메뉴 건너뛰기




Volumn 29, Issue 3, 2014, Pages 275-286

HIV-1 viral infectivity factor interacts with microtubule-associated protein light chain 3 and inhibits autophagy

Author keywords

APOBEC3G; Autophagy; HIV; Microtubule associated protein light chain 3; Viral infectivity factor

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CD4 ANTIGEN; CHEMOKINE RECEPTOR CXCR4; GLYCINE; HOST FACTOR; MESSENGER RNA; MICROTUBULE ASSOCIATED PROTEIN; MICROTUBULE ASSOCIATED PROTEIN LIGHT CHAIN 3B; UNCLASSIFIED DRUG; VIRAL INFECTIVITY FACTOR; VIRUS PROTEIN; LIGHT CHAIN 3, HUMAN; PROTEIN BINDING; VIF PROTEIN; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84927561935     PISSN: 02699370     EISSN: 14735571     Source Type: Journal    
DOI: 10.1097/QAD.0000000000000554     Document Type: Article
Times cited : (50)

References (55)
  • 2
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6
  • 4
    • 4344604111 scopus 로고    scopus 로고
    • HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates
    • Tanida I, Sou YS, Ezaki J, Minematsu-Ikeguchi N, Ueno T, Kominami E. HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates. J Biol Chem 2004; 279:36268-36276.
    • (2004) J Biol Chem , vol.279 , pp. 36268-36276
    • Tanida, I.1    Sou, Y.S.2    Ezaki, J.3    Minematsu-Ikeguchi, N.4    Ueno, T.5    Kominami, E.6
  • 5
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic V, Levine B. Autophagy, immunity, and microbial adaptations. Cell Host Microbe 2009; 5:527-549.
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 6
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B, Mizushima N, Virgin HW. Autophagy in immunity and inflammation. Nature 2011; 469:323-335.
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 7
    • 33746691954 scopus 로고    scopus 로고
    • Autophagy is involved in T cell death after binding of HIV-1 envelope proteins to CXCR4
    • Espert L, Denizot M, Grimaldi M, Robert-Hebmann V, Gay B, Varbanov M, et al. Autophagy is involved in T cell death after binding of HIV-1 envelope proteins to CXCR4. J Clin Invest 2006; 116:2161-2172.
    • (2006) J Clin Invest , vol.116 , pp. 2161-2172
    • Espert, L.1    Denizot, M.2    Grimaldi, M.3    Robert-Hebmann, V.4    Gay, B.5    Varbanov, M.6
  • 8
    • 66749170589 scopus 로고    scopus 로고
    • Differential role of autophagy in CD4 T cells and macrophages during X4 and R5 HIV-1 infection
    • Espert L, Varbanov M, Robert-Hebmann V, Sagnier S, Robbins I, Sanchez F, et al. Differential role of autophagy in CD4 T cells and macrophages during X4 and R5 HIV-1 infection. PLoS One 2009; 4:e5787.
    • (2009) PLoS One , vol.4 , pp. e5787
    • Espert, L.1    Varbanov, M.2    Robert-Hebmann, V.3    Sagnier, S.4    Robbins, I.5    Sanchez, F.6
  • 9
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier D, Bouchonnet F, Clavel F, Hance AJ. Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 2003; 300:1112.
    • (2003) Science , vol.300 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 11
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV- 1 Vif
    • Sheehy AM, Gaddis NC, Malim MH. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV- 1 Vif. Nat Med 2003; 9:1404-1407.
    • (2003) Nat Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 12
    • 84871943090 scopus 로고    scopus 로고
    • APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4R T cells and macrophages
    • Chaipan C, Smith JL, Hu WS, Pathak VK. APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4R T cells and macrophages. J Virol 2013; 87:444-453.
    • (2013) J Virol , vol.87 , pp. 444-453
    • Chaipan, C.1    Smith, J.L.2    Hu, W.S.3    Pathak, V.K.4
  • 13
    • 77954684927 scopus 로고    scopus 로고
    • The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex
    • Bergeron JR, Huthoff H, Veselkov DA, Beavil RL, Simpson PJ, Matthews SJ, et al. The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex. PLoS Pathog 2010; 6:e1000925.
    • (2010) PLoS Pathog , vol.6 , pp. e1000925
    • Bergeron, J.R.1    Huthoff, H.2    Veselkov, D.A.3    Beavil, R.L.4    Simpson, P.J.5    Matthews, S.J.6
