메뉴 건너뛰기




Volumn 333, Issue 2, 2005, Pages 374-386

Complementary function of the two catalytic domains of APOBEC3G

Author keywords

APOBEC3G; Deamination; Encapsidation; HIV 1; Vif

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CYTIDINE DEAMINASE; MUTANT PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 13844270834     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.01.011     Document Type: Article
Times cited : (275)

References (48)
  • 1
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • M.A. Accola, B. Strack, and H.G. Gottlinger Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain J. Virol. 74 12 2000 5395 5402
    • (2000) J. Virol. , vol.74 , Issue.12 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 2
    • 4544232464 scopus 로고    scopus 로고
    • APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
    • T.M. Alce, and W. Popik APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein J. Biol. Chem. 279 33 2004 34083 34086
    • (2004) J. Biol. Chem. , vol.279 , Issue.33 , pp. 34083-34086
    • Alce, T.M.1    Popik, W.2
  • 3
    • 0025266663 scopus 로고
    • Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus
    • A. Aldovini, and R.A. Young Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus J. Virol. 64 5 1990 1920 1926
    • (1990) J. Virol. , vol.64 , Issue.5 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 4
    • 0025960804 scopus 로고
    • Specificity of retroviral RNA packaging
    • R. Aronoff, and M. Linial Specificity of retroviral RNA packaging J. Virol. 65 1 1991 71 80
    • (1991) J. Virol. , vol.65 , Issue.1 , pp. 71-80
    • Aronoff, R.1    Linial, M.2
  • 6
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2.3 a crystal structure of an enzyme: Transition-state analog complex
    • L. Betts, S. Xiang, S.A. Short, R. Wolfenden, and C.W. Carter Jr. Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex J. Mol. Biol. 235 2 1994 635 656
    • (1994) J. Mol. Biol. , vol.235 , Issue.2 , pp. 635-656
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter Jr., C.W.5
  • 8
    • 1642367210 scopus 로고    scopus 로고
    • A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor
    • H.P. Bogerd, B.P. Doehle, H.L. Wiegand, and B.R. Cullen A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor Proc. Natl. Acad. Sci. U.S.A. 101 11 2004 3770 3774
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.11 , pp. 3770-3774
    • Bogerd, H.P.1    Doehle, B.P.2    Wiegand, H.L.3    Cullen, B.R.4
  • 10
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • R.I. Connor, B.K. Chen, S. Choe, and N.R. Landau Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes Virology 206 1995 936 944
    • (1995) Virology , vol.206 , pp. 936-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 11
    • 0034887093 scopus 로고    scopus 로고
    • Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors
    • D. Derse, S.A. Hill, P.A. Lloyd, H. Chung, and B.A. Morse Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors J. Virol. 75 18 2001 8461 8468
    • (2001) J. Virol. , vol.75 , Issue.18 , pp. 8461-8468
    • Derse, D.1    Hill, S.A.2    Lloyd, P.A.3    Chung, H.4    Morse, B.A.5
  • 13
  • 15
    • 0036863733 scopus 로고    scopus 로고
    • RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators
    • R.S. Harris, S.K. Petersen-Mahrt, and M.S. Neuberger RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators Mol. Cell 10 5 2002 1247 1253
    • (2002) Mol. Cell , vol.10 , Issue.5 , pp. 1247-1253
    • Harris, R.S.1    Petersen-Mahrt, S.K.2    Neuberger, M.S.3
  • 18
    • 0028085932 scopus 로고
    • Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene
    • P.P. Lau, H.J. Zhu, A. Baldini, C. Charnsangavej, and L. Chan Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene Proc. Natl. Acad. Sci. U.S.A. 91 18 1994 8522 8526
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , Issue.18 , pp. 8522-8526
    • Lau, P.P.1    Zhu, H.J.2    Baldini, A.3    Charnsangavej, C.4    Chan, L.5
  • 19
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • D. Lecossier, F. Bouchonnet, F. Clavel, and A.J. Hance Hypermutation of HIV-1 DNA in the absence of the Vif protein Science 300 5622 2003 1112
    • (2003) Science , vol.300 , Issue.5622 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 20
    • 7444268898 scopus 로고    scopus 로고
    • Functional domains of APOBEC3G required for antiviral activity
