1876-1885
    • Trkola, A.1    Ketas, T.2    Kewalramani, V.N.3    Endorf, F.4    Binley, J.M.5    Katinger, H.6
  • 54
    • 7044239645 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in plants using bimolecular fluorescence complementation
    • Bracha-Drori K., Shichrur K., Katz A., Oliva M., Angelovici R., Yalovsky S., and Ohad N. Detection of protein-protein interactions in plants using bimolecular fluorescence complementation. Plant J. 40 (2004) 419-427
    • (2004) Plant J. , vol.40 , pp. 419-427
    • Bracha-Drori, K.1    Shichrur, K.2    Katz, A.3    Oliva, M.4    Angelovici, R.5    Yalovsky, S.6    Ohad, N.7
  • 55
    • 2942559261 scopus 로고    scopus 로고
    • Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells
    • Grinberg A.V., Hu C.D., and Kerppola T.K. Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells. Mol. Cell. Biol. 24 (2004) 4294-4308
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4294-4308
    • Grinberg, A.V.1    Hu, C.D.2    Kerppola, T.K.3
  • 56
    • 3142766112 scopus 로고    scopus 로고
    • Visualization of G protein betagamma dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting
    • Hynes T.R., Tang L., Mervine S.M., Sabo J.L., Yost E.A., Devreotes P.N., and Berlot C.H. Visualization of G protein betagamma dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting. J. Biol. Chem. 279 (2004) 30279-30286
    • (2004) J. Biol. Chem. , vol.279 , pp. 30279-30286
    • Hynes, T.R.1    Tang, L.2    Mervine, S.M.3    Sabo, J.L.4    Yost, E.A.5    Devreotes, P.N.6    Berlot, C.H.7
  • 57
    • 34247525991 scopus 로고    scopus 로고
    • Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case
    • Morell M., Espargaro A., Aviles F.X., and Ventura S. Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 7 (2007) 1023-1036
    • (2007) Proteomics , vol.7 , pp. 1023-1036
    • Morell, M.1    Espargaro, A.2    Aviles, F.X.3    Ventura, S.4
  • 58
    • 13244266915 scopus 로고    scopus 로고
    • Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo
    • Matsubara M., Jing T., Kawamura K., Shimojo N., Titani K., Hashimoto K., and Hayashi N. Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo. Protein Sci. 14 (2005) 494-503
    • (2005) Protein Sci. , vol.14 , pp. 494-503
    • Matsubara, M.1    Jing, T.2    Kawamura, K.3    Shimojo, N.4    Titani, K.5    Hashimoto, K.6    Hayashi, N.7
  • 59
    • 0034602776 scopus 로고    scopus 로고
    • The Nef protein of HIV-1 associates with rafts and primes T cells for activation
    • Wang J.K., Kiyokawa E., Verdin E., and Trono D. The Nef protein of HIV-1 associates with rafts and primes T cells for activation. Proc. Natl Acad. Sci. USA 97 (2000) 394-399
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 394-399
    • Wang, J.K.1    Kiyokawa, E.2    Verdin, E.3    Trono, D.4
  • 60
    • 0033917035 scopus 로고    scopus 로고
    • Characterization and molecular basis of the oligomeric structure of HIV-1 nef protein
    • Arold S., Hoh F., Domergue S., Birck C., Delsuc M.A., Jullien M., and Dumas C. Characterization and molecular basis of the oligomeric structure of HIV-1 nef protein. Protein Sci. 9 (2000) 1137-1148
    • (2000) Protein Sci. , vol.9 , pp. 1137-1148
    • Arold, S.1    Hoh, F.2    Domergue, S.3    Birck, C.4    Delsuc, M.A.5    Jullien, M.6    Dumas, C.7
  • 62
    • 0034134113 scopus 로고    scopus 로고
    • Interactions of HIV-1 NEF with cellular signal transducing proteins
    • Renkema G.H., and Saksela K. Interactions of HIV-1 NEF with cellular signal transducing proteins. Front. Biosci. 5 (2000) D268-D283
    • (2000) Front. Biosci. , vol.5
    • Renkema, G.H.1    Saksela, K.2
  • 63
    • 0033153464 scopus 로고    scopus 로고
    • Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions
    • Fackler O.T., Luo W., Geyer M., Alberts A.S., and Peterlin B.M. Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions. Mol. Cell 3 (1999) 729-739
    • (1999) Mol. Cell , vol.3 , pp. 729-739
    • Fackler, O.T.1    Luo, W.2    Geyer, M.3    Alberts, A.S.4    Peterlin, B.M.5
  • 64
    • 0029064101 scopus 로고
    • A conserved domain and membrane targeting of Nef from HIV and SIV are required for association with a cellular serine kinase activity
    • Sawai E.T., Baur A.S., Peterlin B.M., Levy J.A., and Cheng-Mayer C. A conserved domain and membrane targeting of Nef from HIV and SIV are required for association with a cellular serine kinase activity. J. Biol. Chem. 270 (1995) 15307-15314
    • (1995) J. Biol. Chem. , vol.270 , pp. 15307-15314
    • Sawai, E.T.1    Baur, A.S.2    Peterlin, B.M.3    Levy, J.A.4    Cheng-Mayer, C.5
  • 65
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu C.D., Chinenov Y., and Kerppola T.K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9 (2002) 789-798
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 66
    • 33750321026 scopus 로고    scopus 로고
    • Nef alleles from human immunodeficiency virus type 1-infected long-term-nonprogressor hemophiliacs with or without late disease progression are defective in enhancing virus replication and CD4 down-regulation
    • Crotti A., Neri F., Corti D., Ghezzi S., Heltai S., Baur A., et al. Nef alleles from human immunodeficiency virus type 1-infected long-term-nonprogressor hemophiliacs with or without late disease progression are defective in enhancing virus replication and CD4 down-regulation. J. Virol. 80 (2006) 10663-10674
    • (2006) J. Virol. , vol.80 , pp. 10663-10674
    • Crotti, A.1    Neri, F.2    Corti, D.3    Ghezzi, S.4    Heltai, S.5    Baur, A.6
  • 69
    • 48049095013 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in Caenorhabditis elegans
    • Hiatt S.M., Shyu Y.J., Duren H.M., and Hu C.D. Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in Caenorhabditis elegans. Methods 45 (2008) 185-191
    • (2008) Methods , vol.45 , pp. 185-191
    • Hiatt, S.M.1    Shyu, Y.J.2    Duren, H.M.3    Hu, C.D.4
  • 70
    • 0025959660 scopus 로고
    • BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias
    • Muller A.J., Young J.C., Pendergast A.M., Pondel M., Landau R.N., Littman D.R., and Witte O.N. BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias. Mol. Cell. Biol. 11 (1991) 1785-1792
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1785-1792
    • Muller, A.J.1    Young, J.C.2    Pendergast, A.M.3    Pondel, M.4    Landau, R.N.5    Littman, D.R.6    Witte, O.N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.