메뉴 건너뛰기




Volumn 14, Issue 6, 2015, Pages 838-847

Evolutionarily conserved pressure for the existence of distinct g2/m cell cycle arrest and a3h inactivation functions in hiv-1 vif

Author keywords

Apobec3h; Cell cycle regulation; Evolutionary selection; Proteasomal degradation; Vif

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3H; HYDROLASE; PROTEIN VARIANT; UNCLASSIFIED DRUG; VIF PROTEIN; AMINO ACID; APOBEC3H PROTEIN, HUMAN; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84928137477     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.1080/15384101.2014.1000212     Document Type: Article
Times cited : (18)

References (51)
  • 2
    • 0023267788 scopus 로고
    • The HIV A (Sor) gene product is essential for virus infectivity
    • PMID:2441266
    • Strebel K, Daugherty D, Clouse K, Cohen D, Folks T, Martin MA. The HIV A (sor) gene product is essential for virus infectivity. Nature 1987; 328:728-30;PMID:2441266; http://dx.doi.org/10.1038/328728a0
    • (1987) Nature , vol.328 , pp. 728-730
    • Strebel, K.1    Daugherty, D.2    Clouse, K.3    Cohen, D.4    Folks, T.5    Martin, M.A.6
  • 3
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • PMID:12167863
    • Sheehy AM, Gaddis NC, Choi JD, Malim MH. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002; 418:646-50; PMID:12167863; http://dx.doi.org/ 10.1038/nature00939
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 5
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • PMID:14564014
    • Yu X, Yu Y, Liu B, Luo K, Kong W, Mao P, Yu XF. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003; 302:1056-60;PMID:14564014; http://dx.doi. org/10.1126/science.1089591
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 6
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • PMID:14528301;
    • Marin M, Rose KM, Kozak SL, Kabat D. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 2003; 9:1398-403;PMID:14528301; http://dx.doi.org/10.1038/nm946
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 7
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • PMID:14528300;
    • Sheehy AM, Gaddis NC, Malim MH. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med 2003; 9:1404-7;PMID:14528300; http://dx.doi.org/10.1038/nm945
    • (2003) Nat Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 8
    • 0842347676 scopus 로고    scopus 로고
    • Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G
    • PMID:14747572
    • Liu B, Yu X, Luo K, Yu Y, Yu XF. Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G. J Virol 2004; 78:2072-81; PMID:14747572; http://dx.doi.org/10.1128/ JVI.78.4.2072-2081.2004
    • (2004) J Virol , vol.78 , pp. 2072-2081
    • Liu, B.1    Yu, X.2    Luo, K.3    Yu, Y.4    Yu, X.F.5
  • 9
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function
    • ; PMID:15781449
    • Kobayashi M, Takaori-Kondo A, Miyauchi Y, Iwai K, Uchiyama T. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. J Biol Chem 2005; 280:18573-8; PMID:15781449; http://dx.doi.org/ 10.1074/jbc.C500082200
    • (2005) J Biol Chem , vol.280 , pp. 18573-18578
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3    Iwai, K.4    Uchiyama, T.5
  • 10
    • 67649888155 scopus 로고    scopus 로고
    • Natural variation in Vif: Differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
    • PMID:16201018
    • Simon V, Zennou V, Murray D, Huang Y, Ho DD, Bieniasz PD. Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification. PLoS Pathogens 2005; 1:e6; PMID:16201018; http://dx.doi.org/10.1371/journal. ppat.0010006
    • (2005) Plos Pathogens , pp. 1
    • Simon, V.1    Zennou, V.2    Murray, D.3    Huang, Y.4    Ho, D.D.5    Bieniasz, P.D.6
  • 12
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • PMID:15574593
    • Yu Y, Xiao Z, Ehrlich ES, Yu X, Yu XF. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev 2004; 18:2867-72;PMID:15574593; http://dx.doi.org/10.1101/ gad.1250204
    • (2004) Genes Dev , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 13
