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Volumn 12, Issue 5, 2006, Pages

APOBEC deaminases as cellular antiviral factors: A novel natural host defense mechanism

Author keywords

APOBECs; Human immunodeficiency virus (HIV); Vif antiviral natural defense

Indexed keywords

ANTIVIRUS AGENT; APOLIPOPROTEIN B; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 1; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3A; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3B; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3C; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3D; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3E; 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; APOLIPOPROTEIN B100; APOLIPOPROTEIN B48; CULLIN; CYTIDINE DEAMINASE; CYTOSINE; ELONGIN B; ELONGIN C; PROTEASOME INHIBITOR; RNA DIRECTED DNA POLYMERASE INHIBITOR; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; URACIL; URACIL DNA GLYCOSYLTRANSFERASE; VIF PROTEIN; VIRUS DNA; VIRUS RNA;

EID: 33646468134     PISSN: 12341010     EISSN: 16433750     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (20)

References (78)
  • 1
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello SG, Harris RS, Neuberger MS: The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr Biol, 2003; 13: 2009-13
    • (2003) Curr Biol , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 2
    • 1642334586 scopus 로고    scopus 로고
    • Cloning and expression of the AID gene in the channel catfish
    • Saunders HL, Magor BG: Cloning and expression of the AID gene in the channel catfish. Dev Comp Immunol, 2004; 28: 657-63
    • (2004) Dev Comp Immunol , vol.28 , pp. 657-663
    • Saunders, H.L.1    Magor, B.G.2
  • 3
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris RS, Liddament MT: Retroviral restriction by APOBEC proteins. Nat Rev Immunol, 2004; 4: 868-77
    • (2004) Nat Rev Immunol , vol.4 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 4
    • 0036200070 scopus 로고    scopus 로고
    • An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22
    • Jarmuz A, Chester A, Bayliss J et al: An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics, 2002; 79: 285-96
    • (2002) Genomics , vol.79 , pp. 285-296
    • Jarmuz, A.1    Chester, A.2    Bayliss, J.3
  • 5
    • 2942613670 scopus 로고    scopus 로고
    • AID: How does it aid antibody diversity?
    • Honjo T, Muramatsu M, Fagarasan S: AID: how does it aid antibody diversity? Immunity, 2004; 20: 659-68
    • (2004) Immunity , vol.20 , pp. 659-668
    • Honjo, T.1    Muramatsu, M.2    Fagarasan, S.3
  • 7
    • 0035658430 scopus 로고    scopus 로고
    • ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing
    • Anant S, Mukhopadhyay D, Sankaranand V et al: ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing. Am J Physiol Cell Physiol, 2001; 281: C1904-16
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Anant, S.1    Mukhopadhyay, D.2    Sankaranand, V.3
  • 8
    • 0033526865 scopus 로고    scopus 로고
    • APOBEC-2, a cardiac- and skeletal muscle-specific member of the cytidine deaminase supergene family
    • Liao W, Hong SH, Chan BH et al: APOBEC-2, a cardiac- and skeletal muscle-specific member of the cytidine deaminase supergene family. Biochem Biophys Res Commun, 1999; 260: 398-404
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 398-404
    • Liao, W.1    Hong, S.H.2    Chan, B.H.3
  • 9
    • 23344440307 scopus 로고    scopus 로고
    • Mice deficient in APOBEC2 and APOBEC3
    • Mikl MC, Watt IN, Lu M et al: Mice deficient in APOBEC2 and APOBEC3. Mol Cell Biol, 2005; 25: 7270-27
    • (2005) Mol Cell Biol , vol.25 , pp. 7270-7327
    • Mikl, M.C.1    Watt, I.N.2    Lu, M.3
  • 10
    • 0035824543 scopus 로고    scopus 로고
    • A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing
    • Lau PP, Villanueva H, Kobayashi K et al: A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing. J Biol Chem, 2001; 276: 46445-52
    • (2001) J Biol Chem , vol.276 , pp. 46445-46452
    • Lau, P.P.1    Villanueva, H.2    Kobayashi, K.3
  • 11
    • 0029004350 scopus 로고
    • Apobec-1, the catalytic subunit of the mammalian apolipoprotein B mRNA editing enzyme, is a novel RNA-binding protein
