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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 20 May 2015.

Adenosine deaminase, RNA-specific, B1

RED1, ADAR2, RNA editing enzyme
This gene encodes the enzyme responsible for pre-mRNA editing of the glutamate receptor subunit B by site-specific deamination of adenosines. Studies in rat found that this enzyme acted on its own pre-mRNA molecules to convert an AA dinucleotide to an AI dinucleotide which resulted in a new splice site. Alternative splicing of this gene results in several transcript variants, some of which have been characterized by the presence or absence of an ALU cassette insert and a short or long C-terminal region. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PKI, CAN, ACID, V1a, APOBEC-1
Papers on RED1
Aberrant alternative splicing pattern of ADAR2 downregulates adenosine-to-inosine editing in glioma.
Zhang et al., Changchun, China. In Oncol Rep, 30 Jun 2015
ADAR2 is the main enzyme responsible for A-to-I editing in humans, and A-to-I underediting at the glutamine (Q)/arginine (R) site of the glutamate receptor subunit B (GluR-B) is associated with the pathogenesis and invasiveness of glioma.
Autophagy in spinal motor neurons of conditional ADAR2-knockout mice: an implication for a role of calcium in increased autophagy flux in ALS.
Shin et al., Tokyo, Japan. In Neurosci Lett, 14 Jun 2015
UNASSIGNED: In the motor neurons of amyotrophic lateral sclerosis (ALS) patients, an RNA editing enzyme called adenosine deaminase acting on RNA 2 (ADAR2) is down-regulated and consequently GluA2 mRNAs unedited at the Q/R site is expressed in contrast to normal motor neurons that express only GluA2 edited at this site.
Identification of DNA cleavage- and recombination-specific hnRNP cofactors for activation-induced cytidine deaminase.
Honjo et al., Kyoto, Japan. In Proc Natl Acad Sci U S A, 05 Jun 2015
AID originally was postulated to function as an RNA-editing enzyme, based on its strong homology with apolipoprotein B mRNA-editing enzyme, catalytic polypeptide 1 (APOBEC1), the enzyme that edits apolipoprotein B-100 mRNA in the presence of the APOBEC cofactor APOBEC1 complementation factor/APOBEC complementation factor (A1CF/ACF).
New non-coding lytic transcripts derived from the Epstein Barr virus latency origin of replication oriP are hyper-edited, bind the paraspeckle protein, NONO/p54nrb, and support lytic viral transcription.
Flemington et al., New Orleans, United States. In J Virol, 29 May 2015
The double-stranded RNA-binding protein and RNA-editing enzyme ADAR was found to bind to oriPtLs, likely facilitating editing of the FR hairpin.
Circular RNAs in the Mammalian Brain Are Highly Abundant, Conserved, and Dynamically Expressed.
Rajewsky et al., Berlin, Germany. In Mol Cell, 22 May 2015
circRNA expression correlated negatively with expression of the RNA-editing enzyme ADAR1.
The Supraspliceosome - A Multi-Task Machine for Regulated Pre-mRNA Processing in the Cell Nucleus.
Sperling et al., Israel. In Comput Struct Biotechnol J, Sep 2014
Supraspliceosomes harbor additional pre-mRNA processing components, such as the 5'-end and 3'-end processing components, and the RNA editing enzymes ADAR1 and ADAR2.
Glutamate drugs and pharmacogenetics of OCD: a pathway-based exploratory approach.
Fortune et al., Baltimore, United States. In Expert Opin Drug Discov, 2013
Furthermore, recent genetic epidemiology research findings are presented with a focus on the positional candidate genes SLC1A1 (a glutamate transporter), ADAR3 (an RNA-editing enzyme), RYR3 (a Ca(2+) channel), PBX1 (a homeobox transcription factor) and a GWAS candidate gene, DLGAP1 (a protein interacting with post-synaptic density).
Aicardi-Goutières syndrome: clues from the RNase H2 knock-out mouse.
Rabe, Kiel, Germany. In J Mol Med (berl), 2013
AGS-causing mutations have also been found in the genes of the 3'-exonuclease TREX1, the dNTP triphosphatase SAMHD1, as well as the RNA-editing enzyme ADAR1, defining defects in nucleic acid metabolism pathways as a common hallmark of AGS pathology.