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • PMID:15574592
    • Mehle A, Goncalves J, Santa-Marta M, McPike M, Gabuzda D. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev 2004; 18:2861-6; PMID:15574592; http://dx.doi.org/ 10.1101/gad.1249904
    • (2004) Genes Dev , vol.18 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 14
    • 0027447213 scopus 로고
    • Cell-dependent requirement of human immunodeficiency virus type 1 Vif protein for maturation of virus particles
    • PMID:8437236
    • Sakai H, Shibata R, Sakuragi J, Sakuragi S, Kawamura M, Adachi A. Cell-dependent requirement of human immunodeficiency virus type 1 Vif protein for maturation of virus particles. J Virol 1993; 67:1663-6; PMID:8437236
    • (1993) J Virol , vol.67 , pp. 1663-1666
    • Sakai, H.1    Shibata, R.2    Sakuragi, J.3    Sakuragi, S.4    Kawamura, M.5    Adachi, A.6
  • 15
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-b regulates HIV-1 Vif-mediated evasion of host restriction
    • Zhang W, Du J, Evans SL, Yu Y, Yu XF. T-cell differentiation factor CBF-b regulates HIV-1 Vif-mediated evasion of host restriction. Nature 2012; 481:376-9
    • (2012) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.F.5
  • 16
    • 84894600842 scopus 로고    scopus 로고
    • Evolutionarily conserved requirement for core binding factor b in the assembly of the human immunodeficiency virus/ simian immunodeficiency virus Vif-cullin 5-RING E3 ubiquitin ligase
    • PMID:24390335
    • Han X, Liang W, Hua D, Zhou X, Du J, Evans SL, Gao Q, Wang H, Viqueira R, Wei W, et al. Evolutionarily conserved requirement for core binding factor b in the assembly of the human immunodeficiency virus/ simian immunodeficiency virus Vif-cullin 5-RING E3 ubiquitin ligase. J Virol 2014; 88:3320-8; PMID:24390335; http://dx.doi.org/10.1128/JVI. 03833-13
    • (2014) J Virol , vol.88 , pp. 3320-3328
    • Han, X.1    Liang, W.2    Hua, D.3    Zhou, X.4    Du, J.5    Evans, S.L.6    Gao, Q.7    Wang, H.8    Viqueira, R.9    Wei, W.10
  • 17
    • 84859119983 scopus 로고    scopus 로고
    • Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFbeta and CRL5 E3 ubiquitin ligase components
    • PMID:22479405
    • Zhou X, Evans SL, Han X, Liu Y, Yu XF. Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFbeta and CRL5 E3 ubiquitin ligase components. PloS One 2012; 7:e33495;PMID:22479405; http://dx.doi.org/10.1371/journal. pone.0033495
    • (2012) Plos One , pp. 7
    • Zhou, X.1    Evans, S.L.2    Han, X.3    Liu, Y.4    Yu, X.F.5
  • 18
    • 84896723296 scopus 로고    scopus 로고
    • Dispersed and Conserved Hydrophobic Residues of HIV-1 Vif Are Essential for CBFbeta Recruitment and A3G Suppression
    • Zhou X, Han X, Zhao K, Du J, Evans SL, Wang H, Li P, Zheng W, Rui Y, Kang J, et al. Dispersed and Conserved Hydrophobic Residues of HIV-1 Vif Are Essential for CBFbeta Recruitment and A3G Suppression. J Virol 2014; 88:2555-63;PMID:24352440; http://dx. doi.org/10.1128/JVI.03604-13
    • (2014) J Virol , vol.88 , pp. 2555-2563
    • Zhou, X.1    Han, X.2    Zhao, K.3    Du, J.4    Evans, S.L.5    Wang, H.6    Li, P.7    Zheng, W.8    Rui, Y.9    Kang, J.10
  • 19
    • 84892188402 scopus 로고    scopus 로고
    • Structural basis for hijacking CBF-b and CUL5 E3 ligase complex by HIV-1 Vif
    • PMID:24402281
    • Guo Y, Dong L, Qiu X, Wang Y, Zhang B, Liu H, Yu Y, Zang Y, Yang M, Huang Z. Structural basis for hijacking CBF-b and CUL5 E3 ligase complex by HIV-1 Vif. Nature 2014; 505:229-33; PMID:24402281; http://dx.doi.org/10.1038/nature 12884
    • (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    Yu, Y.7    Zang, Y.8    Yang, M.9    Huang, Z.10
  • 20
    • 84873043568 scopus 로고    scopus 로고
    • Differential requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor b
    • PMID:23175372
    • Du J, Zhao K, Rui Y, Li P, Zhou X, Zhang W, Yu XF. Differential requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor b. J Virol 2013; 87:1906-11;PMID:23175372; http://dx.doi.org/10.1128/JVI.02199-12
