Associated Papers
APOBEC3G protects the genome of human cultured cells and mice from radiation-induced damage.
Britan-Rosich Y et al.
The Febs Journal, 2023
Structural Determinants of the APOBEC3G N-Terminal Domain for HIV-1 RNA Association.
Fukuda H et al.
Frontiers in Cellular and Infection Microbiology, 2019
Deaminase-Dead Mouse APOBEC3 Is an In Vivo Retroviral Restriction Factor.
Stavrou S et al.
Journal of Virology, 2018
Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.
Marx A et al.
Scientific Reports, 2015
RNA-binding residues in the N-terminus of APOBEC3G influence its DNA sequence specificity and retrovirus restriction efficiency.
Bélanger K et al.
Virology, 2015
Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.
Mitra M et al.
Retrovirology, 2015
Catalytic activity of APOBEC3F is required for efficient restriction of Vif-deficient human immunodeficiency virus.
Albin JS et al.
Virology, 2014
Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity.
Horn AV et al.
Nucleic Acids Research, 2014
The local dinucleotide preference of APOBEC3G can be altered from 5'-CC to 5'-TC by a single amino acid substitution.
Rathore A et al.
Journal of Molecular Biology, 2013
APOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotransposition.
Koyama T et al.
Plos One, 2013
A Comparison of Two Single-Stranded DNA Binding Models by Mutational Analysis of APOBEC3G.
Shindo K et al.
Biology, 2012
The innate antiviral factor APOBEC3G targets replication of measles, mumps and respiratory syncytial viruses.
Fehrholz M et al.
The Journal of General Virology, 2012
Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein.
Demorest ZL et al.
The Journal of Biological Chemistry, 2011
Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces.
Shandilya SM et al.
Structure (london, England : 1993), 2010
APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G.
Holmes RK et al.
The Journal of Biological Chemistry, 2007
The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.
Shindo K et al.
The Journal of Biological Chemistry, 2003
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