APOBEC3G

Summary

Gene Symbol: APOBEC3G
Description: apolipoprotein B mRNA editing enzyme catalytic subunit 3G
Alias: A3G, ARCD, ARP-9, ARP9, CEM-15, CEM15, MDS019, bK150C2.7, dJ494G10.1, DNA dC->dU-editing enzyme APOBEC-3G, APOBEC-related cytidine deaminase, APOBEC-related protein 9, DNA dC->dU editing enzyme, apolipoprotein B editing enzyme catalytic polypeptide-like 3G, apolipoprotein B mRNA editing enzyme cytidine deaminase, apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G, apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3G, deoxycytidine deaminase, phorbolin-like protein MDS019
Species: human
Products:     APOBEC3G

Top Publications

  1. Burdick R, Smith J, Chaipan C, Friew Y, Chen J, Venkatachari N, et al. P body-associated protein Mov10 inhibits HIV-1 replication at multiple stages. J Virol. 2010;84:10241-53 pubmed publisher
    Recent studies have shown that APOBEC3G (A3G), a potent inhibitor of human immunodeficiency virus type 1 (HIV-1) replication, is localized to cytoplasmic mRNA-processing bodies (P bodies)...
  2. Sadler H, Stenglein M, Harris R, Mansky L. APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis. J Virol. 2010;84:7396-404 pubmed publisher
    ..b>APOBEC3G can extinguish HIV-1 infectivity by its incorporation into virus particles and subsequent cytosine deaminase ..
  3. Wissing S, Galloway N, Greene W. HIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factors. Mol Aspects Med. 2010;31:383-97 pubmed publisher
    ..Vif acts by preventing virion encapsidation of two potent antiviral factors, the APOBEC3G and APOBEC3F cytidine deaminases...
  4. Hu C, Saenz D, Fadel H, Walker W, Peretz M, Poeschla E. The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F. J Virol. 2010;84:11981-93 pubmed publisher
    ..in non-vif-permissive cells (HuT78, H9, and primary human peripheral blood mononuclear cells [PBMCs]), suggesting APOBEC3G (A3G) restriction...
  5. Nagao T, Yamashita T, Miyake A, Uchiyama T, Nomaguchi M, Adachi A. Different interaction between HIV-1 Vif and its cellular target proteins APOBEC3G/APOBEC3F. J Med Invest. 2010;57:89-94 pubmed
    ..mutants of human immunodeficiency virus type 1 (HIV-1) Vif for their interaction with cellular anti-viral factors APOBEC3G/APOBEC3F...
  6. Phalora P, Sherer N, Wolinsky S, Swanson C, Malim M. HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies. J Virol. 2012;86:11712-24 pubmed publisher
    ..b>APOBEC3G and APOBEC3F interact with numerous proteins that regulate cellular RNA metabolism, including components of the ..
  7. Shirakawa K, Takaori Kondo A, Kobayashi M, Tomonaga M, Izumi T, Fukunaga K, et al. Ubiquitination of APOBEC3 proteins by the Vif-Cullin5-ElonginB-ElonginC complex. Virology. 2006;344:263-6 pubmed
    ..HIV-1 Vif overcomes the antiviral activity of APOBEC3G by ubiquitinating the protein...
  8. Soros V, Yonemoto W, Greene W. Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H. PLoS Pathog. 2007;3:e15 pubmed
    APOBEC3G (A3G) is a potent antiretroviral deoxycytidine deaminase that, when incorporated into HIV virions, hypermutates nascent viral DNA formed during reverse transcription...
  9. Wang Y, Shao Q, Yu X, Kong W, Hildreth J, Liu B. N-terminal hemagglutinin tag renders lysine-deficient APOBEC3G resistant to HIV-1 Vif-induced degradation by reduced polyubiquitination. J Virol. 2011;85:4510-9 pubmed publisher
    b>APOBEC3G, a potent HIV-1 host restriction factor, is overcome by HIV-1 viral infectivity factor (Vif), which induces its polyubiquitination and proteasomal degradation...

More Information

Publications142 found, 100 shown here

  1. Yang Y, Guo F, Cen S, Kleiman L. Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F. Virology. 2007;365:92-100 pubmed
    Vif-negative HIV-1 produced in non-permissive human cells incorporate both APOBEC3F (hA3F) AND APOBEC3G (hA3G), and have a severely reduced ability to produce viral DNA in newly infected cells...
