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Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G

This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. The protein encoded by this gene has been found to be a specific inhibitor of human immunodeficiency virus-1 (HIV-1) infectivity. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, APOBEC3, APOBEC-1, CD4, ACID
Papers on APOBEC3G
Basal transcription of APOBEC3G is regulated by USF1 gene in hepatocyte.
Kang et al., Zhengzhou, China. In Biochem Biophys Res Commun, Feb 2016
UNASSIGNED: Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G, A3G) exert antiviral defense as an important factor of innate immunity.
Specific induction of endogenous viral restriction factors using CRISPR/Cas-derived transcriptional activators.
Cullen et al., Durham, United States. In Proc Natl Acad Sci U S A, Jan 2016
Here, we demonstrate that such "synergistic activation mediators" can induce the expression of two restriction factors, APOBEC3G (A3G) and APOBEC3B (A3B), in human cells that normally lack these proteins.
Overexpression of APOBEC3F in tumor tissues is potentially predictive for poor recurrence-free survival from HBV-related hepatocellular carcinoma.
Chen et al., Shanghai, China. In Discov Med, Dec 2015
APOBEC3B, which was significantly up-regulated in HCC tumor tissues (P<0.001), was negatively associated with HCC overall survival by Cox regression (HR=1.005,
APOBEC3G Variants and Protection against HIV-1 Infection in Burkina Faso.
Simpore et al., Ouagadougou, Burkina Faso. In Plos One, Dec 2015
Studies on host factors, particularly the APOBEC3G gene, have previously found an association with AIDS progression in some populations and against some HIV-1 strains but not others.
The Role of the Single Deaminase Domain APOBEC3A in Virus Restriction, Retrotransposition, DNA Damage and Cancer.
Stephens et al., Denver, United States. In J Gen Virol, Nov 2015
The best studied of the A3 proteins has been APOBEC3G because of its potent activity against HIV-1Δvif.
Targeting virus-host interactions of HIV replication.
Debyser et al., Leuven, Belgium. In Curr Top Med Chem, Oct 2015
In this respect, compounds targeting the Vif-APOBEC3G interaction have been described.
Molecular targets and pathways involved in liver metastasis of colorectal cancer.
Krüger et al., München, Germany. In Clin Exp Metastasis, Aug 2015
In addition, the functional role and validation of targets such as PRL3, Trop-2, L1CAM, S100A4, S100P, CD133, LIPC, and APOBEC3G are summarized.
Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.
Alian et al., Haifa, Israel. In Sci Rep, 2014
We reveal a novel allosteric regulatory mechanism of APOBEC3 enzymes showing that APOBEC3G and APOBEC3A coordination of a secondary zinc ion, reminiscent to ancestral deoxycytidylate deaminases, enhances deamination activity.
Restriction Factors in HIV-1 Disease Progression.
Berthoux et al., Trois-Rivières, Canada. In Curr Hiv Res, 2014
TRIM5α, Mx2/MxB, TRIM22/Staf50, SAMHD1, p21/CDKN1, tetherin/BST2/CD137, APOBEC3G and APOBEC3F have all been proposed to inhibit HIV-1, often with gene variant- or cellular context-specificity.
[Cellular restriction factors that inhibit human immunodeficiency virus replication: new strategies in antiretroviral therapy].
Vázquez-Pérez et al., In Rev Invest Clin, 2014
The best characterized restriction factor is the cytidine deaminase APOBEC3G that has been shown to have an important role in HIV pathogenesis.
Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein.
Williams et al., Boston, United States. In Nat Chem, 2014
APOBEC3G is a member of this family that inhibits HIV-1 replication in the absence of the viral infectivity factor Vif. Inhibition of HIV replication occurs by both deamination of viral single-stranded DNA and a deamination-independent mechanism.
APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10.
Zhang et al., Guangzhou, China. In J Biol Chem, 2012
APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10
APOBEC3G expression and hypermutation are inversely associated with human immunodeficiency virus type 1 (HIV-1) burden in vivo.
D'Aquila et al., Nashville, United States. In Virology, 2012
These results indicate that APOBEC3G deaminase-dependent activity above a threshold level, and its deaminase-independent functions, contribute to decreasing Vif-positive HIV virus replication in vivo.
Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.
Lyubchenko et al., Omaha, United States. In Biochemistry, 2012
APOBEC3G monomers, dimers, and higher-order oligomers can bind ssDNA substrates in a manner independent of strand polarity and availability of free ssDNA ends.
APOBEC3G enhances lymphoma cell radioresistance by promoting cytidine deaminase-dependent DNA repair.
Kotler et al., Jerusalem, Israel. In Blood, 2012
APOBEC3G activity involved processing of DNA flanking a DSB in an integrated reporter cassette. Atomic force microscopy indicated that APOBEC3G multimers associate with ssDNA termini, triggering multimer disassembly to multiple catalytic units.
Signals in APOBEC3F N-terminal and C-terminal deaminase domains each contribute to encapsidation in HIV-1 virions and are both required for HIV-1 restriction.
Donahue et al., Nashville, United States. In J Biol Chem, 2012
Analysis of the A3F (W126A L306A) double mutant revealed that both residues are required for full anti-HIV function
T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction.
Yu et al., Changchun, China. In Nature, 2012
In our study, knockdown of endogenous CBF-β blocked Vif-induced APOBEC3G polyubiquitination and degradation.
Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.
Krogan et al., San Francisco, United States. In Nature, 2012
CBF-beta is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity
The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells.
Collins et al., Ann Arbor, United States. In Nat Immunol, 2011
report that viral protein R (Vpr), which interacts with a uracil glycosylase, also counteracted APOBEC3G by diminishing the incorporation of uridine
Damage control: how HIV survives the editor APOBEC3G.
Gasser et al., In Nat Immunol, 2011
The antiviral factor APOBEC3G upregulates the expression of ligands for the activating receptor NKG2D via DNA damage induced by the viral protein Vpr in cells infected with human immunodeficiency virus.
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