  • 14
    • 84856009926 scopus 로고    scopus 로고
    • Vif hijacks CBF-beta to degrade APOBEC3G and promote HIV-1 infection
    • Jager S, Kim DY, Hultquist JF, Shindo K, LaRue RS, Kwon E, et al. Vif hijacks CBF-beta to degrade APOBEC3G and promote HIV-1 infection. Nature 2011; 481:371-375.
    • (2011) Nature , vol.481 , pp. 371-375
    • Jager, S.1    Kim, D.Y.2    Hultquist, J.F.3    Shindo, K.4    Larue, R.S.5    Kwon, E.6
  • 15
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-beta regulates HIV-1 Vif-mediated evasion of host restriction
    • Zhang W, Du J, Evans SL, Yu Y, Yu XF. T-cell differentiation factor CBF-beta regulates HIV-1 Vif-mediated evasion of host restriction. Nature 2011; 481:376-379.
    • (2011) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.F.5
  • 16
    • 66749141973 scopus 로고    scopus 로고
    • Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors
    • Henriet S, Mercenne G, Bernacchi S, Paillart JC, Marquet R. Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors. Microbiol Mol Biol Rev 2009; 73:211-232.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 211-232
    • Henriet, S.1    Mercenne, G.2    Bernacchi, S.3    Paillart, J.C.4    Marquet, R.5
  • 17
    • 77953757638 scopus 로고    scopus 로고
    • Dissection of the HIV Vif interaction with human E3 ubiquitin ligase
    • Wolfe LS, Stanley BJ, Liu C, Eliason WK, Xiong Y. Dissection of the HIV Vif interaction with human E3 ubiquitin ligase. J Virol 2010; 84:7135-7139.
    • (2010) J Virol , vol.84 , pp. 7135-7139
    • Wolfe, L.S.1    Stanley, B.J.2    Liu, C.3    Eliason, W.K.4    Xiong, Y.5
  • 18
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, et al. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci U S A 2005; 102:11444-11449.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11444-11449
    • Luo, K.1    Xiao, Z.2    Ehrlich, E.3    Yu, Y.4    Liu, B.5    Zheng, S.6
  • 19
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • Stanley BJ, Ehrlich ES, Short L, Yu Y, Xiao Z, Yu XF, et al. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J Virol 2008; 82:8656-8663.
    • (2008) J Virol , vol.82 , pp. 8656-8663
    • Stanley, B.J.1    Ehrlich, E.S.2    Short, L.3    Yu, Y.4    Xiao, Z.5    Yu, X.F.6
  • 20
    • 79953686217 scopus 로고    scopus 로고
    • Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif
    • Bernacchi S, Mercenne G, Tournaire C, Marquet R, Paillart JC. Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif. Nucleic Acids Res 2011; 39:2404-2415.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2404-2415
    • Bernacchi, S.1    Mercenne, G.2    Tournaire, C.3    Marquet, R.4    Paillart, J.C.5
  • 21
    • 0030985926 scopus 로고    scopus 로고
    • The Vif and Gag proteins of human immunodeficiency virus type 1 colocalize in infected human T cells
    • Simon JH, Fouchier RA, Southerling TE, Guerra CB, Grant CK, Malim MH. The Vif and Gag proteins of human immunodeficiency virus type 1 colocalize in infected human T cells. J Virol 1997; 71:5259-5267.
    • (1997) J Virol , vol.71 , pp. 5259-5267
    • Simon, J.H.1    Fouchier, R.A.2    Southerling, T.E.3    Guerra, C.B.4    Grant, C.K.5    Malim, M.H.6
  • 22
    • 0037458718 scopus 로고    scopus 로고
    • Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins
    • Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, et al. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. J Biol Chem 2003; 278:6596-6602.
    • (2003) J Biol Chem , vol.278 , pp. 6596-6602
    • Yang, B.1    Gao, L.2    Li, L.3    Lu, Z.4    Fan, X.5    Patel, C.A.6
  • 23
    • 0035895896 scopus 로고    scopus 로고
    • The multimerization of human immunodeficiency virus type i Vif protein: A requirement for Vif function in the viral life cycle
    • Yang S, Sun Y, Zhang H. The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J Biol Chem 2001; 276:4889-4893.
    • (2001) J Biol Chem , vol.276 , pp. 4889-4893
    • Yang, S.1    Sun, Y.2    Zhang, H.3
  • 24