  2. Smith H. APOBEC3G: a double agent in defense. Trends Biochem Sci. 2011;36:239-44 pubmed publisher
    b>APOBEC3G (A3G) is an effective cellular host defense factor under experimental conditions in which a functional form of the HIV-encoded protein Vif cannot be expressed...
  3. Gallois Montbrun S, Kramer B, Swanson C, Byers H, Lynham S, Ward M, et al. Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules. J Virol. 2007;81:2165-78 pubmed
    ..edit DNA or RNA and potentially mutate cellular targets, their activities are presumably regulated; for instance, APOBEC3G (A3G) recruitment into high-molecular-weight ribonucleoprotein (RNP) complexes has been shown to suppress its ..
  4. Arias J, Koyama T, Kinomoto M, Tokunaga K. Retroelements versus APOBEC3 family members: No great escape from the magnificent seven. Front Microbiol. 2012;3:275 pubmed publisher
    ..This review summarizes the recent advances in our understanding of the interplay between the retroelements currently active in the human genome and the anti-retroelement A3 proteins...
  5. 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 pubmed
    ..The human immunodeficiency virus type 1 (HIV-1) virion infectivity factor (Vif) overcomes the antiviral activity of APOBEC3G to protect HIV-1 DNA from G-to-A hypermutation...
  6. Chelico L, Prochnow C, Erie D, Chen X, Goodman M. Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G. J Biol Chem. 2010;285:16195-205 pubmed publisher
    APOBEC3G (Apo3G) is a single-stranded DNA-dependent deoxycytidine deaminase, which, in the absence of the human immunodeficiency virus (HIV) viral infectivity factor, is encapsulated into HIV virions...
  7. Romani B, Engelbrecht S, Glashoff R. Antiviral roles of APOBEC proteins against HIV-1 and suppression by Vif. Arch Virol. 2009;154:1579-88 pubmed publisher
    ..The antiviral activity of APOBEC3G and APOBEC3F has been studied more extensively than that of the other members of this family...
  8. Ao Z, Wang X, Bello A, Jayappa K, Yu Z, Fowke K, et al. Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages. Hum Gene Ther. 2011;22:1225-37 pubmed publisher
    In this study, we characterized the anti-HIV activities of various R88-APOBEC3G (R88-A3G) mutant fusion proteins in which each A3G mutant was fused with a virus-targeting polypeptide (R14-88, hereafter named R88) derived from HIV-1 Vpr...
  9. Shlyakhtenko L, Lushnikov A, Miyagi A, Li M, Harris R, Lyubchenko Y. Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA. Biochemistry. 2012;51:6432-40 pubmed
    The DNA cytosine deaminase APOBEC3G (A3G) is capable of blocking retrovirus replication by editing viral cDNA and impairing reverse transcription. However, the biophysical details of this host-pathogen interaction are unclear...
  10. Huthoff H, Towers G. Restriction of retroviral replication by APOBEC3G/F and TRIM5alpha. Trends Microbiol. 2008;16:612-9 pubmed publisher
    ..Examples of such molecules are APOBEC3G, APOBEC3F and TRIM5alpha...
  11. Navarro F, Bollman B, Chen H, König R, Yu Q, Chiles K, et al. Complementary function of the two catalytic domains of APOBEC3G. Virology. 2005;333:374-86 pubmed
    ..viral accessory protein Vif prevents the encapsidation of the antiviral cellular cytidine deaminases APOBEC3F and APOBEC3G by inducing their proteasomal degradation...
  12. Schumacher A, Haché G, MacDuff D, Brown W, Harris R. The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction. J Virol. 2008;82:2652-60 pubmed publisher
    Human APOBEC3G and several other APOBEC3 proteins have been shown to inhibit the replication of a variety of retrotransposons and retroviruses...
  13. Izumi T, Takaori Kondo A, Shirakawa K, Higashitsuji H, Itoh K, Io K, et al. MDM2 is a novel E3 ligase for HIV-1 Vif. Retrovirology. 2009;6:1 pubmed publisher
    ..virus type 1 (HIV-1) Vif plays a crucial role in the viral life cycle by antagonizing a host restriction factor APOBEC3G (A3G)...
  14. Xiao Z, Ehrlich E, Luo K, Xiong Y, Yu X. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J. 2007;21:217-22 pubmed
    ..Treatment with TPEN at an IC50 of 1.79 microM inhibits Cul5 recruitment and APOBEC3G (A3G) degradation...