    • (2013) J Virol , vol.87 , pp. 1906-1911
    • Du, J.1    Zhao, K.2    Rui, Y.3    Li, P.4    Zhou, X.5    Zhang, W.6    Yu, X.F.7
  • 21
    • 84870002103 scopus 로고    scopus 로고
    • HIV type 1 viral infectivity factor and the RUNX transcription factors interact with core binding factor bon genetically distinct surfaces
    • PMID:22725134
    • Hultquist JF, McDougle RM, Anderson BD, Harris RS. HIV type 1 viral infectivity factor and the RUNX transcription factors interact with core binding factor bon genetically distinct surfaces. AIDS Res Hum Retroviruses 2012; 28:1543-51;PMID:22725134; http://dx. doi.org/10.1089/aid.2012.0142
    • (2012) AIDS Res Hum Retroviruses , vol.28 , pp. 1543-1551
    • Hultquist, J.F.1    McDougle, R.M.2    Erson, B.D.3    Harris, R.S.4
  • 22
    • 84901236370 scopus 로고    scopus 로고
    • ZhangW. Identification of HIV-1 Vif Regions Required for CBF-b Interaction and APOBEC3 Suppression
    • PMID:24810617
    • Wang H, Liu B, Liu X, Li Z, Yu X-F, ZhangW. Identification of HIV-1 Vif Regions Required for CBF-b Interaction and APOBEC3 Suppression. PloS One 2014; 9:e95738;PMID:24810617; http://dx.doi.org/ 10.1371/journal.pone.0095738
    • (2014) Plos One , pp. 9
    • Wang, H.1    Liu, B.2    Liu, X.3    Li, Z.4    Yu, X.-F.5
  • 23
    • 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
    • PMID:16076960
    • Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, Yu XF. 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; 102:11444-9;PMID:16076960; http://dx.doi.org/10.1073/pnas. 0502440102
    • (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    Yu, X.F.7
  • 24
    • 33646866382 scopus 로고    scopus 로고
    • Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif
    • PMID:16530799
    • Xiao Z, Ehrlich E, Yu Y, Luo K, Wang T, Tian C, Yu XF. Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. Virology 2006; 349:290-9; PMID:16530799; http://dx.doi.org/10.1016/j.virol. 2006.02.002
    • (2006) Virology , vol.349 , pp. 290-299
    • Xiao, Z.1    Ehrlich, E.2    Yu, Y.3    Luo, K.4    Wang, T.5    Tian, C.6    Yu, X.F.7
  • 25
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • PMID:16636053
    • Mehle A, Thomas ER, Rajendran KS, Gabuzda D. A zinc-binding region in Vif binds Cul5 and determines cullin selection. J Biol Chem 2006; 281:17259-65;PMID:16636053; http://dx.doi.org/10.1074/jbc. M602413200
    • (2006) J Biol Chem , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 26
    • 33845505955 scopus 로고    scopus 로고
    • Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions
    • PMID:17132731
    • Paul I, Cui J, Maynard EL. Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions. Proc Natl Acad Sci U S A 2006; 103:18475- 80;PMID:17132731; http://dx.doi.org/10.1073/pnas.0604150103
    • (2006) Proc Natl Acad Sci U S A , vol.103
    • Paul, I.1    Cui, J.2    Maynard, E.L.3
  • 27
    • 33845996549 scopus 로고    scopus 로고
    • Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
    • PMID:17135358
    • Xiao Z, Ehrlich E, Luo K, Xiong Y, Yu XF. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J 2007; 21:217-22; PMID:17135358; http:// dx.doi.org/10.1096/fj.06-6773com
    • (2007) FASEB J , vol.21 , pp. 217-222
    • Xiao, Z.1    Ehrlich, E.2    Luo, K.3    Xiong, Y.4    Yu, X.F.5
  • 28
    • 34748882327 scopus 로고    scopus 로고
    • Characterization of a novel Cullin5 binding domain in HIV-1 Vif
    • PMID:17869271
    • Xiao Z, Xiong Y, Zhang W, Tan L, Ehrlich E, Guo D, Yu XF. Characterization of a novel Cullin5 binding domain in HIV-1 Vif. J Mol Biol 2007; 373:541-50;PMID:17869271; http://dx.doi.org/10.1016/j. jmb.2007.07.029
    • (2007) J Mol Biol , vol.373 , pp. 541-550
    • Xiao, Z.1    Xiong, Y.2    Zhang, W.3    Tan, L.4    Ehrlich, E.5    Guo, D.6    Yu, X.F.7
  • 29
    • 84892410245 scopus 로고    scopus 로고