    • 46549089412 scopus 로고    scopus 로고
    • The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
    • Donahue JP, Vetter ML, Mukhtar NA, D'Aquila RT. The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation. Virology 2008; 377:49-53.
    • (2008) Virology , vol.377 , pp. 49-53
    • Donahue, J.P.1    Vetter, M.L.2    Mukhtar, N.A.3    D'Aquila, R.T.4
  • 25
    • 3242702452 scopus 로고    scopus 로고
    • Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation
    • Fujita M, Akari H, Sakurai A, Yoshida A, Chiba T, Tanaka K, et al. Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation. Microbes Infect 2004; 6:791-798.
    • (2004) Microbes Infect , vol.6 , pp. 791-798
    • Fujita, M.1    Akari, H.2    Sakurai, A.3    Yoshida, A.4    Chiba, T.5    Tanaka, K.6
  • 27
    • 84892188402 scopus 로고    scopus 로고
    • Structural basis for hijacking CBF-beta and CUL5 E3 ligase complex by HIV-1 Vif
    • Guo Y, Dong L, Qiu X, Wang Y, Zhang B, Liu H, et al. Structural basis for hijacking CBF-beta and CUL5 E3 ligase complex by HIV-1 Vif. Nature 2014; 505:229-233.
    • (2014) Nature , vol.505 , pp. 229-233
    • Guo, Y.1    Dong, L.2    Qiu, X.3    Wang, Y.4    Zhang, B.5    Liu, H.6
  • 29
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: An FFTbased protein docking program with pairwise potentials
    • Kozakov D, Brenke R, Comeau SR, Vajda S. PIPER: an FFTbased protein docking program with pairwise potentials. Proteins 2006; 65:392-406.
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4
  • 30
    • 0004232308 scopus 로고    scopus 로고
    • Upper Saddle River, NJ:Prentice-Hall College Div
    • Zar JH. Biostatistical analysis, 3rd ed. Upper Saddle River, NJ: Prentice-Hall College Div; 1996.
    • (1996) Biostatistical Analysis, 3rd Ed
    • Zar, J.H.1
  • 31
    • 34548259958 scopus 로고    scopus 로고
    • P62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282:24131-24145.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6
  • 32
    • 84869222326 scopus 로고    scopus 로고
    • ATG8 family proteins act as scaffolds for assembly of the ULK complex: Sequence requirements for LC3-interacting region (LIR) motifs
    • Alemu EA, Lamark T, TorgersenKM, Birgisdottir AB, Larsen KB, Jain A, et al. ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs. J Biol Chem 2012; 287:39275-39290.
    • (2012) J Biol Chem , vol.287 , pp. 39275-39290
    • Alemu, E.A.1    Lamark, T.2    Torgersen, K.M.3    Birgisdottir, A.B.4    Larsen, K.B.5    Jain, A.6
  • 33
    • 65649136884 scopus 로고    scopus 로고
    • The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
    • Satoo K, Noda NN, Kumeta H, Fujioka Y, Mizushima N, Ohsumi Y, et al. The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy. EMBO J 2009; 28:1341-1350.
    • (2009) EMBO J , vol.28 , pp. 1341-1350
    • Satoo, K.1    Noda, N.N.2    Kumeta, H.3    Fujioka, Y.4    Mizushima, N.5    Ohsumi, Y.6
  • 35
    • 41349095737 scopus 로고    scopus 로고
    • Human immunodeficiency virus type-1 infection inhibits autophagy
    • Zhou D, Spector SA. Human immunodeficiency virus type-1 infection inhibits autophagy. AIDS 2008; 22:695-699.
    • (2008) AIDS , vol.22 , pp. 695-699
    • Zhou, D.1    Spector, S.A.2
  • 36
    • 0037225730 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection
    • Kao S, Akari H, Khan MA, Dettenhofer M, Yu XF, Strebel K. Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection. J Virol 2003; 77:1131-1140.
    • (2003) J Virol , vol.77 , pp. 1131-1140
    • Kao, S.1    Akari, H.2    Khan, M.A.3    Dettenhofer, M.4    Yu, X.F.5    Strebel, K.6
  • 37
  • 39
    • 69249220263 scopus 로고    scopus 로고
    • Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization
    • Dang Y, Wang X, Zhou T, York IA, Zheng YH. Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. J Virol 2009; 83:8544-8552.
    • (2009) J Virol , vol.83 , pp. 8544-8552
    • Dang, Y.1    Wang, X.2    Zhou, T.3    York, I.A.4    Zheng, Y.H.5
  • 40
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • He Z, Zhang W, Chen G, Xu R, Yu XF. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J Mol Biol 2008; 381:1000-1011.