    • Anant S, MacGinnitie AJ, Davidson NO: Apobec-1, the catalytic subunit of the mammalian apolipoprotein B mRNA editing enzyme, is a novel RNA-binding protein. J Biol Chem, 1995; 270: 14762-67
    • (1995) J Biol Chem , vol.270 , pp. 14762-14767
    • Anant, S.1    MacGinnitie, A.J.2    Davidson, N.O.3
  • 12
    • 0034725660 scopus 로고    scopus 로고
    • Induction of cytidine to uridine editing on cytoplasmic apolipoprotein B mRNA by overexpressing APOBEC-1
    • Yang Y, Sowden MP, Smith HC: Induction of cytidine to uridine editing on cytoplasmic apolipoprotein B mRNA by overexpressing APOBEC-1. J Biol Chem, 2000; 275: 22663-69
    • (2000) J Biol Chem , vol.275 , pp. 22663-22669
    • Yang, Y.1    Sowden, M.P.2    Smith, H.C.3
  • 13
    • 13844309367 scopus 로고    scopus 로고
    • Editing at the crossroad of innate and adaptive immunity
    • Turelli P, Trono D: Editing at the crossroad of innate and adaptive immunity. Science, 2005; 307: 1061-65
    • (2005) Science , vol.307 , pp. 1061-1065
    • Turelli, P.1    Trono, D.2
  • 14
    • 1542563409 scopus 로고    scopus 로고
    • Initial sequencing and comparative analysis of the mouse genome
    • Waterston RH, Lindblad-Toh K, Birney E et al: Initial sequencing and comparative analysis of the mouse genome. Nature, 2002; 420: 520-62
    • (2002) Nature , vol.420 , pp. 520-562
    • Waterston, R.H.1    Lindblad-Toh, K.2    Birney, E.3
  • 15
    • 25444527785 scopus 로고    scopus 로고
    • APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis
    • Rogozin IB, Basu MK, Jordan IK et al: APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis. Cell Cycle, 2005; 4: 1281-85
    • (2005) Cell Cycle , vol.4 , pp. 1281-1285
    • Rogozin, I.B.1    Basu, M.K.2    Jordan, I.K.3
  • 16
    • 0022678249 scopus 로고
    • Identification of HTLV-III/LAV sor gene product and detection of antibodies in human sera
    • Kan NC, Franchini G, Wong-Staal F et al: Identification of HTLV-III/LAV sor gene product and detection of antibodies in human sera. Science, 1986; 231: 1553-55
    • (1986) Science , vol.231 , pp. 1553-1555
    • Kan, N.C.1    Franchini, G.2    Wong-Staal, F.3
  • 17
    • 0022680624 scopus 로고
    • A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses
    • Lee TH, Coligan JE, Allan JS et al: A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses. Science, 1986; 231: 1546-49
    • (1986) Science , vol.231 , pp. 1546-1549
    • Lee, T.H.1    Coligan, J.E.2    Allan, J.S.3
  • 18
    • 0022383333 scopus 로고
    • Transcription of novel open reading frames of AIDS retrovirus during infection of lymphocytes
    • Rabson AB, Daugherty DF, Venkatesan S et al: Transcription of novel open reading frames of AIDS retrovirus during infection of lymphocytes. Science, 1985; 229: 1388-90
    • (1985) Science , vol.229 , pp. 1388-1390
    • Rabson, A.B.1    Daugherty, D.F.2    Venkatesan, S.3
  • 19
    • 0022676327 scopus 로고
    • Replicative and cytopathic potential of HTLV-III/LAV with sor gene deletions
    • Sodroski J, Goh WC, Rosen C et al: Replicative and cytopathic potential of HTLV-III/LAV with sor gene deletions. Science, 1986; 231: 1549-53
    • (1986) Science , vol.231 , pp. 1549-1553
    • Sodroski, J.1    Goh, W.C.2    Rosen, C.3
  • 20
    • 0023191658 scopus 로고
    • The sor gene of HIV-1 is required for efficient virus transmission in vitro
    • Fisher AG, Ensoli B, Ivanoff L et al: The sor gene of HIV-1 is required for efficient virus transmission in vitro. Science, 1987; 237: 888-93
    • (1987) Science , vol.237 , pp. 888-893
    • Fisher, A.G.1    Ensoli, B.2    Ivanoff, L.3
  • 21
    • 0026544438 scopus 로고
    • Conservation of amino-acid sequence motifs in lentivirus Vif proteins
    • Oberste MS, Gonda MA: Conservation of amino-acid sequence motifs in lentivirus Vif proteins. Virus Genes, 1992; 6: 95-102
    • (1992) Virus Genes , vol.6 , pp. 95-102
    • Oberste, M.S.1    Gonda, M.A.2
  • 22
    • 0023228920 scopus 로고
    • Sequence of simian immunodeficiency virus from macaque and its relationship to other human and simian retroviruses
    • Chakrabarti L, Guyader M, Alizon M et al: Sequence of simian immunodeficiency virus from macaque and its relationship to other human and simian retroviruses. Nature, 1987; 328: 543-47
    • (1987) Nature , vol.328 , pp. 543-547
    • Chakrabarti, L.1    Guyader, M.2    Alizon, M.3
  • 23
    • 0023657622 scopus 로고
