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Volumn 368, Issue 1, 2007, Pages 7-16

Structural constraints on human immunodeficiency virus type 1 Nef function

Author keywords

CD4 down modulation; GFP; HIV 1; MHC I down modulation; Nef; PAK 2 activation; Peptide tags; Structure function

Indexed keywords

CD4 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NEF PROTEIN; P21 ACTIVATED KINASE 2;

EID: 35349019766     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.02.036     Document Type: Article
Times cited : (9)

References (50)
  • 1
    • 0029015330 scopus 로고
    • Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis
    • Aiken C., and Trono D. Nef stimulates human immunodeficiency virus type 1 proviral DNA synthesis. J. Virol. 69 8 (1995) 5048-5056
    • (1995) J. Virol. , vol.69 , Issue.8 , pp. 5048-5056
    • Aiken, C.1    Trono, D.2
  • 2
    • 0034001233 scopus 로고    scopus 로고
    • Nef-induced major histocompatibility complex class I down-regulation is functionally dissociated from its virion incorporation, enhancement of viral infectivity, and CD4 down-regulation
    • Akari H., Arold S., Fukumori T., Okazaki T., Strebel K., and Adachi A. Nef-induced major histocompatibility complex class I down-regulation is functionally dissociated from its virion incorporation, enhancement of viral infectivity, and CD4 down-regulation. J. Virol. 74 6 (2000) 2907-2912
    • (2000) J. Virol. , vol.74 , Issue.6 , pp. 2907-2912
    • Akari, H.1    Arold, S.2    Fukumori, T.3    Okazaki, T.4    Strebel, K.5    Adachi, A.6
  • 3
    • 0035368515 scopus 로고    scopus 로고
    • Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein
    • Arold S.T., and Baur A.S. Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein. Trends Biochem. Sci. 26 6 (2001) 356-363
    • (2001) Trends Biochem. Sci. , vol.26 , Issue.6 , pp. 356-363
    • Arold, S.T.1    Baur, A.S.2
  • 4
    • 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 10 (1997) 1361-1372
    • (1997) Structure , vol.5 , Issue.10 , 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
  • 5
    • 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 6 (2000) 1137-1148
    • (2000) Protein Sci. , vol.9 , Issue.6 , 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
  • 7
    • 0028062729 scopus 로고
    • Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic
    • Benichou S., Bomsel M., Bodeus M., Durand H., Doute M., Letourneur F., Camonis J., and Benarous R. Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic. J. Biol. Chem. 269 48 (1994) 30073-30076
    • (1994) J. Biol. Chem. , vol.269 , Issue.48 , pp. 30073-30076
    • Benichou, S.1    Bomsel, M.2    Bodeus, M.3    Durand, H.4    Doute, M.5    Letourneur, F.6    Camonis, J.7    Benarous, R.8
  • 8
    • 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 6 (1993) 1561-1566
    • (1993) J. Exp. Med. , vol.177 , Issue.6 , pp. 1561-1566
    • Benson, R.E.1    Sanfridson, A.2    Ottinger, J.S.3    Doyle, C.4    Cullen, B.R.5
  • 9
    • 0141730449 scopus 로고    scopus 로고
    • The di-leucine motif in the cytoplasmic tail of CD4 is not required for binding to human immunodeficiency virus type 1 Nef, but is critical for CD4 down-modulation
    • Bentham M., Mazaleyrat S., and Harris M. The di-leucine motif in the cytoplasmic tail of CD4 is not required for binding to human immunodeficiency virus type 1 Nef, but is critical for CD4 down-modulation. J. Gen. Virol. 84 Pt. 10 (2003) 2705-2713
    • (2003) J. Gen. Virol. , vol.84 , Issue.PART 10 , pp. 2705-2713