    • J. Li, M.J. Potash, and D.J. Volsky Functional domains of APOBEC3G required for antiviral activity J. Cell. Biochem. 92 3 2004 560 5672
    • (2004) J. Cell. Biochem. , vol.92 , Issue.3 , pp. 560-5672
    • Li, J.1    Potash, M.J.2    Volsky, D.J.3
  • 21
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • M.T. Liddament, W.L. Brown, A.J. Schumacher, and R.S. Harris APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo Curr. Biol. 14 15 2004 1385 1391
    • (2004) Curr. Biol. , vol.14 , Issue.15 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 22
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
    • K. Luo, B. Liu, Z. Xiao, Y. Yu, X. Yu, R. Gorelick, and X.F. Yu Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging J. Virol. 78 21 2004 11841 11852
    • (2004) J. Virol. , vol.78 , Issue.21 , pp. 11841-11852
    • Luo, K.1    Liu, B.2    Xiao, Z.3    Yu, Y.4    Yu, X.5    Gorelick, R.6    Yu, X.F.7
  • 23
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • B. Mangeat, P. Turelli, G. Caron, M. Friedli, L. Perrin, and D. Trono Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts Nature 424 6944 2003 99 103
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 24
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • B. Mangeat, P. Turelli, S. Liao, and D. Trono A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action J. Biol. Chem. 279 15 2004 14481 14483
    • (2004) J. Biol. Chem. , vol.279 , Issue.15 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 26
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • A. Mehle, B. Strack, P. Ancuta, C. Zhang, M. McPike, and D. Gabuzda Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway J. Biol. Chem. 279 9 2004 7792 7798
    • (2004) J. Biol. Chem. , vol.279 , Issue.9 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 27
    • 0034268780 scopus 로고    scopus 로고
    • Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme
    • M. Muramatsu, K. Kinoshita, S. Fagarasan, S. Yamada, Y. Shinkai, and T. Honjo Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme Cell 102 5 2000 553 563
    • (2000) Cell , vol.102 , Issue.5 , pp. 553-563
    • Muramatsu, M.1    Kinoshita, K.2    Fagarasan, S.3    Yamada, S.4    Shinkai, Y.5    Honjo, T.6
  • 28
    • 0034662773 scopus 로고    scopus 로고
    • Isolation, tissue distribution, and chromosomal localization of the human activation-induced cytidine deaminase (AID) gene
    • T. Muto, M. Muramatsu, M. Taniwaki, K. Kinoshita, and T. Honjo Isolation, tissue distribution, and chromosomal localization of the human activation-induced cytidine deaminase (AID) gene Genomics 68 1 2000 85 88
    • (2000) Genomics , vol.68 , Issue.1 , pp. 85-88
    • Muto, T.1    Muramatsu, M.2    Taniwaki, M.3    Kinoshita, K.4    Honjo, T.5
  • 29
    • 0029056474 scopus 로고
    • Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
    • N. Navaratnam, S. Bhattacharya, T. Fujino, D. Patel, A.L. Jarmuz, and J. Scott Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site Cell 81 2 1995 187 195
    • (1995) Cell , vol.81 , Issue.2 , pp. 187-195
    • Navaratnam, N.1    Bhattacharya, S.2    Fujino, T.3    Patel, D.4    Jarmuz, A.L.5    Scott, J.6
  • 31
    • 5344222683 scopus 로고    scopus 로고
    • Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor
    • A. Schafer, H.P. Bogerd, and B.R. Cullen Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor Virology 328 2 2004 163 168
    • (2004) Virology , vol.328 , Issue.2 , pp. 163-168
    • Schafer, A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 32
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • B. Schrofelbauer, D. Chen, and N.R. Landau A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif) Proc. Natl. Acad. Sci. U.S.A. 101 11 2004 3927 3932
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.11 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 33
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • A.M. Sheehy, N.C. Gaddis, J.D. Choi, and M.H. Malim Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein Nature 418 6898 2002 646 650
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 34
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • A.M. Sheehy, N.C. Gaddis, and M.H. Malim The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif Nat. Med. 9 11 2003 1404 1407
    • (2003) Nat. Med. , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 35
    • 0242497878 scopus 로고    scopus 로고
    • The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity
    • K. Shindo, A. Takaori-Kondo, M. Kobayashi, A. Abudu, K. Fukunaga, and T. Uchiyama The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity J. Biol. Chem. 278 45 2003 44412 44416
    • (2003) J. Biol. Chem. , vol.278 , Issue.45 , pp. 44412-44416
    • Shindo, K.1    Takaori-Kondo, A.2    Kobayashi, M.3    Abudu, A.4    Fukunaga, K.5    Uchiyama, T.6
  • 37
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • K. Stopak, C. de Noronha, W. Yonemoto, and W.C. Greene HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability Mol. Cell 12 3 2003 591 601
    • (2003) Mol. Cell , vol.12 , Issue.3 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 38
    • 4143124683 scopus 로고    scopus 로고
    • Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs
    • E.S. Svarovskaia, H. Xu, J.L. Mbisa, R. Barr, R.J. Gorelick, A. Ono, E.O. Freed, W.S. Hu, and V.K. Pathak Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs J. Biol. Chem. 279 34 2004 35822 35828
    • (2004) J. Biol. Chem. , vol.279 , Issue.34 , pp. 35822-35828
    • Svarovskaia, E.S.1    Xu, H.2    Mbisa, J.L.3    Barr, R.4    Gorelick, R.J.5    Ono, A.6    Freed, E.O.7    Hu, W.S.8    Pathak, V.K.9
  • 39
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by APOBEC3G
    • P. Turelli, B. Mangeat, S. Jost, S. Vianin, and D. Trono Inhibition of hepatitis B virus replication by APOBEC3G Science 303 5665 2004 1829
    • (2004) Science , vol.303 , Issue.5665 , pp. 1829
    • Turelli, P.1    Mangeat, B.2    Jost, S.3    Vianin, S.4    Trono, D.5
  • 40
    • 0345270035 scopus 로고    scopus 로고
    • Messenger RNA editing in mammals: New members of the APOBEC family seeking roles in the family business
    • J.E. Wedekind, G.S. Dance, M.P. Sowden, and H.C. Smith Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business Trends Genet. 19 4 2003 207 216
    • (2003) Trends Genet. , vol.19 , Issue.4 , pp. 207-216
    • Wedekind, J.E.1    Dance, G.S.2    Sowden, M.P.3    Smith, H.C.4
  • 41
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • H.L. Wiegand, B.P. Doehle, H.P. Bogerd, and B.R. Cullen A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins EMBO J. 23 12 2004 2451 2458
    • (2004) EMBO J. , vol.23 , Issue.12 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 42
    • 1842732157 scopus 로고    scopus 로고
    • A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion
    • H. Xu, E.S. Svarovskaia, R. Barr, Y. Zhang, M.A. Khan, K. Strebel, and V.K. Pathak A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion Proc. Natl. Acad. Sci. U.S.A. 101 15 2004 5652 5657
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.15 , pp. 5652-5657
    • Xu, H.1    Svarovskaia, E.S.2    Barr, R.3    Zhang, Y.4    Khan, M.A.5    Strebel, K.6    Pathak, V.K.7
  • 43
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • X. Yu, Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X.F. Yu Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex Science 302 5647 2003 1056 1060
    • (2003) Science , vol.302 , Issue.5647 , 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
  • 44
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • Q. Yu, D. Chen, R. Konig, R. Mariani, D. Unutmaz, and N.R. Landau APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication J. Biol. Chem. 279 51 2004 53379 53386
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 53379-53386
    • Yu, Q.1    Chen, D.2    Konig, R.3    Mariani, R.4    Unutmaz, D.5    Landau, N.R.6
  • 46
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • V. Zennou, D. Perez-Caballero, H. Gottlinger, and P.D. Bieniasz APOBEC3G incorporation into human immunodeficiency virus type 1 particles J. Virol. 78 21 2004 12058 12061
    • (2004) J. Virol. , vol.78 , Issue.21 , pp. 12058-12061
    • Zennou, V.1    Perez-Caballero, D.2    Gottlinger, H.3    Bieniasz, P.D.4
  • 47
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • H. Zhang, B. Yang, R.J. Pomerantz, C. Zhang, S.C. Arunachalam, and L. Gao The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA Nature 424 6944 2003 94 98
    • (2003) Nature , vol.424 , Issue.6944 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 48
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Y.H. Zheng, D. Irwin, T. Kurosu, K. Tokunaga, T. Sata, and B.M. Peterlin Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication J. Virol. 78 11 2004 6073 6076
    • (2004) J. Virol. , vol.78 , Issue.11 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.