    • Genome organization and transactivation of the human immunodeficiency virus type 2
    • Guyader M, Emerman M, Sonigo P et al: Genome organization and transactivation of the human immunodeficiency virus type 2. Nature, 1987; 326: 662-69
    • (1987) Nature , vol.326 , pp. 662-669
    • Guyader, M.1    Emerman, M.2    Sonigo, P.3
  • 24
    • 0026070511 scopus 로고
    • A specific inhibitor of cysteine proteases impairs a Vif-dependent modification of human immunodeficiency virus type 1 Env protein
    • Guy B, Geist M, Dott K et al: A specific inhibitor of cysteine proteases impairs a Vif-dependent modification of human immunodeficiency virus type 1 Env protein. J Virol, 1991; 65: 1325-31
    • (1991) J Virol , vol.65 , pp. 1325-1331
    • Guy, B.1    Geist, M.2    Dott, K.3
  • 25
    • 0025036273 scopus 로고
    • Nucleotide sequence and transcriptional analysis of molecular clones of CAEV which generate infectious virus
    • Saltarelli M, Querat G, Konings DA et al: Nucleotide sequence and transcriptional analysis of molecular clones of CAEV which generate infectious virus. Virology, 1990; 179: 347-64
    • (1990) Virology , vol.179 , pp. 347-364
    • Saltarelli, M.1    Querat, G.2    Konings, D.A.3
  • 26
    • 0022359843 scopus 로고
    • Nucleotide sequence of the visna lentivirus: Relationship to the AIDS virus
    • Sonigo P, Alizon M, Staskus K et al: Nucleotide sequence of the visna lentivirus: relationship to the AIDS virus. Cell, 1985; 42: 369-82
    • (1985) Cell , vol.42 , pp. 369-382
    • Sonigo, P.1    Alizon, M.2    Staskus, K.3
  • 27
    • 0000523078 scopus 로고
    • Nucleotide sequence and genomic organization of feline immunodeficiency virus
    • USA
    • Talbott RL, Sparger EE, Lovelace KM et al: Nucleotide sequence and genomic organization of feline immunodeficiency virus. Proc Natl Acad Sci USA, 1989; 86: 5743-47
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 5743-5747
    • Talbott, R.L.1    Sparger, E.E.2    Lovelace, K.M.3
  • 28
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • Madani N, Kabat D: An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. J Virol, 1998; 72: 10251-55
    • (1998) J Virol , vol.72 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 29
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • Simon JH, Gaddis NC, Fouchier RA, Malim MH: Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nat Med, 1998; 4: 1397-400
    • (1998) Nat Med , vol.4 , pp. 1397-1400
    • Simon, J.H.1    Gaddis, N.C.2    Fouchier, R.A.3    Malim, M.H.4
  • 30
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • 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
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 31
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
    • von Schwedler U, Song J, Aiken C, Trono D: Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells. J Virol, 1993; 67: 4945-55
    • (1993) J Virol , vol.67 , pp. 4945-4955
    • Von Schwedler, U.1    Song, J.2    Aiken, C.3    Trono, D.4
  • 32
    • 0028926644 scopus 로고
    • Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps
    • Courcoul M, Patience C, Rey F et al: Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps. J Virol, 1995; 69: 2068-74
    • (1995) J Virol , vol.69 , pp. 2068-2074
    • Courcoul, M.1    Patience, C.2    Rey, F.3
  • 33
    • 0029861076 scopus 로고    scopus 로고
    • Role of Vif in human immunodeficiency virus type 1 reverse transcription
    • Goncalves J, Korin Y, Zack J, Gabuzda D: Role of Vif in human immunodeficiency virus type 1 reverse transcription. J Virol, 1996; 70: 8701-9
    • (1996) J Virol , vol.70 , pp. 8701-8709
    • Goncalves, J.1    Korin, Y.2    Zack, J.3    Gabuzda, D.4
  • 34
    • 0029956256 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
    • Simon JH, Malim MH: The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. J Virol, 1996; 70: 5297-305
    • (1996) J Virol , vol.70 , pp. 5297-5305
    • Simon, J.H.1    Malim, M.H.2
  • 35
    • 0033798414 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription
    • Dettenhofer M, Cen S, Carlson BA et al: Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription. J Virol, 2000; 74: 8938-45
    • (2000) J Virol , vol.74 , pp. 8938-8945
    • Dettenhofer, M.1    Cen, S.2    Carlson, B.A.3
  • 36
