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Items: 1 to 20 of 143

1.

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. Epub 2012 Jul 20.

2.

Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.

Feng Y, Chelico L.

J Biol Chem. 2011 Apr 1;286(13):11415-26. doi: 10.1074/jbc.M110.199604. Epub 2011 Feb 7.

3.

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.

4.

Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms.

Ara A, Love RP, Chelico L.

PLoS Pathog. 2014 Mar 20;10(3):e1004024. doi: 10.1371/journal.ppat.1004024. eCollection 2014 Mar.

5.

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. Epub 2012 Nov 22. Review.

6.

The local dinucleotide preference of APOBEC3G can be altered from 5'-CC to 5'-TC by a single amino acid substitution.

Rathore A, Carpenter MA, Demir Ö, Ikeda T, Li M, Shaban NM, Law EK, Anokhin D, Brown WL, Amaro RE, Harris RS.

J Mol Biol. 2013 Nov 15;425(22):4442-54. doi: 10.1016/j.jmb.2013.07.040. Epub 2013 Aug 11.

7.

Replication protein A (RPA) hampers the processive action of APOBEC3G cytosine deaminase on single-stranded DNA.

Lada AG, Waisertreiger IS, Grabow CE, Prakash A, Borgstahl GE, Rogozin IB, Pavlov YI.

PLoS One. 2011;6(9):e24848. doi: 10.1371/journal.pone.0024848. Epub 2011 Sep 15.

8.

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

Bélanger K, Langlois MA.

Virology. 2015 Sep;483:141-8. doi: 10.1016/j.virol.2015.04.019. Epub 2015 May 15.

9.

Efficient deamination of 5-methylcytosines in DNA by human APOBEC3A, but not by AID or APOBEC3G.

Wijesinghe P, Bhagwat AS.

Nucleic Acids Res. 2012 Oct;40(18):9206-17. doi: 10.1093/nar/gks685. Epub 2012 Jul 13.

10.

The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action.

Coker HA, Petersen-Mahrt SK.

DNA Repair (Amst). 2007 Feb 4;6(2):235-43. Epub 2006 Dec 8.

PMID:
17161027
11.

Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n.

Refsland EW, Hultquist JF, Harris RS.

PLoS Pathog. 2012;8(7):e1002800. doi: 10.1371/journal.ppat.1002800. Epub 2012 Jul 12.

12.

[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.

PMID:
24783502
13.

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.

14.

Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells.

Chiu YL, Soros VB, Kreisberg JF, Stopak K, Yonemoto W, Greene WC.

Nature. 2005 May 5;435(7038):108-14. Epub 2005 Apr 13. Retraction in: Nature. 2010 Jul 8;466(7303):276.

PMID:
15829920
15.

Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo.

Beale RC, Petersen-Mahrt SK, Watt IN, Harris RS, Rada C, Neuberger MS.

J Mol Biol. 2004 Mar 26;337(3):585-96.

PMID:
15019779
16.

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.

PMID:
12808466
17.

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. Epub 2009 Mar 21.

18.

Death by deamination: a novel host restriction system for HIV-1.

Goff SP.

Cell. 2003 Aug 8;114(3):281-3. Review.

19.

A biochemical analysis linking APOBEC3A to disparate HIV-1 restriction and skin cancer.

Pham P, Landolph A, Mendez C, Li N, Goodman MF.

J Biol Chem. 2013 Oct 11;288(41):29294-304. doi: 10.1074/jbc.M113.504175. Epub 2013 Aug 26.

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