    • Bentham, M.1    Mazaleyrat, S.2    Harris, M.3
  • 10
    • 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 6 (2002) 853-866
    • (2002) Cell , vol.111 , Issue.6 , pp. 853-866
    • Blagoveshchenskaya, A.D.1    Thomas, L.2    Feliciangeli, S.F.3    Hung, C.H.4    Thomas, G.5
  • 11
    • 0033568211 scopus 로고    scopus 로고
    • Cutting edge: SIV Nef protein utilizes both leucine- and tyrosine-based protein sorting pathways for down-regulation of CD4
    • Bresnahan P.A., Yonemoto W., and Greene W.C. Cutting edge: SIV Nef protein utilizes both leucine- and tyrosine-based protein sorting pathways for down-regulation of CD4. J. Immunol. 163 6 (1999) 2977-2981
    • (1999) J. Immunol. , vol.163 , Issue.6 , pp. 2977-2981
    • Bresnahan, P.A.1    Yonemoto, W.2    Greene, W.C.3
  • 13
    • 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., and 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. 73 12 (1999) 9899-9907
    • (1999) J. Virol. , vol.73 , Issue.12 , pp. 9899-9907
    • Brown, A.1    Wang, X.2    Sawai, E.3    Cheng-Mayer, C.4
  • 15
    • 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 5 (1994) 2906-2914
    • (1994) J. Virol. , vol.68 , Issue.5 , 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
  • 16
    • 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 6665 (1998) 397-401
    • (1998) Nature , vol.391 , Issue.6665 , pp. 397-401
    • Collins, K.L.1    Chen, B.K.2    Kalams, S.A.3    Walker, B.D.4    Baltimore, D.5
  • 17
    • 0032530773 scopus 로고    scopus 로고
    • Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity
    • Craig H.M., Pandori M.W., and Guatelli J.C. Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity. Proc. Natl. Acad. Sci. U.S.A. 95 19 (1998) 11229-11234
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.19 , pp. 11229-11234
    • Craig, H.M.1    Pandori, M.W.2    Guatelli, J.C.3
  • 18
    • 0034713437 scopus 로고    scopus 로고
    • Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif
    • Craig H.M., Reddy T.R., Riggs N.L., Dao P.P., and Guatelli J.C. Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif. Virology 271 1 (2000) 9-17
    • (2000) Virology , vol.271 , Issue.1 , pp. 9-17
    • Craig, H.M.1    Reddy, T.R.2    Riggs, N.L.3    Dao, P.P.4    Guatelli, J.C.5
  • 19
    • 27144505682 scopus 로고    scopus 로고
    • Nef is physically recruited into the immunological synapse and potentiates T cell activation early after TCR engagement
    • Fenard D., Yonemoto W., de Noronha C., Cavrois M., Williams S.A., and Greene W.C. Nef is physically recruited into the immunological synapse and potentiates T cell activation early after TCR engagement. J. Immunol. 175 9 (2005) 6050-6057
    • (2005) J. Immunol. , vol.175 , Issue.9 , pp. 6050-6057
    • Fenard, D.1    Yonemoto, W.2    de Noronha, C.3    Cavrois, M.4    Williams, S.A.5    Greene, W.C.6
  • 20
    • 0035138509 scopus 로고    scopus 로고
    • Genetic and functional diversity of human immunodeficiency virus type 1 subtype B Nef primary isolates
    • Foster J.L., Molina R.P., Luo T., Arora V.K., Huang Y., Ho D.D., and Garcia J.V. Genetic and functional diversity of human immunodeficiency virus type 1 subtype B Nef primary isolates. J. Virol. 75 4 (2001) 1672-1680
    • (2001) J. Virol. , vol.75 , Issue.4 , pp. 1672-1680
    • Foster, J.L.1    Molina, R.P.2    Luo, T.3    Arora, V.K.4    Huang, Y.5    Ho, D.D.6    Garcia, J.V.7
  • 21
    • 0030589550 scopus 로고    scopus 로고
    • Structural and functional correlates between HIV-1 and SIV Nef isolates
