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Gene Review

APOBEC3G  -  apolipoprotein B mRNA editing enzyme,...

Homo sapiens

Synonyms: A3G, APOBEC-related cytidine deaminase, APOBEC-related protein, APOBEC-related protein 9, ARCD, ...
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Disease relevance of APOBEC3G

  • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif [1].
  • Because DNA deamination takes place after virus entry into target cells, APOBEC3G function is dependent on its association with the viral nucleoprotein complexes that synthesize cDNA and must therefore be incorporated into virions as they assemble in infected cells [1].
  • The APOBEC3G enzyme inhibits the replication of retroviruses by deaminating nascent retroviral cDNA cytosines to uracils, lesions that can result in lethal levels of hypermutation [2].
  • Two members of this family, APOBEC3G and APOBEC3F, have been found to have potent activity against virion infectivity factor deficient (Deltavif) human immunodeficiency virus 1 (HIV-1) [3].
  • The reduction in APOBEC3G incorporation was equivalent to the reduction in the total RNA present in the nucleocapsid mutant virions [4].

Psychiatry related information on APOBEC3G

  • Our findings provided the first evidence showing that APOBEC3G is induced by IFN stimulation in human hepatocytes and thus could be involved in host defense mechanisms directed against hepatitis viruses [5].
  • CONCLUSIONS: Apart from patients in the preclinical phase of Alzheimer's disease, the ARCD category includes non-demented patients who have brain dysfunction that may represent a distinct clinical entity [6].
  • METHODS: Double-sandwich ELISA (Innotest htau antigen and beta-Amyloid (1-42), Innogenetics) were used to quantify the above markers in a total of 20 patients with ARCD, 33 AD patients with mild to moderate dementia and 50 mentally intact subjects [7].
  • METHODS: All persons aged 60 years or older who were residents of the rural area of Wadi Ara were examined for identification of DAT, vascular dementia (VaD) and conversion from age related cognitive decline (ARCD) to DAT using DSM-IV criteria and a semi-structured questionnaire for collection of demographic and medical data [8].

High impact information on APOBEC3G


Chemical compound and disease context of APOBEC3G


Biological context of APOBEC3G


Anatomical context of APOBEC3G


Associations of APOBEC3G with chemical compounds


Physical interactions of APOBEC3G

  • Further, the N-terminal half determined RNase sensitivity and was necessary for the high molecular mass complex assembly of APOBEC3G but not APOBEC3F [27].

Regulatory relationships of APOBEC3G

  • CONCLUSION: APOBEC3G is incorporated into HTLV-1 virions and inhibits the infection of HTLV-1 without exerting its cytidine deaminase activity [28].
  • Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G [29].
  • Mutations of conserved hydrophobic residues (Ile-120, Ala-123, and Leu-124) located between the two Cys residues in the HCCH motif disrupt binding of the zinc-coordinating region to Cul5 and inhibit APOBEC3G degradation [30].

