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Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.

Chen KM, Harjes E, Gross PJ, Fahmy A, Lu Y, Shindo K, Harris RS, Matsuo H.

Nature. 2008 Mar 6;452(7183):116-9. doi: 10.1038/nature06638. Epub 2008 Feb 20.


Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications.

Holden LG, Prochnow C, Chang YP, Bransteitter R, Chelico L, Sen U, Stevens RC, Goodman MF, Chen XS.

Nature. 2008 Nov 6;456(7218):121-4. doi: 10.1038/nature07357. Epub 2008 Oct 12.


An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model.

Harjes E, Gross PJ, Chen KM, Lu Y, Shindo K, Nowarski R, Gross JD, Kotler M, Harris RS, Matsuo H.

J Mol Biol. 2009 Jun 26;389(5):819-32. doi: 10.1016/j.jmb.2009.04.031. Epub 2009 Apr 21.


Structure and real-time monitoring of the enzymatic reaction of APOBEC3G which is involved in anti-HIV activity.

Furukawa A, Nagata T, Matsugami A, Habu Y, Sugiyama R, Hayashi F, Kobayashi N, Yokoyama S, Takaku H, Katahira M.

Nucleic Acids Symp Ser (Oxf). 2009;(53):87-8. doi: 10.1093/nass/nrp044.


[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.


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. Epub 2004 Jun 20.


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. Epub 2013 Jan 11.


Dissecting APOBEC3G substrate specificity by nucleoside analog interference.

Rausch JW, Chelico L, Goodman MF, Le Grice SF.

J Biol Chem. 2009 Mar 13;284(11):7047-58. doi: 10.1074/jbc.M807258200. Epub 2009 Jan 9.


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 Jul 3;424(6944):99-103. Epub 2003 May 28.


The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction.

Schumacher AJ, Haché G, Macduff DA, Brown WL, Harris RS.

J Virol. 2008 Mar;82(6):2652-60. doi: 10.1128/JVI.02391-07. Epub 2008 Jan 9.


Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA.

Lu X, Zhang T, Xu Z, Liu S, Zhao B, Lan W, Wang C, Ding J, Cao C.

J Biol Chem. 2015 Feb 13;290(7):4010-21. doi: 10.1074/jbc.M114.624262. Epub 2014 Dec 25.


Identification of an HIV-1 replication inhibitor which rescues host restriction factor APOBEC3G in Vif-APOBEC3G complex.

Zhang S, Zhong L, Chen B, Pan T, Zhang X, Liang L, Li Q, Zhang Z, Chen H, Zhou J, Luo H, Zhang H, Bai C.

Antiviral Res. 2015 Oct;122:20-7. doi: 10.1016/j.antiviral.2015.07.009. Epub 2015 Aug 1.


NMR assignments and the identification of the secondary structure of the anti-retroviral cytidine deaminase.

Furukawa A, Nagata T, Habu Y, Sugiyama R, Hayashi F, Yokoyama S, Takaku H, Katahira M.

Nucleic Acids Symp Ser (Oxf). 2008;(52):183-4. doi: 10.1093/nass/nrn093.


Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.

Kouno T, Luengas EM, Shigematsu M, Shandilya SM, Zhang J, Chen L, Hara M, Schiffer CA, Harris RS, Matsuo H.

Nat Struct Mol Biol. 2015 Jun;22(6):485-91. doi: 10.1038/nsmb.3033. Epub 2015 May 18.


APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase.

Suspène R, Sommer P, Henry M, Ferris S, Guétard D, Pochet S, Chester A, Navaratnam N, Wain-Hobson S, Vartanian JP.

Nucleic Acids Res. 2004 Apr 30;32(8):2421-9. Print 2004.


Complementary function of the two catalytic domains of APOBEC3G.

Navarro F, Bollman B, Chen H, König R, Yu Q, Chiles K, Landau NR.

Virology. 2005 Mar 15;333(2):374-86.


Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G.

Furukawa A, Nagata T, Matsugami A, Habu Y, Sugiyama R, Hayashi F, Kobayashi N, Yokoyama S, Takaku H, Katahira M.

EMBO J. 2009 Feb 18;28(4):440-51. doi: 10.1038/emboj.2008.290. Epub 2009 Jan 15.


A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion.

Xu H, Svarovskaia ES, Barr R, Zhang Y, Khan MA, Strebel K, Pathak VK.

Proc Natl Acad Sci U S A. 2004 Apr 13;101(15):5652-7. Epub 2004 Mar 30.


Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.

Chen KM, Martemyanova N, Lu Y, Shindo K, Matsuo H, Harris RS.

FEBS Lett. 2007 Oct 2;581(24):4761-6. Epub 2007 Sep 7.

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