    • Garcia J.V., and Foster J.L. Structural and functional correlates between HIV-1 and SIV Nef isolates. Virology 226 2 (1996) 161-166
    • (1996) Virology , vol.226 , Issue.2 , pp. 161-166
    • Garcia, J.V.1    Foster, J.L.2
  • 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 6318 (1991) 508-511
    • (1991) Nature , vol.350 , Issue.6318 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 23
    • 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., and Kalbitzer H.R. Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. J. Mol. Biol. 289 1 (1999) 123-138
    • (1999) J. Mol. Biol. , vol.289 , Issue.1 , pp. 123-138
    • Geyer, M.1    Munte, C.E.2    Schorr, J.3    Kellner, R.4    Kalbitzer, H.R.5
  • 24
    • 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 7 (2001) 580-585
    • (2001) EMBO Rep. , vol.2 , Issue.7 , pp. 580-585
    • Geyer, M.1    Fackler, O.T.2    Peterlin, B.M.3
  • 25
    • 0037047282 scopus 로고    scopus 로고
    • Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery
    • Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.H., Fackler O.T., and Peterlin B.M. Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery. J. Biol. Chem. 277 32 (2002) 28521-28529
    • (2002) J. Biol. Chem. , vol.277 , Issue.32 , pp. 28521-28529
    • Geyer, M.1    Yu, H.2    Mandic, R.3    Linnemann, T.4    Zheng, Y.H.5    Fackler, O.T.6    Peterlin, B.M.7
  • 26
    • 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., and Skowronski J. Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation. EMBO J. 16 23 (1997) 6964-6976
    • (1997) EMBO J. , vol.16 , Issue.23 , pp. 6964-6976
    • Greenberg, M.E.1    Bronson, S.2    Lock, M.3    Neumann, M.4    Pavlakis, G.N.5    Skowronski, J.6
  • 27
    • 0032488055 scopus 로고    scopus 로고
    • A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4
    • Greenberg M., DeTulleo L., Rapoport I., Skowronski J., and Kirchhausen T. A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4. Curr. Biol. 8 22 (1998) 1239-1242
    • (1998) Curr. Biol. , vol.8 , Issue.22 , pp. 1239-1242
    • Greenberg, M.1    DeTulleo, L.2    Rapoport, I.3    Skowronski, J.4    Kirchhausen, T.5
  • 28
    • 0032525137 scopus 로고    scopus 로고
    • The SH3 domain-binding surface and an acidic motif in HIV-1 Nef regulate trafficking of class I MHC complexes
    • Greenberg M.E., Iafrate A.J., and Skowronski J. The SH3 domain-binding surface and an acidic motif in HIV-1 Nef regulate trafficking of class I MHC complexes. EMBO J. 17 10 (1998) 2777-2789
    • (1998) EMBO J. , vol.17 , Issue.10 , pp. 2777-2789
    • Greenberg, M.E.1    Iafrate, A.J.2    Skowronski, J.3
  • 29
    • 0023659754 scopus 로고
    • HIV F/3′ orf encodes a phosphorylated GTP-binding protein resembling an oncogene product
    • Guy B., Kieny M.P., Riviere Y., Le Peuch C., Dott K., Girard M., Montagnier L., and Lecocq J.P. HIV F/3′ orf encodes a phosphorylated GTP-binding protein resembling an oncogene product. Nature 330 6145 (1987) 266-269
    • (1987) Nature , vol.330 , Issue.6145 , pp. 266-269
    • Guy, B.1    Kieny, M.P.2    Riviere, Y.3    Le Peuch, C.4    Dott, K.5    Girard, M.6    Montagnier, L.7    Lecocq, J.P.8
  • 30
    • 33746882478 scopus 로고    scopus 로고
    • Conformational features of the full-length HIV and SIV Nef proteins determined by mass spectrometry
    • Hochrein J.M., Wales T.E., Lerner E.C., Schiavone A.P., Smithgall T.E., and Engen J.R. Conformational features of the full-length HIV and SIV Nef proteins determined by mass spectrometry. Biochemistry 45 25 (2006) 7733-7739
