Published in J Biol Chem on October 08, 2008
RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1. PLoS Pathog (2009) 1.84
Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure (2010) 1.65
An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model. J Mol Biol (2009) 1.62
Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G. J Biol Chem (2010) 1.42
Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA. Retrovirology (2009) 1.27
A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function. Biochemistry (2009) 1.01
Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes. J Biol Chem (2011) 1.00
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Leveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS. Future Virol (2009) 0.89
Atomic force microscopy studies of APOBEC3G oligomerization and dynamics. J Struct Biol (2013) 0.88
Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity. Biochem Biophys Res Commun (2011) 0.88
Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA. J Biol Chem (2014) 0.88
Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulations. PLoS One (2010) 0.87
Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase. PLoS One (2013) 0.86
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RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates. Nucleic Acids Res (2015) 0.78
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Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature (2003) 13.24
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Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science (2003) 10.79
The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature (2003) 10.76
Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell (2003) 9.48
HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell (2003) 7.42
An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics (2002) 7.10
Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome. Nat Struct Mol Biol (2004) 6.26
Retracted Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature (2005) 5.28
RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Mol Cell (2002) 5.14
Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Curr Biol (2005) 4.98
APOBEC3G DNA deaminase acts processively 3' --> 5' on single-stranded DNA. Nat Struct Mol Biol (2006) 4.00
A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc Natl Acad Sci U S A (2004) 3.73
Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo. J Mol Biol (2004) 3.59
Complementary function of the two catalytic domains of APOBEC3G. Virology (2005) 3.45
Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev (2004) 3.28
Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J Virol (2006) 3.27
The interaction between HIV-1 Gag and APOBEC3G. J Biol Chem (2004) 3.27
APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J Virol (2004) 3.17
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Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. J Biol Chem (2004) 3.01
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Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature (2008) 2.80
A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J Biol Chem (2004) 2.79
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APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein. J Biol Chem (2004) 2.73
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Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J Virol (2006) 2.63
The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J Biol Chem (2005) 2.62
High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition. Proc Natl Acad Sci U S A (2006) 2.54
Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging. J Virol (2004) 2.34
Inhibition of tRNA₃(Lys)-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. J Virol (2006) 2.32
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Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G. FEBS Lett (2007) 1.62
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Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions. Retrovirology (2007) 1.48
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