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HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G.

Feng Y, Love RP, Chelico L.

J Biol Chem. 2013 Mar 1;288(9):6083-94. doi: 10.1074/jbc.M112.421875.


Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G.

Chelico L, Prochnow C, Erie DA, Chen XS, Goodman MF.

J Biol Chem. 2010 May 21;285(21):16195-205. doi: 10.1074/jbc.M110.107987.


Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.

Love RP, Xu H, Chelico L.

J Biol Chem. 2012 Aug 31;287(36):30812-22. doi: 10.1074/jbc.M112.393181.


RNA-binding residues in the N-terminus of APOBEC3G influence its DNA sequence specificity and retrovirus restriction efficiency.

BĂ©langer K, Langlois MA.

Virology. 2015 Sep;483:141-8. doi: 10.1016/j.virol.2015.04.019.


Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution.

Senavirathne G, Jaszczur M, Auerbach PA, Upton TG, Chelico L, Goodman MF, Rueda D.

J Biol Chem. 2012 May 4;287(19):15826-35. doi: 10.1074/jbc.M112.342790.


AID and Apobec3G haphazard deamination and mutational diversity.

Jaszczur M, Bertram JG, Pham P, Scharff MD, Goodman MF.

Cell Mol Life Sci. 2013 Sep;70(17):3089-108. doi: 10.1007/s00018-012-1212-1. Review.


Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent.

Browne EP, Allers C, Landau NR.

Virology. 2009 May 10;387(2):313-21. doi: 10.1016/j.virol.2009.02.026.


Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase.

Adolph MB, Webb J, Chelico L.

PLoS One. 2013 May 23;8(5):e64196. doi: 10.1371/journal.pone.0064196.


APOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.

Nowarski R, Prabhu P, Kenig E, Smith Y, Britan-Rosich E, Kotler M.

J Mol Biol. 2014 Jul 29;426(15):2840-53. doi: 10.1016/j.jmb.2014.05.012.


[Advances in the study of molecular mechanism of APOBEC3G anti-HIV-1].

Fan B, Cen S, Jiang JD.

Yao Xue Xue Bao. 2008 Jul;43(7):678-82. Review. Chinese.


Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein.

Chaurasiya KR, McCauley MJ, Wang W, Qualley DF, Wu T, Kitamura S, Geertsema H, Chan DS, Hertz A, Iwatani Y, Levin JG, Musier-Forsyth K, Rouzina I, Williams MC.

Nat Chem. 2014 Jan;6(1):28-33. doi: 10.1038/nchem.1795.


[Recent advances in the study of mechanism of APOBEC3G against virus].

Zhu YP, Jiang JD, Peng ZG.

Yao Xue Xue Bao. 2014 Jan;49(1):30-6. Review. Chinese.


Heat shock protein 70 inhibits HIV-1 Vif-mediated ubiquitination and degradation of APOBEC3G.

Sugiyama R, Nishitsuji H, Furukawa A, Katahira M, Habu Y, Takeuchi H, Ryo A, Takaku H.

J Biol Chem. 2011 Mar 25;286(12):10051-7. doi: 10.1074/jbc.M110.166108.


Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.

Feng Y, Love RP, Ara A, Baig TT, Adolph MB, Chelico L.

J Biol Chem. 2015 Nov 6;290(45):27188-203. doi: 10.1074/jbc.M115.666065.


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 ES, Xu H, Mbisa JL, Barr R, Gorelick RJ, Ono A, Freed EO, Hu WS, Pathak VK.

J Biol Chem. 2004 Aug 20;279(34):35822-8.


Uracil DNA glycosylase counteracts APOBEC3G-induced hypermutation of hepatitis B viral genomes: excision repair of covalently closed circular DNA.

Kitamura K, Wang Z, Chowdhury S, Simadu M, Koura M, Muramatsu M.

PLoS Pathog. 2013;9(5):e1003361. doi: 10.1371/journal.ppat.1003361.

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