Other interactions of APOBEC3G


Analytical, diagnostic and therapeutic context of APOBEC3G


  1. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Sheehy, A.M., Gaddis, N.C., Malim, M.H. Nat. Med. (2003) [Pubmed]
  2. APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast. Schumacher, A.J., Nissley, D.V., Harris, R.S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. Yu, Q., Chen, D., König, R., Mariani, R., Unutmaz, D., Landau, N.R. J. Biol. Chem. (2004) [Pubmed]
  4. Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. Svarovskaia, E.S., Xu, H., Mbisa, J.L., Barr, R., Gorelick, R.J., Ono, A., Freed, E.O., Hu, W.S., Pathak, V.K. J. Biol. Chem. (2004) [Pubmed]
  5. Anti-viral protein APOBEC3G is induced by interferon-alpha stimulation in human hepatocytes. Tanaka, Y., Marusawa, H., Seno, H., Matsumoto, Y., Ueda, Y., Kodama, Y., Endo, Y., Yamauchi, J., Matsumoto, T., Takaori-Kondo, A., Ikai, I., Chiba, T. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  6. Age related cognitive decline: a clinical entity? A longitudinal study of cerebral blood flow and memory performance. Celsis, P., Agniel, A., Cardebat, D., Démonet, J.F., Ousset, P.J., Puel, M. J. Neurol. Neurosurg. Psychiatr. (1997) [Pubmed]
  7. The diagnostic value of tau protein, beta-amyloid (1-42) and their ratio for the discrimination of alcohol-related cognitive disorders from Alzheimer's disease in the early stages. Kapaki, E., Liappas, I., Paraskevas, G.P., Theotoka, I., Rabavilas, A. International journal of geriatric psychiatry. (2005) [Pubmed]
  8. Genetic and environmental risk factors for Alzheimer's disease in Israeli Arabs. Bowirrat, A., Friedland, R.P., Farrer, L., Baldwin, C., Korczyn, A. J. Mol. Neurosci. (2002) [Pubmed]
  9. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Marin, M., Rose, K.M., Kozak, S.L., Kabat, D. Nat. Med. (2003) [Pubmed]
  10. 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, W.C. Mol. Cell (2003) [Pubmed]
  11. Guanine-adenine bias: a general property of retroid viruses that is unrelated to host-induced hypermutation. Müller, V., Bonhoeffer, S. Trends Genet. (2005) [Pubmed]
  12. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. Wiegand, H.L., Doehle, B.P., Bogerd, H.P., Cullen, B.R. EMBO J. (2004) [Pubmed]
  13. Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases. Dutko, J.A., Schäfer, A., Kenny, A.E., Cullen, B.R., Curcio, M.J. Curr. Biol. (2005) [Pubmed]
  14. A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Xu, H., Svarovskaia, E.S., Barr, R., Zhang, Y., Khan, M.A., Strebel, K., Pathak, V.K. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  15. 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, M.A., Beale, R.C., Conticello, S.G., Neuberger, M.S. Nucleic Acids Res. (2005) [Pubmed]
  16. HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation. Santa-Marta, M., da Silva, F.A., Fonseca, A.M., Goncalves, J. J. Biol. Chem. (2005) [Pubmed]
  17. Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation. Pace, C., Keller, J., Nolan, D., James, I., Gaudieri, S., Moore, C., Mallal, S. J. Virol. (2006) [Pubmed]
  18. Complementary function of the two catalytic domains of APOBEC3G. Navarro, F., Bollman, B., Chen, H., König, R., Yu, Q., Chiles, K., Landau, N.R. Virology (2005) [Pubmed]
  19. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Mangeat, B., Turelli, P., Caron, G., Friedli, M., Perrin, L., Trono, D. Nature (2003) [Pubmed]
  20. Functional analysis of Vif protein shows less restriction of human immunodeficiency virus type 2 by APOBEC3G. Ribeiro, A.C., Maia e Silva, A., Santa-Marta, M., Pombo, A., Moniz-Pereira, J., Goncalves, J., Barahona, I. J. Virol. (2005) [Pubmed]
  21. Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif. Doehle, B.P., Schäfer, A., Cullen, B.R. Virology (2005) [Pubmed]
  22. Distinct Patterns of Cytokine Regulation of APOBEC3G Expression and Activity in Primary Lymphocytes, Macrophages, and Dendritic Cells. Stopak, K.S., Chiu, Y.L., Kropp, J., Grant, R.M., Greene, W.C. J. Biol. Chem. (2007) [Pubmed]
  23. The Anti-HIV-1 Editing Enzyme APOBEC3G Binds HIV-1 RNA and Messenger RNAs That Shuttle between Polysomes and Stress Granules. Kozak, S.L., Marin, M., Rose, K.M., Bystrom, C., Kabat, D. J. Biol. Chem. (2006) [Pubmed]
  24. Cytidine deamination and resistance to retroviral infection: towards a structural understanding of the APOBEC proteins. Huthoff, H., Malim, M.H. Virology (2005) [Pubmed]
  25. Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus. Rose, K.M., Marin, M., Kozak, S.L., Kabat, D. J. Biol. Chem. (2004) [Pubmed]
  26. Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Newman, E.N., Holmes, R.K., Craig, H.M., Klein, K.C., Lingappa, J.R., Malim, M.H., Sheehy, A.M. Curr. Biol. (2005) [Pubmed]
  27. Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle. Wang, X., Dolan, P.T., Dang, Y., Zheng, Y.H. J. Biol. Chem. (2007) [Pubmed]
  28. APOBEC3G targets human T-cell leukemia virus type 1. Sasada, A., Takaori-Kondo, A., Shirakawa, K., Kobayashi, M., Abudu, A., Hishizawa, M., Imada, K., Tanaka, Y., Uchiyama, T. Retrovirology (2005) [Pubmed]
  29. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Luo, K., Xiao, Z., Ehrlich, E., Yu, Y., Liu, B., Zheng, S., Yu, X.F. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  30. A zinc-binding region in Vif binds Cul5 and determines cullin selection. Mehle, A., Thomas, E.R., Rajendran, K.S., Gabuzda, D. J. Biol. Chem. (2006) [Pubmed]
  31. APOBEC3 proteins inhibit human LINE-1 retrotransposition. Muckenfuss, H., Hamdorf, M., Held, U., Perkovic, M., Löwer, J., Cichutek, K., Flory, E., Schumann, G.G., Münk, C. J. Biol. Chem. (2006) [Pubmed]
  32. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. Kobayashi, M., Takaori-Kondo, A., Miyauchi, Y., Iwai, K., Uchiyama, T. J. Biol. Chem. (2005) [Pubmed]
  33. Restriction of foamy viruses by APOBEC cytidine deaminases. Delebecque, F., Suspène, R., Calattini, S., Casartelli, N., Saïb, A., Froment, A., Wain-Hobson, S., Gessain, A., Vartanian, J.P., Schwartz, O. J. Virol. (2006) [Pubmed]
  34. Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Chiu, Y.L., Soros, V.B., Kreisberg, J.F., Stopak, K., Yonemoto, W., Greene, W.C. Nature (2005) [Pubmed]
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