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A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function.

Salter JD, Krucinska J, Raina J, Smith HC, Wedekind JE.

Biochemistry. 2009 Nov 17;48(45):10685-7. doi: 10.1021/bi901642c.


Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G.

Shlyakhtenko LS, Lushnikov AY, Li M, Lackey L, Harris RS, Lyubchenko YL.

J Biol Chem. 2011 Feb 4;286(5):3387-95. doi: 10.1074/jbc.M110.195685. Epub 2010 Dec 1.


RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1.

Huthoff H, Autore F, Gallois-Montbrun S, Fraternali F, Malim MH.

PLoS Pathog. 2009 Mar;5(3):e1000330. doi: 10.1371/journal.ppat.1000330. Epub 2009 Mar 6.


Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes.

McDougall WM, Okany C, Smith HC.

J Biol Chem. 2011 Sep 2;286(35):30655-61. doi: 10.1074/jbc.M111.269506. Epub 2011 Jul 7.


Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.

McDougall WM, Smith HC.

Biochem Biophys Res Commun. 2011 Sep 9;412(4):612-7. doi: 10.1016/j.bbrc.2011.08.009. Epub 2011 Aug 11.


Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.

Ao Z, Yu Z, Wang L, Zheng Y, Yao X.

PLoS One. 2008 Apr 16;3(4):e1995. doi: 10.1371/journal.pone.0001995.


Inducible APOBEC3G-Vif double stable cell line as a high-throughput screening platform to identify antiviral compounds.

Nowotny B, Schneider T, Pradel G, Schirmeister T, Rethwilm A, Kirschner M.

Antimicrob Agents Chemother. 2010 Jan;54(1):78-87. doi: 10.1128/AAC.00775-09. Epub 2009 Oct 19.


The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication.

Wang X, Ao Z, Chen L, Kobinger G, Peng J, Yao X.

J Virol. 2012 Apr;86(7):3777-86. doi: 10.1128/JVI.06594-11. Epub 2012 Feb 1.


Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif.

Shirakawa K, Takaori-Kondo A, Yokoyama M, Izumi T, Matsui M, Io K, Sato T, Sato H, Uchiyama T.

Nat Struct Mol Biol. 2008 Nov;15(11):1184-91. doi: 10.1038/nsmb.1497. Epub 2008 Oct 5.


Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.

Shlyakhtenko LS, Lushnikov AY, Miyagi A, Li M, Harris RS, Lyubchenko YL.

J Struct Biol. 2013 Nov;184(2):217-25. doi: 10.1016/j.jsb.2013.09.008. Epub 2013 Sep 18.


APOBEC2 is a monomer in solution: implications for APOBEC3G models.

Krzysiak TC, Jung J, Thompson J, Baker D, Gronenborn AM.

Biochemistry. 2012 Mar 6;51(9):2008-17. doi: 10.1021/bi300021s. Epub 2012 Feb 27.


A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV.

Chelico L, Sacho EJ, Erie DA, Goodman MF.

J Biol Chem. 2008 May 16;283(20):13780-91. doi: 10.1074/jbc.M801004200. Epub 2008 Mar 24.


The antiviral factor APOBEC3G improves CTL recognition of cultured HIV-infected T cells.

Casartelli N, Guivel-Benhassine F, Bouziat R, Brandler S, Schwartz O, Moris A.

J Exp Med. 2010 Jan 18;207(1):39-49. doi: 10.1084/jem.20091933. Epub 2009 Dec 28.


Human APOBEC3G-mediated editing can promote HIV-1 sequence diversification and accelerate adaptation to selective pressure.

Kim EY, Bhattacharya T, Kunstman K, Swantek P, Koning FA, Malim MH, Wolinsky SM.

J Virol. 2010 Oct;84(19):10402-5. doi: 10.1128/JVI.01223-10. Epub 2010 Jul 21.


Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules.

Gallois-Montbrun S, Kramer B, Swanson CM, Byers H, Lynham S, Ward M, Malim MH.

J Virol. 2007 Mar;81(5):2165-78. Epub 2006 Dec 13.


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.

Pido-Lopez J, Whittall T, Wang Y, Bergmeier LA, Babaahmady K, Singh M, Lehner T.

J Immunol. 2007 Feb 1;178(3):1671-9.


APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication.

Han Y, Wang X, Dang Y, Zheng YH.

PLoS Pathog. 2008 Jul 4;4(7):e1000095. doi: 10.1371/journal.ppat.1000095.


Exosomes packaging APOBEC3G confer human immunodeficiency virus resistance to recipient cells.

Khatua AK, Taylor HE, Hildreth JE, Popik W.

J Virol. 2009 Jan;83(2):512-21. doi: 10.1128/JVI.01658-08. Epub 2008 Nov 5.


Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G.

Rose KM, Marin M, Kozak SL, Kabat D.

AIDS Res Hum Retroviruses. 2005 Jul;21(7):611-9.

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