    • (2006) Biochemistry , vol.45 , Issue.25 , pp. 7733-7739
    • Hochrein, J.M.1    Wales, T.E.2    Lerner, E.C.3    Schiavone, A.P.4    Smithgall, T.E.5    Engen, J.R.6
  • 31
    • 19344363916 scopus 로고    scopus 로고
    • HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis
    • Janardhan A., Swigut T., Hill B., Myers M.P., and Skowronski J. HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis. PLoS Biol. 2 1 (2004) E6
    • (2004) PLoS Biol. , vol.2 , Issue.1
    • Janardhan, A.1    Swigut, T.2    Hill, B.3    Myers, M.P.4    Skowronski, J.5
  • 32
    • 0035080263 scopus 로고    scopus 로고
    • Nef-induced CD4 downregulation: a diacidic sequence in human immunodeficiency virus type 1 Nef does not function as a protein sorting motif through direct binding to beta-COP
    • Janvier K., Craig H., Le Gall S., Benarous R., Guatelli J., Schwartz O., and Benichou S. Nef-induced CD4 downregulation: a diacidic sequence in human immunodeficiency virus type 1 Nef does not function as a protein sorting motif through direct binding to beta-COP. J. Virol. 75 8 (2001) 3971-3976
    • (2001) J. Virol. , vol.75 , Issue.8 , pp. 3971-3976
    • Janvier, K.1    Craig, H.2    Le Gall, S.3    Benarous, R.4    Guatelli, J.5    Schwartz, O.6    Benichou, S.7
  • 34
    • 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 12 (1999) 622-631
    • (1999) Curr. Biol. , vol.9 , Issue.12 , pp. 622-631
    • Lama, J.1    Mangasarian, A.2    Trono, D.3
  • 35
    • 0032076086 scopus 로고    scopus 로고
    • Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4
    • Lu X., Yu H., Liu S.H., Brodsky F.M., and Peterlin B.M. Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4. Immunity 8 5 (1998) 647-656
    • (1998) Immunity , vol.8 , Issue.5 , pp. 647-656
    • Lu, X.1    Yu, H.2    Liu, S.H.3    Brodsky, F.M.4    Peterlin, B.M.5
  • 36
    • 0029835631 scopus 로고    scopus 로고
    • The association of Nef with a cellular serine/threonine kinase and its enhancement of infectivity are viral isolate dependent
    • Luo T., and Garcia J.V. The association of Nef with a cellular serine/threonine kinase and its enhancement of infectivity are viral isolate dependent. J. Virol. 70 9 (1996) 6493-6496
    • (1996) J. Virol. , vol.70 , Issue.9 , pp. 6493-6496
    • Luo, T.1    Garcia, J.V.2
  • 37
    • 0030614819 scopus 로고    scopus 로고
    • The HIV-1 Nef protein acts as a connector with sorting pathways in the Golgi and at the plasma membrane
    • Mangasarian A., Foti M., Aiken C., Chin D., Carpentier J.L., and Trono D. The HIV-1 Nef protein acts as a connector with sorting pathways in the Golgi and at the plasma membrane. Immunity 6 1 (1997) 67-77
    • (1997) Immunity , vol.6 , Issue.1 , pp. 67-77
    • Mangasarian, A.1    Foti, M.2    Aiken, C.3    Chin, D.4    Carpentier, J.L.5    Trono, D.6
  • 38
    • 0033013962 scopus 로고    scopus 로고
    • Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-terminal alpha helix and proline repeat of Nef selectively regulate MHC-I trafficking
    • Mangasarian A., Piguet V., Wang J.K., Chen Y.L., and Trono D. Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-terminal alpha helix and proline repeat of Nef selectively regulate MHC-I trafficking. J. Virol. 73 3 (1999) 1964-1973
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 1964-1973
    • Mangasarian, A.1    Piguet, V.2    Wang, J.K.3    Chen, Y.L.4    Trono, D.5
  • 39
    • 31144476786 scopus 로고    scopus 로고