    • (2008) J Mol Biol , vol.381 , pp. 1000-1011
    • He, Z.1    Zhang, W.2    Chen, G.3    Xu, R.4    Yu, X.F.5
  • 41
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M, Rose KM, Kozak SL, Kabat D. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 2003; 9:1398-1403.
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 42
    • 36348946397 scopus 로고    scopus 로고
    • Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding
    • Mehle A, Wilson H, Zhang C, Brazier AJ, McPike M, Pery E, et al. Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding. J Virol 2007; 81:13235-13241.
    • (2007) J Virol , vol.81 , pp. 13235-13241
    • Mehle, A.1    Wilson, H.2    Zhang, C.3    Brazier, A.J.4    McPike, M.5    Pery, E.6
  • 43
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • Russell RA, Pathak VK. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J Virol 2007; 81:8201-8210.
    • (2007) J Virol , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 45
    • 84907582154 scopus 로고    scopus 로고
    • Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein: Importance of the C-terminal unstructured tail
    • Sleiman D, Bernacchi S, Xavier Guerrero S, Brachet F, Larue V, Paillart JC, et al. Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein: Importance of the C-terminal unstructured tail. RNA Biol 2014; 11:906-920.
    • (2014) RNA Biol , vol.11 , pp. 906-920
    • Sleiman, D.1    Bernacchi, S.2    Xavier Guerrero, S.3    Brachet, F.4    Larue, V.5    Paillart, J.C.6
  • 46
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW. Network organization of the human autophagy system. Nature 2010; 466:68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 47
    • 84869080400 scopus 로고    scopus 로고
    • LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy
    • von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein A, Bloor S, Rutherford TJ, et al. LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. Mol Cell 2012; 48:329-342.
    • (2012) Mol Cell , vol.48 , pp. 329-342
    • Von Muhlinen, N.1    Akutsu, M.2    Ravenhill, B.J.3    Foeglein, A.4    Bloor, S.5    Rutherford, T.J.6
  • 48
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston TL, Ryzhakov G, Bloor S, von Muhlinen N, Randow F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 2009; 10:1215-1221.
    • (2009) Nat Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 49
    • 0029961360 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env- encoded proteins
    • Fouchier RA, Simon JH, Jaffe AB, Malim MH. Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env- encoded proteins. J Virol 1996; 70:8263-8269.
    • (1996) J Virol , vol.70 , pp. 8263-8269
    • Fouchier, R.A.1    Simon, J.H.2    Jaffe, A.B.3    Malim, M.H.4
  • 50
    • 79960800953 scopus 로고    scopus 로고
    • Beclin-1 targeting for viral immune escape
    • Munz C. Beclin-1 targeting for viral immune escape. Viruses 2011; 3:1166-1178.
    • (2011) Viruses , vol.3 , pp. 1166-1178
    • Munz, C.1
  • 51
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • Kyei GB, Dinkins C, Davis AS, Roberts E, Singh SB, Dong C, et al. Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J Cell Biol 2009; 186:255-268.
    • (2009) J Cell Biol , vol.186 , pp. 255-268
    • Kyei, G.B.1    Dinkins, C.2    Davis, A.S.3    Roberts, E.4    Singh, S.B.5    Dong, C.6
  • 53
    • 0032126632 scopus 로고    scopus 로고
    • Aut2p and Aut7p, two novel microtubuleassociated proteins are essential for delivery of autophagic vesicles to the vacuole
    • Lang T, Schaeffeler E, Bernreuther D, Bredschneider M, Wolf DH, Thumm M. Aut2p and Aut7p, two novel microtubuleassociated proteins are essential for delivery of autophagic vesicles to the vacuole. EMBO J 1998; 17:3597-3607.
    • (1998) EMBO J , vol.17 , pp. 3597-3607
    • Lang, T.1    Schaeffeler, E.2    Bernreuther, D.3    Bredschneider, M.4    Wolf, D.H.5    Thumm, M.6
  • 54


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.