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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2

Top mentioned proteins: APOBEC-1, APOBEC3G, APOBEC3, APOBEC4, APOBEC3A
Papers on APOBEC2
Modulating APOBEC expression enhances DNA vaccine immunogenicity.
Cunha-Neto et al., São Paulo, Brazil. In Immunol Cell Biol, Nov 2015
We also showed that murine APOBEC2 expression in HEK293T cells led to a 10-fold reduction in intracellular plasmid levels and plasmid-encoded mRNA, and a 2.6-fold reduction in GFP-expressing cells.
APOBECs and virus restriction.
Dudley et al., Minneapolis, United States. In Virology, May 2015
APOBEC1 and activation-induced cytosine deaminase (AID) have specialized functions in RNA editing and antibody gene diversification, respectively, whereas APOBEC2 and APOBEC4 appear to have different functions.
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.
Zinc-binding domain-dependent, deaminase-independent actions of apolipoprotein B mRNA-editing enzyme, catalytic polypeptide 2 (Apobec2), mediate its effect on zebrafish retina regeneration.
Goldman et al., Ann Arbor, United States. In J Biol Chem, 2014
Unique among this family is Apobec2, whose enzymatic activity has been questioned and whose function remains poorly explored.
APOBEC2 mRNA and protein is predominantly expressed in skeletal and cardiac muscles of chickens.
Tian et al., China. In Gene, 2014
Apolipoprotein B mRNA-editing enzyme catalytic subunit 2 (APOBEC2) plays an important role in regulating and maintaining muscle development in mammals.
APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.
Mueller et al., Minneapolis, United States. In J Mol Biol, 2014
In contrast, APOBEC3A, APOBEC3C and APOBEC2 are monomers at all tested concentrations.
Crystal structure of the DNA cytosine deaminase APOBEC3F: the catalytically active and HIV-1 Vif-binding domain.
Schiffer et al., Worcester, United States. In Structure, 2013
The A3F-CTD shares structural motifs with portions of APOBEC3G-CTD, APOBEC3C, and APOBEC2.
Focal aberrations indicate EYA2 and hsa-miR-375 as oncogene and tumor suppressor in cervical carcinogenesis.
Steenbergen et al., Amsterdam, Netherlands. In Genes Chromosomes Cancer, 2013
Concurrent altered expression in hgCIN and/or cervical carcinomas compared with normal cervical samples was shown for ATP13A3, HES1, OPA1, HRASLS, EYA2, ZMYND8, APOBEC2, and NCR2.
Excessive activity of apolipoprotein B mRNA editing enzyme catalytic polypeptide 2 (APOBEC2) contributes to liver and lung tumorigenesis.
Chiba et al., Kyoto, Japan. In Int J Cancer, 2012
Hepatocellular carcinoma developed in 2 of 20 APOBEC2 transgenic mice at 72 weeks of age.
Free Energy Profile of APOBEC3G Protein Calculated by a Molecular Dynamics Simulation.
Matsuo et al., Tokyo, Japan. In Biology (basel), 2011
This finding suggests that in solution A3Gctd is not likely to adopt the continuous β2 strand configuration present in the APOBEC2 crystal structure.
Microarray analysis of tonsils in immunoglobulin A nephropathy patients.
Rakugi et al., Suita, Japan. In Biochem Biophys Res Commun, 2010
The APOBEC2 was confirmed to be elevated in the tonsils with IgAN patients, and the gene expression level was negatively related with serum IgG level in overall patients.
Deficiency in APOBEC2 leads to a shift in muscle fiber type, diminished body mass, and myopathy.
Rada et al., Fukuoka, Japan. In J Biol Chem, 2010
Data show that APOBEC2 is preferentially associated with slow-twitch muscle, with its abundance being considerably greater in soleus compared with gastrocnemius muscle and, within soleus muscle, in slow as opposed to fast muscle fibers.
APOBEC deaminases-mutases with defensive roles for immunity.
Chen et al., Los Angeles, United States. In Sci China C Life Sci, 2009
Studies indicate the APOBEC family consists of 11 members: APOBEC-1 (Apo1), APOBEC-2 (Apo2), activation induced cytidine deaminase (AID), APOBEC- 3A, -3B, -3C, -3DE, -3F, -3H (Apo3A-H) and APOBEC- 4 (Apo4).
Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications.
Chen et al., Los Angeles, United States. In Nature, 2008
The APOBEC3G-CD2 structure has a five-stranded beta-sheet core that is common to all known deaminase structures and closely resembles the structure of another APOBEC protein, APOBEC2 (ref.
Cytidine deaminases as a weapon against retroviruses and a new target for antiviral therapy.
Takaori-Kondo et al., Kyoto, Japan. In Mini Rev Med Chem, 2008
It is a member of the APOBEC family of cytidine deaminases consisting of APOBEC1, APOBEC2, APOBEC3 (A to H), and AID (activation induced deaminase).
The AID/APOBEC family of nucleic acid mutators.
Conticello, Florence, Italy. In Genome Biol, 2007
The crystal structure of human APOBEC2 shows remarkable similarities to that of the bacterial tRNA-editing enzyme TadA, which suggests a conserved mechanism by which polynucleotides are recognized and deaminated.
[Vertebrate immunity: mutator proteins and their evolution].
Pavlov et al., In Genetika, 2007
The functions of APOBEC2 and APOBEC4 have not been yet determined.
The APOBEC-2 crystal structure and functional implications for the deaminase AID.
Chen et al., Los Angeles, United States. In Nature, 2007
crystal structure of APOBEC2
DNA deamination in immunity: AID in the context of its APOBEC relatives.
Neuberger et al., Cambridge, United Kingdom. In Adv Immunol, 2006
AID and APOBEC2 are the oldest family members with APOBEC1 and the APOBEC3s being later arrivals restricted to placental mammals.
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