  15. He Z, Zhang W, Chen G, Xu R, Yu X. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J Mol Biol. 2008;381:1000-11 pubmed publisher
    Apolipoprotein B mRNA-editing catalytic polypeptide-like 3G (APOBEC3G, or A3G) and related cytidine deaminases such as apolipoprotein B mRNA-editing catalytic polypeptide-like 3F (APOBEC3F, or A3F) are potent inhibitors of retroviruses...
  16. Xiao Z, Ehrlich E, Yu Y, Luo K, Wang T, Tian C, et al. 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 pubmed
    b>APOBEC3G (A3G) and related cytidine deaminases are potent inhibitors of retroviruses. HIV-1 Vif hijacks the cellular Cul5-E3 ubiquitin ligase to degrade APOBEC3 proteins and render them ineffective against these viruses...
  17. Wang X, Wang X, Zhang H, Lv M, Zuo T, Wu H, et al. Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-? binding to Vif. Retrovirology. 2013;10:94 pubmed publisher
  18. Chelico L, Sacho E, Erie D, Goodman M. A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV. J Biol Chem. 2008;283:13780-91 pubmed publisher
    b>APOBEC3G (A3G) restricts HIV-1 infection by catalyzing processive C --> U deaminations on single-stranded DNA (ssDNA) with marked 3' --> 5' deamination polarity...
  19. Zhang K, Mangeat B, Ortiz M, Zoete V, Trono D, Telenti A, et al. Model structure of human APOBEC3G. PLoS ONE. 2007;2:e378 pubmed
    b>APOBEC3G (apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G) has antiretroviral activity associated with the hypermutation of viral DNA through cytosine deamination...
  20. Kamata M, Nagaoka Y, Chen I. Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells. PLoS Pathog. 2009;5:e1000342 pubmed publisher
    ..A recent study by Chiu et al. implicates APOBEC3G, an anti-retroviral cytidine deaminase, as the cellular restriction factor...
  21. Okeoma C, Huegel A, LINGAPPA J, Feldman M, Ross S. APOBEC3 proteins expressed in mammary epithelial cells are packaged into retroviruses and can restrict transmission of milk-borne virions. Cell Host Microbe. 2010;8:534-43 pubmed publisher
    ..Moreover, APOBEC3G and other APOBEC3 genes are expressed in human mammary cells and have the potential to restrict viruses produced ..
  22. Stenglein M, Matsuo H, Harris R. Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization. J Virol. 2008;82:9591-9 pubmed publisher
    b>APOBEC3G limits the replication of human immunodeficiency virus type 1, other retroviruses, and retrotransposons...
  23. Tanaka Y, Marusawa H, Seno H, Matsumoto Y, Ueda Y, Kodama Y, et al. Anti-viral protein APOBEC3G is induced by interferon-alpha stimulation in human hepatocytes. Biochem Biophys Res Commun. 2006;341:314-9 pubmed
    Apolipoprotein B mRNA-editing enzyme catalytic-polypeptide 3G (APOBEC3G) is a potent inhibitor of infection by a wide range of retroviruses...
  24. Miyagi E, Opi S, Takeuchi H, Khan M, Goila Gaur R, Kao S, et al. Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1. J Virol. 2007;81:13346-53 pubmed
    b>APOBEC3G (APO3G) is a cellular cytidine deaminase with potent antiviral activity...
  25. Ikeda T, Ohsugi T, Kimura T, Matsushita S, Maeda Y, Harada S, et al. The antiretroviral potency of APOBEC1 deaminase from small animal species. Nucleic Acids Res. 2008;36:6859-71 pubmed publisher
    ..Together, these data reveal that A1 may function as a defense mechanism, regulating retroelements in a wide range of mammalian species...
  26. Lee J, Choi J, Lee H, Kim K, Choi B, Oh Y, et al. Repression of porcine endogenous retrovirus infection by human APOBEC3 proteins. Biochem Biophys Res Commun. 2011;407:266-70 pubmed publisher
    ..by human APOBEC3 proteins, we co-transfected 293T cells with a PERV molecular clone and human APOBEC3F or APOBEC3G expression vectors, and monitored PERV replication competency using a quantitative analysis of PERV pol genes...