    • 0026649561 scopus 로고
    • Role of vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes
    • Gabuzda DH, Lawrence K, Langhoff E et al: Role of vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes. J Virol, 1992; 66: 6489-95
    • (1992) J Virol , vol.66 , pp. 6489-6495
    • Gabuzda, D.H.1    Lawrence, K.2    Langhoff, E.3
  • 37
    • 0027183349 scopus 로고
    • Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1
    • Sova P, Volsky DJ: Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1. J Virol, 1993; 67: 6322-26
    • (1993) J Virol , vol.67 , pp. 6322-6326
    • Sova, P.1    Volsky, D.J.2
  • 38
    • 0031044783 scopus 로고    scopus 로고
    • Analysis of vif-defective human immunodeficiency virus type 1 (HIV-1) virions synthesized in 'non-permissive' T lymphoid cells stably infected with selectable HIV-1
    • Ochsenbauer C, Wilk T, Bosch V: Analysis of vif-defective human immunodeficiency virus type 1 (HIV-1) virions synthesized in 'non-permissive' T lymphoid cells stably infected with selectable HIV-1. J Gen Virol, 1997; 78: 627-35
    • (1997) J Gen Virol , vol.78 , pp. 627-635
    • Ochsenbauer, C.1    Wilk, T.2    Bosch, V.3
  • 39
    • 0037630009 scopus 로고    scopus 로고
    • Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions
    • Gaddis NC, Chertova E, Sheehy AM et al: Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. J Virol, 2003; 77: 5810-20
    • (2003) J Virol , vol.77 , pp. 5810-5820
    • Gaddis, N.C.1    Chertova, E.2    Sheehy, A.M.3
  • 40
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Epub 2003 May 28
    • Mangeat B, Turelli P, Caron G et al: Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature, 2003;424: 99-103. Epub 2003 May 28
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3
  • 41
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H, Yang B, Pomerantz RJ et al: The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature, 2003; 424: 94-98
    • (2003) Nature , vol.424 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3
  • 42
    • 0038681901 scopus 로고    scopus 로고
    • DNA deamination mediates innate immunity to retroviral infection
    • Harris RS, Bishop KN, Sheehy AM et al: DNA deamination mediates innate immunity to retroviral infection. Cell, 2003; 113: 803-9
    • (2003) Cell , vol.113 , pp. 803-809
    • Harris, R.S.1    Bishop, K.N.2    Sheehy, A.M.3
  • 43
    • 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
  • 44
    • 1542328859 scopus 로고    scopus 로고
    • Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: Correlation with mutation spectra in vivo
    • Beale RC, Petersen-Mahrt SK, Watt IN et al: Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo. J Mol Biol, 2004; 337: 585-96
    • (2004) J Mol Biol , vol.337 , pp. 585-596
    • Beale, R.C.1    Petersen-Mahrt, S.K.2    Watt, I.N.3
  • 45
    • 2342633240 scopus 로고    scopus 로고
    • Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome
    • Yu Q, Konig R, Pillai S et al: Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome. Nat Struct Mol Biol, 2004; 11: 435-42
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 435-442
    • Yu, Q.1    Konig, R.2    Pillai, S.3
  • 46
    • 0037424364 scopus 로고    scopus 로고
    • Incorporation of uracil into minus strand DNA affects the specificity of plus strand synthesis initiation during lentiviral reverse transcription
    • Klarmann GJ, Chen X, North TW, Preston BD: Incorporation of uracil into minus strand DNA affects the specificity of plus strand synthesis initiation during lentiviral reverse transcription. J Biol Chem, 2003; 278: 7902-9
    • (2003) J Biol Chem , vol.278 , pp. 7902-7909
    • Klarmann, G.J.1    Chen, X.2    North, T.W.3    Preston, B.D.4
  • 47
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak K, de Noronha C, Yonemoto W, Greene WC: HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell, 2003; 12: 591-601
    • (2003) Mol Cell , vol.12 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 48
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity
    • Kao S, Khan MA, Miyagi E et al: The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity. J Virol, 2003; 77: 11398-407
    • (2003) J Virol , vol.77 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3
  • 49
    • 0038107587 scopus 로고    scopus 로고
    • Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif
    • Mariani R, Chen D, Schrofelbauer B et al: Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell, 2003; 114: 21-31
    • (2003) Cell , vol.114 , pp. 21-31
    • Mariani, R.1    Chen, D.2    Schrofelbauer, B.3
  • 50
    • 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: 1398-403
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 51
    • 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: 1404-7
    • (2003) Nat Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 52
    • 0842347676 scopus 로고    scopus 로고
    • Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G
    • Liu B, Yu X, Luo K et al: Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G. J Virol, 2004; 78: 2072-81
    • (2004) J Virol , vol.78 , pp. 2072-2081
    • Liu, B.1    Yu, X.2    Luo, K.3
  • 53
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X, Yu Y, Liu B et al: Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science, 2003; 302: 1056-60
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3
  • 54
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P et al: Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem, 2004; 279: 7792-98
    • (2004) J Biol Chem , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3
  • 55
    • 14844288923 scopus 로고    scopus 로고
    • Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: Correlating function and subcellular localization
    • Wichroski MJ, Ichiyama K, Rana TM: Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: correlating function and subcellular localization. J Biol Chem, 2005; 280: 8387-96
    • (2005) J Biol Chem , vol.280 , pp. 8387-8396
    • Wichroski, M.J.1    Ichiyama, K.2    Rana, T.M.3
  • 57
    • 33646483670 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-cullin5-elonginB-elonginC complex is essential for Vif function
    • Kobayashi M, Takaori-Kondo A, Miyauchi Y et al: Ubiquitination of APOBEC3G by an HIV-1 Vif-cullin5-elonginB-elonginC complex is essential for Vif function. J Biol Chem, 2005; 21: 21
    • (2005) J Biol Chem , vol.21 , pp. 21
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3
  • 58
    • 4143092717 scopus 로고    scopus 로고
    • Cytidine deamination of retroviral DNA by diverse APOBEC proteins
    • Bishop KN, Holmes RK, Sheehy AM et al: Cytidine deamination of retroviral DNA by diverse APOBEC proteins. Curr Biol, 2004; 14: 1392-96
    • (2004) Curr Biol , vol.14 , pp. 1392-1396
    • Bishop, K.N.1    Holmes, R.K.2    Sheehy, A.M.3
  • 59
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand HL, Doehle BP, Bogerd HP, Cullen BR: A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. Embo J, 2004; 23: 2451-58
    • (2004) Embo J , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 60
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng YH, Irwin D, Kurosu T et al: Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J Virol, 2004; 78: 6073-76
    • (2004) J Virol , vol.78 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3
  • 61
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament MT, Brown WL, Schumacher AJ, Harris RS: APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr Biol, 2004; 14: 1385-91
    • (2004) Curr Biol , vol.14 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 62
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • Yu Q, Chen D, Konig R et al: APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J Biol Chem, 2004; 279: 53379-86
    • (2004) J Biol Chem , vol.279 , pp. 53379-53386
    • Yu, Q.1    Chen, D.2    Konig, R.3
  • 63
    • 67649888155 scopus 로고    scopus 로고
    • Natural Variation in Vif: Differential Impact on APOBEC3G/3F and a Potential Role in HIV-1 Diversification
    • Simon V, Zennou V, Murray D et al: Natural Variation in Vif: Differential Impact on APOBEC3G/3F and a Potential Role in HIV-1 Diversification. PLoS Pathog, 2005; 1: e6
    • (2005) PLoS Pathog , vol.1
    • Simon, V.1    Zennou, V.2    Murray, D.3
  • 64
    • 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
    • Shindo K, Takaori-Kondo A, Kobayashi M et al: 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, 2003; 278: 44412-16
    • (2003) J Biol Chem , vol.278 , pp. 44412-44416
    • Shindo, K.1    Takaori-Kondo, A.2    Kobayashi, M.3
  • 65
    • 12544256041 scopus 로고    scopus 로고
    • Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
    • Newman EN, Holmes RK, Craig HM et al: Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Curr Biol, 2005; 15: 166-70
    • (2005) Curr Biol , vol.15 , pp. 166-170
    • Newman, E.N.1    Holmes, R.K.2    Craig, H.M.3
  • 66
    • 13844270834 scopus 로고    scopus 로고
    • Complementary function of the two catalytic domains of APOBEC3G
    • Navarro F, Bollman B, Chen H et al: Complementary function of the two catalytic domains of APOBEC3G. Virology, 2005; 333: 374-86
    • (2005) Virology , vol.333 , pp. 374-386
    • Navarro, F.1    Bollman, B.2    Chen, H.3
  • 67
    • 17144432313 scopus 로고    scopus 로고
    • Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities
    • Langlois MA, Beale RC, Conticello SG, Neuberger MS: Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities. Nucleic Acids Res, 2005; 33: 1913-23
    • (2005) Nucleic Acids Res , vol.33 , pp. 1913-1923
    • Langlois, M.A.1    Beale, R.C.2    Conticello, S.G.3    Neuberger, M.S.4
  • 69
    • 23044514707 scopus 로고    scopus 로고
    • APOBEC-mediated interference with hepadnavirus production
    • Rosler C, Kock J, Kann M et al: APOBEC-mediated interference with hepadnavirus production. Hepatology, 2005; 42: 301-9
    • (2005) Hepatology , vol.42 , pp. 301-309
    • Rosler, C.1    Kock, J.2    Kann, M.3
  • 70
    • 20344379929 scopus 로고    scopus 로고
    • The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein
    • USA
    • Lochelt M, Romen F, Bastone P et al: The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein. Proc Natl Acad Sci USA, 2005; 102: 7982-87
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 7982-7987
    • Lochelt, M.1    Romen, F.2    Bastone, P.3
  • 71
    • 25444447177 scopus 로고    scopus 로고
    • APOBEC3G targets human T-cell leukemia virus type 1
    • Sasada A, Takaori-Kondo A, Shirakawa K et al: APOBEC3G targets human T-cell leukemia virus type 1. Retrovirology, 2005; 2: 32
    • (2005) Retrovirology , vol.2 , pp. 32
    • Sasada, A.1    Takaori-Kondo, A.2    Shirakawa, K.3
  • 72
    • 4644241324 scopus 로고    scopus 로고
    • Comment on "Inhibition of hepatitis B virus replication by APOBEC3G"
    • Rosler C, Kock J, Malim MH et al: Comment on "Inhibition of hepatitis B virus replication by APOBEC3G". Science, 2004; 305: 1403
    • (2004) Science , vol.305 , pp. 1403
    • Rosler, C.1    Kock, J.2    Malim, M.H.3
  • 73
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by APOBEC3G
    • Turelli P, Mangeat B, Jost S et al: Inhibition of hepatitis B virus replication by APOBEC3G. Science, 2004; 303: 1829
    • (2004) Science , vol.303 , pp. 1829
    • Turelli, P.1    Mangeat, B.2    Jost, S.3
  • 74
    • 3343024503 scopus 로고    scopus 로고
    • Eradication of HIV in infected patients: Some potential approaches
    • Yang QE: Eradication of HIV in infected patients: some potential approaches. Med Sci Monit, 2004; 10(7): RA155-RA165
    • (2004) Med Sci Monit , vol.10 , Issue.7
    • Yang, Q.E.1
  • 75
    • 4444298202 scopus 로고    scopus 로고
    • APOBEC3G versus reverse transcriptase in the generation of HIV-1 drug-resistance mutations
    • Berkhout B, de Ronde A: APOBEC3G versus reverse transcriptase in the generation of HIV-1 drug-resistance mutations. Aids, 2004; 18: 1861-63
    • (2004) Aids , vol.18 , pp. 1861-1863
    • Berkhout, B.1    De Ronde, A.2
  • 76
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat B, Turelli P, Liao S, Trono D: A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J Biol Chem, 2004; 279: 14481-83
    • (2004) J Biol Chem , vol.279 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 77
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • USA
    • Schrofelbauer B, Chen D, Landau NR: A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc Natl Acad Sci USA, 2004; 101: 3927-32
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 78
    • 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
    • USA
    • Bogerd HP, Doehle BP, Wiegand HL, Cullen BR: 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 USA, 2004; 101: 3770-74
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 3770-3774
    • Bogerd, H.P.1    Doehle, B.P.2    Wiegand, H.L.3    Cullen, B.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.