Astrocytic 5-HT(2B) receptor as in vitro and in vivo target of SSRIs.
Huang et al., Shenyang, China. In Recent Pat Cns Drug Discov, 2012
Chronic treatment with fluoxetine upregulates gene expression of cPLA₂, ADAR2, GluK2 and 5-HT(2B) receptors, and RNA editing of the later two in cultured astrocytes and in astrocytes obtained by fluorescence-activated cell sorting of cells from fluoxetinetreated mice.
[Molecular link between inefficient GluA2 RNA editing and TDP-43 pathology in ALS motor neurons].
Kwak, Tokyo, Japan. In Brain Nerve, 2012
Importantly, this molecular abnormality is a direct cause of death of motor neurons in conditional knockout mice for adenosine deaminase acting on RNA 2 (ADAR2), the enzyme that specifically catalyzes RNA editing at the GluA2 Q/R site.
Profound downregulation of the RNA editing enzyme ADAR2 in ALS spinal motor neurons.
Kwak et al., Tokyo, Japan. In Neurobiol Dis, 2012
These results indicated that ADAR2 downregulation is a profound pathological change relevant to death of motor neurons in ALS.
Pin1 and WWP2 regulate GluR2 Q/R site RNA editing by ADAR2 with opposing effects.
O'Connell et al., Edinburgh, United Kingdom. In Embo J, 2011
ADAR2 protein levels and catalytic activity are coordinately regulated in a positive manner by Pin1 and negatively by WWP2 and this may have downstream effects on the function of glutamate receptor 2.
An essential role of RNA editing enzyme ADAR1 in mouse skin.
Wang et al., In J Dermatol Sci, 2011
Through these gene knockout animal models we demonstrated for the first time that ADAR1 is an essential molecule for skin integrity.
Functional conservation in human and Drosophila of Metazoan ADAR2 involved in RNA editing: loss of ADAR1 in insects.
O'Connell et al., Edinburgh, United Kingdom. In Nucleic Acids Res, 2011
The strong functional similarity of human ADAR2 and Drosophila Adar suggests rather that these are true orthologs.
Host response to polyomavirus infection is modulated by RNA adenosine deaminase ADAR1 but not by ADAR2.
Samuel et al., Santa Barbara, United States. In J Virol, 2011
These results provide evidence that ADAR1, and not ADAR2, is the deaminase responsible for protection against virus-induced cytopathic effects, and that ADAR de fi ciency does not adversely affect PyV growth.
The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove.
Allain et al., Zürich, Switzerland. In Cell, 2010
Here, we report the solution structure of the ADAR2 double-stranded RNA-binding motifs (dsRBMs) bound to a stem-loop pre-mRNA encoding the R/G editing site of GluR-2.
A new function for the RNA-editing enzyme ADAR1.
Nishikura et al., Philadelphia, United States. In Nat Immunol, 2009
This RNA-editing enzyme is now shown to be involved in hematopoiesis, where it acts to suppress interferon signaling and to block premature apoptosis.
Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.
Matsuo et al., Minneapolis, United States. In Nature, 2008
The human APOBEC3G (apolipoprotein B messenger-RNA-editing enzyme, catalytic polypeptide-like 3G) protein is a single-strand DNA deaminase that inhibits the replication of human immunodeficiency virus-1 (HIV-1), other retroviruses and retrotransposons.
Helicobacter pylori infection triggers aberrant expression of activation-induced cytidine deaminase in gastric epithelium.
Chiba et al., Kyoto, Japan. In Nat Med, 2007
Here we show that infection of gastric epithelial cells with 'cag' pathogenicity island (cagPAI)-positive H. pylori induced aberrant expression of activation-induced cytidine deaminase (AID), a member of the cytidine-deaminase family that acts as a DNA- and RNA-editing enzyme, via the IkappaB kinase-dependent nuclear factor-kappaB activation pathway.
The APOBEC-2 crystal structure and functional implications for the deaminase AID.
Chen et al., Los Angeles, United States. In Nature, 2007
APOBEC-2 (APO2) belongs to the family of apolipoprotein B messenger RNA-editing enzyme catalytic (APOBEC) polypeptides, which deaminates mRNA and single-stranded DNA.
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