  27. Hosseini I, Mac Gabhann F. Multi-scale modeling of HIV infection in vitro and APOBEC3G-based anti-retroviral therapy. PLoS Comput Biol. 2012;8:e1002371 pubmed publisher
    The human APOBEC3G is an innate restriction factor that, in the absence of Vif, restricts HIV-1 replication by inducing excessive deamination of cytidine residues in nascent reverse transcripts and inhibiting reverse transcription and ..
  28. Coker H, Petersen Mahrt S. The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action. DNA Repair (Amst). 2007;6:235-43 pubmed
    ..This is in contrast to the cytoplasmically expressed anti-viral DNA deaminase APOBEC3G, which acts in a processive manner, possibly suggesting that evolutionary pressure has altered the ability of DNA ..
  29. Pido Lopez J, Whittall T, Wang Y, Bergmeier L, Babaahmady K, Singh M, et al. Stimulation of cell surface CCR5 and CD40 molecules by their ligands or by HSP70 up-regulates APOBEC3G expression in CD4(+) T cells and dendritic cells. J Immunol. 2007;178:1671-9 pubmed
    Apolipoprotein B mRNA-editing, enzyme-catalytic, polypeptide-like-3G (A3G) is an intracellular innate antiviral factor that deaminates retroviral cytidine to uridine...
  30. Lafferty M, Sun L, DeMasi L, Lu W, Garzino Demo A. CCR6 ligands inhibit HIV by inducing APOBEC3G. Blood. 2010;115:1564-71 pubmed publisher
    ..the induction of the host restriction factor apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G)...
  31. Hultquist J, Binka M, LaRue R, Simon V, Harris R. Vif proteins of human and simian immunodeficiency viruses require cellular CBF? to degrade APOBEC3 restriction factors. J Virol. 2012;86:2874-7 pubmed publisher
    HIV-1 requires the cellular transcription factor CBF? to stabilize its accessory protein Vif and promote APOBEC3G degradation...
  32. Ooms M, Brayton B, Letko M, Maio S, Pilcher C, Hecht F, et al. HIV-1 Vif adaptation to human APOBEC3H haplotypes. Cell Host Microbe. 2013;14:411-21 pubmed publisher
    ..Proviral DNA from A3H-restricted viruses showed high levels of G-to-A mutations in an A3H-specific GA dinucleotide context. Taken together, our data validate A3H expressed at endogenous levels as a bona fide HIV-1 restriction factor. ..
  33. Delebecque F, Susp ne R, Calattini S, Casartelli N, Sa b A, Froment A, et al. Restriction of foamy viruses by APOBEC cytidine deaminases. J Virol. 2006;80:605-14 pubmed publisher
    ..We show that human APOBEC3G is a potent inhibitor of FV infectivity in cell culture experiments...
  34. Bell C, Connell B, Capovilla A, Venter W, Stevens W, Papathanasopoulos M. Molecular characterization of the HIV type 1 subtype C accessory genes vif, vpr, and vpu. AIDS Res Hum Retroviruses. 2007;23:322-30 pubmed
    ..presence of highly conserved structural and functional motifs similar to other sub-types, for example, the Vif-APOBEC3G interaction domains...
  35. Kitamura S, Ode H, Iwatani Y. Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities. Front Microbiol. 2011;2:258 pubmed publisher
    ..A3F and A3G are the most potent inhibitors of HIV-1, but only in the absence of the virus-encoded protein, Vif...
  36. Hakata Y, Landau N. Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. J Biol Chem. 2006;281:36624-31 pubmed
    ..The Vif protein of lentiviruses binds to specific APOBEC3 proteins, notably A3F and A3G, to induce their degradation by proteasomes...
  37. Bernacchi S, Henriet S, Dumas P, Paillart J, Marquet R. RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study. J Biol Chem. 2007;282:26361-8 pubmed
    ..In these cells, Vif counteracts the natural antiretroviral activity of the DNA-editing enzymes APOBEC3G/3F...
  38. Gallois Montbrun S, Holmes R, Swanson C, Fernández Ocaña M, Byers H, Ward M, et al. Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins. J Virol. 2008;82:5636-42 pubmed publisher
    The human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F (APOBEC3F [A3F]) and A3G proteins are effective inhibitors of infection by various retroelements and share approximately 50% amino acid sequence identity...