    • HIV-1 Vif N-terminal Motif is required for recruitment of Cul5 to Suppress APOBEC 3
    • PMID:24422669
    • Evans SL, Schon A, Gao Q, Han X, Zhou X, Freire E, Yu XF. HIV-1 Vif N-terminal Motif is required for recruitment of Cul5 to Suppress APOBEC 3. Retrovirology 2014; 11:4; PMID:24422669; http://dx.doi. org/10.1186/1742-4690-11-4
    • (2014) Retrovirology , vol.11 , pp. 4
    • Evans, S.L.1    Schon, A.2    Gao, Q.3    Han, X.4    Zhou, X.5    Freire, E.6    Yu, X.F.7
  • 30
    • 77958040891 scopus 로고    scopus 로고
    • Conformational analysis of a peptide approximating the HCCH motif in HIV-1 Vif
    • 19382167
    • Giri K, Maynard EL. Conformational analysis of a peptide approximating the HCCH motif in HIV-1 Vif. Biopolymers 2009; 92:417-25;19382167; http://dx.doi.org/10.1002/bip.21209
    • (2009) Biopolymers , vol.92 , pp. 417-425
    • Giri, K.1    Maynard, E.L.2
  • 31
    • 69049101321 scopus 로고    scopus 로고
    • Molecular structure and biochemical properties of the HCCH-Zn2C site in HIV-1 Vif
    • PMID:19588889;
    • Giri K, Scott RA, Maynard EL. Molecular structure and biochemical properties of the HCCH-Zn2C site in HIV-1 Vif. Biochemistry 2009; 48:7969-78;PMID:19588889; http://dx.doi.org/10.1021/bi900677w
    • (2009) Biochemistry , vol.48 , pp. 7969-7978
    • Giri, K.1    Scott, R.A.2    Maynard, E.L.3
  • 32
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • PMID:18619467
    • 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 Biol2008; 381:1000-11; PMID:18619467; http://dx.doi. org/10.1016/j.jmb.2008.06.061
    • J Mol Biol2008 , vol.381 , pp. 1000-1011
    • He, Z.1    Zhang, W.2    Chen, G.3    Xu, R.4    Yu, X.F.5
  • 33
    • 60049098639 scopus 로고    scopus 로고
    • Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif
    • PMID:19109396;
    • Pery E, Rajendran KS, Brazier AJ, Gabuzda D. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J Virol 2009; 83:2374-81;PMID:19109396; http://dx.doi.org/ 10.1128/JVI.01898-08
    • (2009) J Virol , vol.83 , pp. 2374-2381
    • Pery, E.1    Rajendran, K.S.2    Brazier, A.J.3    Gabuzda, D.4
  • 34
    • 69249215357 scopus 로고    scopus 로고
    • A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G
    • Chen G, He Z,Wang T, Xu R, Yu XF. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. J Virol 2009; 83:8674-82; PMID:19535450; http://dx.doi.org/10.1128/JVI.00653-09
    • (2009) J Virol , vol.83 , pp. 8674-8682
    • Chen, G.1    He, Z.2    Wang, T.3    Xu, R.4    Yu, X.F.5
  • 35
    • 33644752777 scopus 로고    scopus 로고
    • Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F
    • PMID:16501124
    • Tian C, Yu X, Zhang W, Wang T, Xu R, Yu XF. Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J Virol 2006; 80:3112-5; PMID:16501124; http://dx.doi.org/10.1128/JVI.80.6.3112-3115.2006
    • (2006) J Virol , vol.80 , pp. 3112-3115
    • Tian, C.1    Yu, X.2    Zhang, W.3    Wang, T.4    Xu, R.5    Yu, X.F.6
  • 36
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • PMID:17522216
    • 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; 81:8201-10; PMID:17522216; http://dx.doi.org/10.1128/JVI. 00395-07
    • (2007) J Virol , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 37
    • 50849100134 scopus 로고    scopus 로고
    • Antiretroelement activity of APOBEC3H was lost twice in recent human evolution
    • PMID:18779051
    • OhAinle M, Kerns JA, Li MM, Malik HS, Emerman M. Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host Microbe 2008; 4:249-59, PMID:18779051; http://dx.doi.org/ 10.1016/j.chom.2008.07.005
    • (2008) Cell Host Microbe , vol.4 , pp. 249-259
    • Ohainle, M.1    Kerns, J.A.2    Li, M.M.3    Malik, H.S.4    Emerman, M.5
  • 38
    • 58149374613 scopus 로고    scopus 로고
    • Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H
    • PMID:18945781
    • Harari A, Ooms M, Mulder LC, Simon V. Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H. J virol 2009; 83:295- 303 PMID:18945781; http://dx.doi.org/10.1128/ JVI.01665- 0839.