    • Dynamic evolution of the human immunodeficiency virus type 1 pathogenic factor, Nef
    • O'Neill E., Kuo L.S., Krisko J.F., Tomchick D.R., Garcia J.V., and Foster J.L. Dynamic evolution of the human immunodeficiency virus type 1 pathogenic factor, Nef. J. Virol. 80 3 (2006) 1311-1320
    • (2006) J. Virol. , vol.80 , Issue.3 , pp. 1311-1320
    • O'Neill, E.1    Kuo, L.S.2    Krisko, J.F.3    Tomchick, D.R.4    Garcia, J.V.5    Foster, J.L.6
  • 40
    • 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 3 (2000) 163-167
    • (2000) Nat. Cell Biol. , vol.2 , Issue.3 , pp. 163-167
    • Piguet, V.1    Wan, L.2    Borel, C.3    Mangasarian, A.4    Demaurex, N.5    Thomas, G.6    Trono, D.7
  • 41
    • 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., and 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. 75 5 (2001) 2154-2160
    • (2001) J. Virol. , vol.75 , Issue.5 , pp. 2154-2160
    • Renkema, G.H.1    Manninen, A.2    Saksela, K.3
  • 42
    • 33745122662 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways
    • Roeth J.F., and Collins K.L. Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways. Microbiol. Mol. Biol. Rev. 70 2 (2006) 548-563
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , Issue.2 , pp. 548-563
    • Roeth, J.F.1    Collins, K.L.2
  • 43
    • 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 12 (1999) 613-621
    • (1999) Curr. Biol. , vol.9 , Issue.12 , pp. 613-621
    • Ross, T.M.1    Oran, A.E.2    Cullen, B.R.3
  • 45
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein
    • Schwartz O., Marechal V., Le Gall S., Lemonnier F., and Heard J.M. Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat. Med. 2 3 (1996) 338-342
    • (1996) Nat. Med. , vol.2 , Issue.3 , pp. 338-342
    • Schwartz, O.1    Marechal, V.2    Le Gall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 46
    • 8644289282 scopus 로고    scopus 로고
    • Impact of Nef-mediated downregulation of major histocompatibility complex class I on immune response to simian immunodeficiency virus
    • Swigut T., Alexander L., Morgan J., Lifson J., Mansfield K.G., Lang S., Johnson R.P., Skowronski J., and Desrosiers R. Impact of Nef-mediated downregulation of major histocompatibility complex class I on immune response to simian immunodeficiency virus. J. Virol. 78 23 (2004) 13335-13344
    • (2004) J. Virol. , vol.78 , Issue.23 , pp. 13335-13344
    • Swigut, T.1    Alexander, L.2    Morgan, J.3    Lifson, J.4    Mansfield, K.G.5    Lang, S.6    Johnson, R.P.7    Skowronski, J.8    Desrosiers, R.9
  • 48
    • 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 23 (2002) 12173-12184
    • (2002) J. Virol. , vol.76 , Issue.23 , 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
  • 49
    • 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 1 (2005) 632-636
    • (2005) J. Virol. , vol.79 , Issue.1 , pp. 632-636
    • Williams, M.1    Roeth, J.F.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 50
    • 0030273317 scopus 로고    scopus 로고
    • HIV-1 Nef association with cellular serine kinase correlates with enhanced virion infectivity and efficient proviral DNA synthesis
    • Wiskerchen M., and Cheng-Mayer C. HIV-1 Nef association with cellular serine kinase correlates with enhanced virion infectivity and efficient proviral DNA synthesis. Virology 224 1 (1996) 292-301
    • (1996) Virology , vol.224 , Issue.1 , pp. 292-301
    • Wiskerchen, M.1    Cheng-Mayer, C.2


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