  39. Pido Lopez J, Jeffrey P, Wang Y, Seidl T, Babaahmady K, Vaughan R, et al. The effect of allogeneic in vitro stimulation and in vivo immunization on memory CD4(+) T-cell APOBEC3G expression and HIV-1 infectivity. Eur J Immunol. 2009;39:1956-65 pubmed publisher
    Allogeneic immunity is one of the most potent natural immune responses. APOBEC3G (A3G) is an intracellular anti-viral factor that deaminates cytidine to uridine...
  40. Harris R, Hultquist J, Evans D. The restriction factors of human immunodeficiency virus. J Biol Chem. 2012;287:40875-83 pubmed publisher
    ..These HIV restriction and counter-restriction mechanisms suggest strategies for new therapeutic interventions...
  41. Bennett R, Salter J, Liu X, Wedekind J, Smith H. APOBEC3G subunits self-associate via the C-terminal deaminase domain. J Biol Chem. 2008;283:33329-36 pubmed publisher
    Human APOBEC3G (hA3G) is a cytidine deaminase active on HIV single-stranded DNA. Small angle x-ray scattering and molecular envelope restorations predicted a C-terminal dimeric model for RNA-depleted hA3G in solution...
  42. Ali A, Wang J, Nathans R, Cao H, Sharova N, Stevenson M, et al. Synthesis and structure-activity relationship studies of HIV-1 virion infectivity factor (Vif) inhibitors that block viral replication. ChemMedChem. 2012;7:1217-29 pubmed publisher
    ..virus from innate antiviral cellular factor apolipoprotein B mRNA-editing, enzyme-catalytic, polypeptide-like 3G (APOBEC3G; A3G) and is an attractive target for the development of novel antiviral therapeutics...
  43. Kourteva Y, De Pasquale M, Allos T, McMunn C, D Aquila R. APOBEC3G expression and hypermutation are inversely associated with human immunodeficiency virus type 1 (HIV-1) burden in vivo. Virology. 2012;430:1-9 pubmed publisher
    b>APOBEC3G (A3G) and APOBEC3F (A3F) reduce Vif-negative HIV-1 provirus formation and cause disabling provirus G-to-A hypermutation in vitro...
  44. Hatziioannou T, Princiotta M, Piatak M, Yuan F, Zhang F, Lifson J, et al. Generation of simian-tropic HIV-1 by restriction factor evasion. Science. 2006;314:95 pubmed
  45. Bach D, Peddi S, Mangeat B, Lakkaraju A, Strub K, Trono D. Characterization of APOBEC3G binding to 7SL RNA. Retrovirology. 2008;5:54 pubmed publisher
    ..Here, we show that APOBEC3G, but not other APOBEC3 family members, binds 7SL RNA, the common ancestor of Alu RNAs that is specifically ..
  46. Haché G, Abbink T, Berkhout B, Harris R. Optimal translation initiation enables Vif-deficient human immunodeficiency virus type 1 to escape restriction by APOBEC3G. J Virol. 2009;83:5956-60 pubmed publisher
    b>APOBEC3G restricts Vif-deficient human immunodeficiency virus type 1 (HIV-1) by deaminating viral cDNA cytosines to uracils. This promutagenic activity is counteracted by HIV-1 Vif, which is a natural APOBEC3G antagonist...
  47. Feng Y, Chelico L. Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain. J Biol Chem. 2011;286:11415-26 pubmed publisher
    b>APOBEC3G is a single-stranded (ss) DNA deaminase that restricts replication of HIV-1 by inducing viral genome mutagenesis through deamination of cytosine to uracil on HIV-1 cDNA...
  48. Russell R, Pathak V. 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 pubmed
    Human cytidine deaminases APOBEC3G (A3G) and APOBEC3F (A3F) inhibit replication of Vif-deficient human immunodeficiency virus type 1 (HIV-1)...
  49. Huthoff H, Malim M. Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation. J Virol. 2007;81:3807-15 pubmed
    ..to neutralize the human antiviral proteins apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G (APOBEC3G [A3G]) and A3F...
  50. Zhang L, Saadatmand J, Li X, Guo F, Niu M, Jiang J, et al. Function analysis of sequences in human APOBEC3G involved in Vif-mediated degradation. Virology. 2008;370:113-21 pubmed
    Human APOBEC3G (hA3G) has been identified as an anti-HIV cellular factor. As a counter measure, the HIV-1 protein Vif causes the degradation of hA3G by binding to it and directing it to the cellular proteasome...
