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

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. The protein encoded by this gene lacks the zinc binding activity of other family members. The protein plays a role in immunity, by restricting transmission of foreign DNA such as viruses. One mechanism of foreign DNA restriction is deamination of foreign double-stranded DNA cytidines to uridines, which leads to DNA degradation. However, other mechanisms are also thought to be involved, as anti-viral effect is not dependent on deaminase activity. One allele of this gene results from the deletion of approximately 29.5 kb of sequence between this gene, APOBEC3A, and the adjacent gene APOBEC3B. The breakpoints of the deletion are within the two genes, so the deletion allele is predicted to have the promoter and coding region of APOBEC3A, but the 3' UTR of APOBEC3B. [provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: APOBEC3, APOBEC3G, CAN, APOBEC-1, ACID
Papers on APOBEC3A
APOBEC-induced mutations in human cancers are strongly enriched on the lagging DNA strand during replication.
Nikolaev et al., Moscow, Russia. In Genome Res, Feb 2016
UNASSIGNED: APOBEC3A and APOBEC3B, cytidine deaminases of the APOBEC family, are among the main factors causing mutations in human cancers.
Interferon-γ and Tumor Necrosis Factor-α Produced by T Cells Reduce the HBV Persistence Form, cccDNA, Without Cytolysis.
Protzer et al., München, Germany. In Gastroenterology, Jan 2016
In liver biopsy specimens from patients with acute hepatitis B, but not chronic hepatitis B or controls, hepatocytes expressed APOBEC3A and APOBEC3B.
Molecular basis of the attenuated phenotype of human APOBEC3B DNA mutator enzyme.
Wain-Hobson et al., Paris, France. In Nucleic Acids Res, Nov 2015
The human APOBEC3A and APOBEC3B genes (A3A and A3B) encode DNA mutator enzymes that deaminate cytidine and 5-methylcytidine residues in single-stranded DNA (ssDNA).
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
UNASSIGNED: The apolipoprotein mRNA editing catalytic peptide 3 (APOBEC3; A3) proteins are a family of seven are cytidine deaminases (A3A, A3B, A3C, A3D, A3F, A3G, and A3H) that restrict certain viral infections.
An APOBEC3A hypermutation signature is distinguishable from the signature of background mutagenesis by APOBEC3B in human cancers.
Gordenin et al., United States. In Nat Genet, Sep 2015
Previous indirect evidence implicated APOBEC3B as the more likely major mutator deaminase, whereas the role of APOBEC3A is not established.
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.
The Frequency of Cytidine Editing of Viral DNA Is Differentially Influenced by Vpx and Nucleosides during HIV-1 or SIVMAC Infection of Dendritic Cells.
Cimarelli et al., Lyon, France. In Plos One, 2014
Two cellular factors are currently known to modulate lentiviral infection specifically in myeloid cells: SAMHD1 and APOBEC3A (A3A).
The eQTL-missense polymorphisms of APOBEC3H are associated with lung cancer risk in a Han Chinese population.
Shen et al., Nanjing, China. In Sci Rep, 2014
To test this hypothesis, we systematically screened predicted deleterious polymorphisms in the exon regions of 10 APOBEC core genes (APOBEC1, APOBEC2, APOBEC3A, APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, APOBEC3H, and APOBEC4) and evaluated them with a case-control study including 1200 cases and 1253 controls.
Virology. Comment on "Specific and nonhepatotoxic degradation of nuclear hepatitis B virus cccDNA".
Seeger et al., Los Angeles, United States. In Science, 2014
Lucifora et al. (Research Articles, 14 March 2014, p. 1221) report that the hepatitis B virus (HBV) transcriptional template, a long-lived covalently closed circular DNA (cccDNA) molecule, is degraded noncytolytically by agents that up-regulate APOBEC3A and 3B.
Association of a germline copy number polymorphism of APOBEC3A and APOBEC3B with burden of putative APOBEC-dependent mutations in breast cancer.
Stratton et al., Sanger, United States. In Nat Genet, 2014
A germline copy number polymorphism involving APOBEC3A and APOBEC3B, which effectively deletes APOBEC3B, has been associated with modestly increased risk of breast cancer.
Specific and nonhepatotoxic degradation of nuclear hepatitis B virus cccDNA.
Protzer et al., München, Germany. In Science, 2014
Interferon-α and lymphotoxin-β receptor activation up-regulated APOBEC3A and APOBEC3B cytidine deaminases, respectively, in HBV-infected cells, primary hepatocytes, and human liver needle biopsies.
Molecular mechanisms of HIV immune evasion of the innate immune response in myeloid cells.
Collins et al., Ann Arbor, United States. In Viruses, 2013
Recent findings have provided insight into how the lentiviral accessory proteins, Vpx, Vpr and Vif counteract antiviral factors found in myeloid cells including SAMHD1, APOBEC3G, APOBEC3A, UNG2 and uracil.
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
Chelico et al., Saskatoon, Canada. In J Biol Chem, 2012
APOBEC3A was able to deaminate dsDNA undergoing transcription suggests a genomic cost of a deamination-based retroviral restriction system.
APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1.
Münk et al., New York City, United States. In J Virol, 2012
The authors show that APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 (A3H hapII) acted as potent inhibitors of HTLV-1.
Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.
Krogan et al., San Francisco, United States. In Nature, 2012
CBF-β, which normally functions in concert with RUNX DNA binding proteins, allows the reconstitution of a recombinant six-protein assembly that elicits specific polyubiquitination activity with APOBEC3G, but not the related deaminase APOBEC3A.
Target cell-mediated editing of HIV-1 cDNA by APOBEC3 proteins in human macrophages.
Malim et al., London, United Kingdom. In J Virol, 2011
The authors show that infrequent editing of HIV-1 reverse transcripts can also be mediated by APOBEC3 proteins supplied by the targets of infection.
Evolution of the primate APOBEC3A cytidine deaminase gene and identification of related coding regions.
Vartanian et al., Paris, France. In Plos One, 2011
Data suggest that positive selection was apparent along a few branches which differed compared to positive selection in the carboxy-terminal of APOBEC3G (A3G) that clusters with APOBEC3A (A3A) among cytidine deaminases.
Genetic variants in urinary bladder cancer: collective power of the "wimp SNPs".
Hengstler et al., Dortmund, Germany. In Arch Toxicol, 2011
These SNPs are located next to the following genes: MYC, TP63, PSCA, the TERT-CLPTM1L locus, FGFR3, TACC3, NAT2, CBX6, APOBEC3A, CCNE1, and UGT1A.
APOBEC3A can activate the DNA damage response and cause cell-cycle arrest.
Weitzman et al., Los Angeles, United States. In Embo Rep, 2011
APOBEC3A can activate the DNA damage response and cause cell-cycle arrest.
An overview of cytidine deaminases.
Sarwar et al., London, United Kingdom. In Int J Hematol, 2006
This motif is present in APOBEC family members including activation-induced cytidine deaminase (AID), APOBEC2, and APOBEC3A through APOBEC3G.
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