    • (2009) J Virol , vol.83
    • Harari, A.1    Ooms, M.2    Mulder, L.C.3    Simon, V.4
  • 39
    • 58249114897 scopus 로고    scopus 로고
    • Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV- 1
    • PMID:18827027;
    • Tan L, Sarkis PT, Wang T, Tian C, Yu XF. Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV- 1. FASEB J 2009; 23:279-87; PMID:18827027; http://dx.doi.org/10.1096/fj.07-088781
    • (2009) FASEB J , vol.23 , pp. 279-287
    • Tan, L.1    Sarkis, P.T.2    Wang, T.3    Tian, C.4    Yu, X.F.5
  • 41
    • 84855982190 scopus 로고    scopus 로고
    • The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H
    • PMID:22013041
    • Binka M, Ooms M, Steward M, Simon V. The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H. J Virol 2012; 86:49-59;PMID:22013041; http://dx.doi.org/ 10.1128/JVI.06082-11
    • (2012) J Virol , vol.86 , pp. 49-59
    • Binka, M.1    Ooms, M.2    Steward, M.3    Simon, V.4
  • 42
    • 84874574872 scopus 로고    scopus 로고
    • The resistance of human APOBEC3H to HIV-1 NL4-3 molcular clone is determined by a single amino acid in Vif
    • PMID:23469063
    • Ooms M, Letko M, Binka M, Simon V. The resistance of human APOBEC3H to HIV-1 NL4-3 molcular clone is determined by a single amino acid in Vif. PloS One 2013; 8:e57744; PMID:23469063; http://dx.doi. org/10.1371/journal.pone.0057744
    • (2013) Plos One , pp. 8
    • Ooms, M.1    Letko, M.2    Binka, M.3    Simon, V.4
  • 43
    • 33644764832 scopus 로고    scopus 로고
    • The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest
    • Sakai K, Dimas J, Lenardo MJ. The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest. Proc Natl Acad Sci 2006; 103:3369-74; http://dx.doi.org/10.1073/ pnas.0509417103
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 3369-3374
    • Sakai, K.1    Dimas, J.2    Lenardo, M.J.3
  • 44
    • 33847076286 scopus 로고    scopus 로고
    • The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells
    • PMID:17056089
    • Wang J, Shackelford JM, Casella CR, Shivers DK, Rapaport EL, Liu B, Yu XF, Finkel TH. The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells. Virology 2007; 359:243-52; PMID:17056089; http://dx.doi.org/10.1016/j.virol.2006.09.026
    • (2007) Virology , vol.359 , pp. 243-252
    • Wang, J.1    Shackelford, J.M.2    Casella, C.R.3    Shivers, D.K.4    Rapaport, E.L.5    Liu, B.6    Yu, X.F.7    Finkel, T.H.8
  • 46
    • 75449093805 scopus 로고    scopus 로고
    • A single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivity
    • PMID:19939923
    • Zhen A, Wang T, Zhao K, Xiong Y, Yu XF. A single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivity. J Virol 2010; 84:1902-11; PMID:19939923; http://dx.doi.org/ 10.1128/JVI.01509-09
    • (2010) J Virol , vol.84 , pp. 1902-1911
    • Zhen, A.1    Wang, T.2    Zhao, K.3    Xiong, Y.4    Yu, X.F.5
  • 47
    • 84864456753 scopus 로고    scopus 로고
    • Reduced APOBEC3H variant anti-viral activities are associated with altered RNA binding activities
    • PMID:22859935
    • Zhen A, Du J, Zhou X, Xiong Y, Yu XF. Reduced APOBEC3H variant anti-viral activities are associated with altered RNA binding activities. PloS One 2012; 7: e38771; PMID:22859935; http://dx.doi.org/10.1371/ journal.pone.0038771
    • (2012) Plos One , pp. 7
    • Zhen, A.1    Du, J.2    Zhou, X.3    Xiong, Y.4    Yu, X.F.5
  • 51
    • 84857865923 scopus 로고    scopus 로고
    • BinkaM, Larue RS, Simon V, Harris RS. Vif proteins of human and simian immunodeficiency viruses require cellular CBFbeta to degrade APOBEC3 restriction factors
    • PMID:22205746
    • Hultquist JF, BinkaM, Larue RS, Simon V, Harris RS. Vif proteins of human and simian immunodeficiency viruses require cellular CBFbeta to degrade APOBEC3 restriction factors. J Virol 2012; 86:2874-7; PMID:22205746; http:// dx.doi.org/10.1128/JVI.06950-11
    • (2012) J Virol , vol.86 , pp. 2874-2877
    • Hultquist, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.