  51. Goila Gaur R, Khan M, Miyagi E, Kao S, Opi S, Takeuchi H, et al. HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexes. Virology. 2008;372:136-46 pubmed
    HIV-1 Vif inhibits the antiviral activity of APOBEC3G (APO3G) by inducing proteasomal degradation. Here, we studied the effects of Vif on APO3G in vitro. In this system, Vif did not cause APO3G degradation...
  52. Malim M. APOBEC proteins and intrinsic resistance to HIV-1 infection. Philos Trans R Soc Lond B Biol Sci. 2009;364:675-87 pubmed publisher
    Members of the APOBEC family of cellular polynucleotide cytidine deaminases, most notably APOBEC3G and APOBEC3F, are potent inhibitors of HIV-1 infection...
  53. Huthoff H, Autore F, Gallois Montbrun S, Fraternali F, Malim M. RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1. PLoS Pathog. 2009;5:e1000330 pubmed publisher
    The human cytidine deaminase APOBEC3G (A3G) is a potent inhibitor of retroviruses and transposable elements and is able to deaminate cytidines to uridines in single-stranded DNA replication intermediates...
  54. Wolfe L, Stanley B, Liu C, Eliason W, Xiong Y. Dissection of the HIV Vif interaction with human E3 ubiquitin ligase. J Virol. 2010;84:7135-9 pubmed publisher
    ..composed of cullin 5 (Cul5), Rbx2, Elongin B, and Elongin C (EloBC), to polyubiquitinate the antiviral protein APOBEC3G. Multiple regions in the C-terminal half of Vif interact with the E3 ligase...
  55. Holmes R, Koning F, Bishop K, Malim M. APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J Biol Chem. 2007;282:2587-95 pubmed
    ..apolipoprotein B mRNA-editing enzyme catalytic polypeptide 1-like protein 3F) is a cytidine deaminase that, like APOBEC3G, is able to restrict the replication of HIV-1/delta vif...
  56. Reddy K, Winkler C, Werner L, Mlisana K, Abdool Karim S, Ndung u T. APOBEC3G expression is dysregulated in primary HIV-1 infection and polymorphic variants influence CD4+ T-cell counts and plasma viral load. AIDS. 2010;24:195-204 pubmed publisher
    ..Vif), cellular cytosine deaminases such as apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G) inhibit the virus by inducing hypermutations on viral DNA, among other mechanisms of action...
  57. Heger E, Thielen A, Gilles R, Obermeier M, Lengauer T, Kaiser R, et al. APOBEC3G/F as one possible driving force for co-receptor switch of the human immunodeficiency virus-1. Med Microbiol Immunol. 2012;201:7-16 pubmed publisher
    ..Causative agents for G-to-A mutations are the deaminases APOBEC3F and APOBEC3G. We therefore hypothesize that these proteins are one driving force facilitating the appearance of X4 variants...
  58. Aguiar R, Peterlin B. APOBEC3 proteins and reverse transcription. Virus Res. 2008;134:74-85 pubmed publisher
    ..Together, these proteins provide strong and immediate intracellular immunity against incoming pathogens and restrict the movement of mobile genetic elements protecting the genome. ..
  59. Chen K, Harjes E, Gross P, Fahmy A, Lu Y, Shindo K, et al. Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature. 2008;452:116-9 pubmed publisher
    The human APOBEC3G (apolipoprotein B messenger-RNA-editing enzyme, catalytic polypeptide-like 3G) protein is a single-strand DNA deaminase that inhibits the replication of human immunodeficiency virus-1 (HIV-1), other retroviruses and ..
  60. Sato K, Izumi T, Misawa N, Kobayashi T, Yamashita Y, Ohmichi M, et al. Remarkable lethal G-to-A mutations in vif-proficient HIV-1 provirus by individual APOBEC3 proteins in humanized mice. J Virol. 2010;84:9546-56 pubmed publisher
    ..Human APOBEC3G was identified as an HIV-1 restriction factor, which edits nascent HIV-1 DNA by inducing G-to-A hypermutations ..
  61. Kremer M, Suezer Y, Martinez Fernandez Y, Munk C, Sutter G, Schnierle B. Vaccinia virus replication is not affected by APOBEC3 family members. Virol J. 2006;3:86 pubmed
    The APOBEC3G protein represents a novel innate defense mechanism against retroviral infection. It facilitates the deamination of the cytosine residues in the single stranded cDNA intermediate during early steps of retroviral infection...
  62. Muckenfuss H, Kaiser J, Krebil E, Battenberg M, Schwer C, Cichutek K, et al. Sp1 and Sp3 regulate basal transcription of the human APOBEC3G gene. Nucleic Acids Res. 2007;35:3784-96 pubmed
    b>APOBEC3G (A3G), a member of the recently discovered family of human cytidine deaminases, is expressed in peripheral blood lymphocytes and has been shown to be active against HIV-1 and other retroviruses...
  63. Chiu Y. Biochemical fractionation and purification of high-molecular-mass APOBEC3G complexes. Methods Mol Biol. 2011;718:185-206 pubmed publisher
    Human APOBEC3G (A3G) is a cytidine deaminase that broadly restricts the replication of many retroviruses, including HIV-1...
  64. Nathans R, Chu C, Serquina A, Lu C, Cao H, Rana T. Cellular microRNA and P bodies modulate host-HIV-1 interactions. Mol Cell. 2009;34:696-709 pubmed publisher
    ..Thus we provide an example of a single host miRNA regulating HIV-1 production and infectivity. These studies highlight the significance of miRNAs and P bodies in modulating host cell interactions with HIV-1 and possibly other viruses. ..
  65. Du J, Zhao K, Rui Y, Li P, Zhou X, Zhang W, et al. Differential requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor beta. J Virol. 2013;87:1906-11 pubmed publisher
    ..The important interaction domains that are uniquely required for Vif but not RUNX function represent novel targets for the development of HIV inhibitors. ..
  66. Haché G, Liddament M, Harris R. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J Biol Chem. 2005;280:10920-4 pubmed
    The human proteins APOBEC3F and APOBEC3G restrict retroviral infection by deaminating cytosine residues in the first cDNA strand of a replicating virus...
  67. Chen H, Lilley C, Yu Q, Lee D, Chou J, Narvaiza I, et al. APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr Biol. 2006;16:480-5 pubmed
    ..They also highlight the functional differences between APOBEC3 proteins. The APOBEC3 family members have distinct functions and may have evolved to resist various classes of genetic elements. ..
  68. Luo K, Wang T, Liu B, Tian C, Xiao Z, Kappes J, et al. Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J Virol. 2007;81:7238-48 pubmed
    b>APOBEC3G (A3G) is a single-stranded DNA cytidine deaminase that targets retroviral minus-strand DNA and has potent antiviral activity against diverse retroviruses...
  69. Norman J, Mashiba M, McNamara L, Onafuwa Nuga A, Chiari Fort E, Shen W, et al. The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells. Nat Immunol. 2011;12:975-83 pubmed publisher
    b>APOBEC3G (A3G) is an intrinsic antiviral factor that inhibits the replication of human immunodeficiency virus (HIV) by deaminating cytidine residues to uridine...
  70. Hulme A, Bogerd H, Cullen B, Moran J. Selective inhibition of Alu retrotransposition by APOBEC3G. Gene. 2007;390:199-205 pubmed
    ..Here, we have examined the effect of APOBEC3G and APOBEC3F, cytidine deaminases that inhibit Vif-deficient HIV-1 replication, on Alu retrotransposition and ..
  71. Bulliard Y, Turelli P, Röhrig U, Zoete V, Mangeat B, Michielin O, et al. Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition. J Virol. 2009;83:12611-21 pubmed publisher
    ..These enzymes are structurally organized in one or two domains comprising a zinc-coordinating motif. APOBEC3G contains two such domains, only the C terminal of which is endowed with editing activity, while its N-terminal ..
  72. Zhang W, Du J, Evans S, Yu Y, Yu X. T-cell differentiation factor CBF-? regulates HIV-1 Vif-mediated evasion of host restriction. Nature. 2011;481:376-9 pubmed publisher
    ..In our study, knockdown of endogenous CBF-? blocked Vif-induced APOBEC3G polyubiquitination and degradation...
  73. Uyttendaele I, Lavens D, Catteeuw D, Lemmens I, Bovijn C, Tavernier J, et al. Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G. PLoS ONE. 2012;7:e44143 pubmed publisher
    ..The strategy was used to detect residues of the human cytidine deaminase Apobec3G that are important for its homodimerization and its interaction with the HIV-1 Gag and Vif proteins...
  74. Stanley D, Bartholomeeusen K, Crosby D, Kim D, Kwon E, Yen L, et al. Inhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3G. PLoS Pathog. 2012;8:e1003085 pubmed publisher
    ..by the NEDD8-conjugating enzyme UBE2F is required for HIV Vif-mediated degradation of the host restriction factor APOBEC3G (A3G)...
  75. Iwatani Y, Chan D, Wang F, Maynard K, Sugiura W, Gronenborn A, et al. Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G. Nucleic Acids Res. 2007;35:7096-108 pubmed
    b>APOBEC3G (A3G), a host protein that inhibits HIV-1 reverse transcription and replication in the absence of Vif, displays cytidine deaminase and single-stranded (ss) nucleic acid binding activities...
  76. Harjes E, Gross P, Chen K, Lu Y, Shindo K, Nowarski R, et al. An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model. J Mol Biol. 2009;389:819-32 pubmed publisher
    Human APOBEC3G (A3G) belongs to a family of polynucleotide cytidine deaminases. This family includes APOBEC1 and AID, which edit APOB mRNA and antibody gene DNA, respectively...
  77. Vetter M, D Aquila R. Cytoplasmic APOBEC3G restricts incoming Vif-positive human immunodeficiency virus type 1 and increases two-long terminal repeat circle formation in activated T-helper-subtype cells. J Virol. 2009;83:8646-54 pubmed publisher
    Cytoplasmic APOBEC3G has been reported to block wild-type human immunodeficiency virus type 1 (HIV-1) infection in some primary cells...
  78. Sharifi H, Furuya A, de Noronha C. The role of HIV-1 Vpr in promoting the infection of nondividing cells and in cell cycle arrest. Curr Opin HIV AIDS. 2012;7:187-94 pubmed publisher
    ..killer-cell ligands on the surface of HIV-1-infected cells requires the actions of both the cytidine deaminase APOBEC3G and uracil-N-glycosylase 2 in association with HIV-1 Vpr...
  79. Strebel K. HIV accessory proteins versus host restriction factors. Curr Opin Virol. 2013;3:692-9 pubmed publisher
    ..This review aims at providing an update of our current understanding of how Vif, Vpu, and Vpx control the cellular restriction factors APOBEC3G, BST-2, and SAMHD1, respectively.
  80. Komohara Y, Suekane S, Noguchi M, Matsuoka K, Yamada A, Itoh K. Expression of APOBEC3G in kidney cells. Tissue Antigens. 2007;69:95-8 pubmed
    The apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G (APOBEC3G), a member of the APOBEC family possessing DNA mutator activity through cytosine deamination, is reported to play an important role in host defense against ..
  81. Han Y, Wang X, Dang Y, Zheng Y. APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication. PLoS Pathog. 2008;4:e1000095 pubmed publisher
    b>APOBEC3G (A3G)/APOBEC3F (A3F) are two members of APOBEC3 cytidine deaminase subfamily. Although they potently inhibit the replication of vif-deficient HIV-1, this mechanism is still poorly understood...
  82. Zhang L, Li X, Ma J, Yu L, Jiang J, Cen S. The incorporation of APOBEC3 proteins into murine leukemia viruses. Virology. 2008;378:69-78 pubmed publisher
  83. De Maio F, Rocco C, Aulicino P, Bologna R, Mangano A, Sen L. Effect of HIV-1 Vif variability on progression to pediatric AIDS and its association with APOBEC3G and CUL5 polymorphisms. Infect Genet Evol. 2011;11:1256-62 pubmed publisher
    The APOBEC3G protein is a restriction factor that can inhibit the replication of HIV-1...
  84. Amoedo N, Afonso A, Cunha S, Oliveira R, Machado E, Soares M. Expression of APOBEC3G/3F and G-to-A hypermutation levels in HIV-1-infected children with different profiles of disease progression. PLoS ONE. 2011;6:e24118 pubmed publisher
    Increasing evidence has accumulated showing the role of APOBEC3G (A3G) and 3F (A3F) in the control of HIV-1 replication and disease progression in humans. However, very few studies have been conducted in HIV-infected children...
  85. Chiu Y, Greene W. The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu Rev Immunol. 2008;26:317-53 pubmed publisher
    ..The discovery of APOBEC3G and related cytidine deaminases as one class of host restriction factors and of the action of HIV-1 Vif as a ..
  86. Chiu Y, Greene W. APOBEC3G: an intracellular centurion. Philos Trans R Soc Lond B Biol Sci. 2009;364:689-703 pubmed publisher
    The intrinsic antiretroviral factor APOBEC3G (A3G) is highly active against HIV-1 and other retroviruses...