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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Mar 2014.

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, POLYMERASE
Papers on RED1
Normal root elongation requires arginine produced by argininosuccinate lyase in rice.
New
Ma et al., Kurashiki, Japan. In Plant J, 17 Mar 2014
Here we report a rice mutant (red1 for root elongation defect 1) with short root.
Abnormal expression of an ADAR2 alternative splicing variant in gliomas downregulates adenosine-to-inosine RNA editing.
New
Tian et al., Changchun, China. In Acta Neurochir (wien), 11 Mar 2014
ADAR2 is the main enzyme responsible for recoding editing in humans.
MicroRNA Editing Facilitates Immune Elimination of HCMV Infected Cells.
New
Mandelboim et al., Jerusalem, Israel. In Plos Pathog, 28 Feb 2014
Here we demonstrate that in response to HCMV infection, the expression of the short form of the RNA editing enzyme ADAR1 (ADAR1-p110) is induced.
Oligophrenin-1 (OPHN1), a Gene Involved in X-Linked Intellectual Disability, Undergoes RNA Editing and Alternative Splicing during Human Brain Development.
New
Gallo et al., Roma, Italy. In Plos One, Dec 2013
Specifically, ADAR2 activity is essential for brain development and function.
Down-Regulation of the RNA Editing Enzyme ADAR2 Contributes to RGC Death in a Mouse Model of Glaucoma.
New
Nawy et al., New York City, United States. In Plos One, Dec 2013
The activity of ADAR2, the enzyme responsible for this RNA editing, generally ensures that the vast majority of GluA2 proteins are edited.
Astrocytic 5-HT(2B) receptor as in vitro and in vivo target of SSRIs.
Review
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].
Review
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.
Zalpha-domains: at the intersection between RNA editing and innate immunity.
Review
Athanasiadis, Portugal. In Semin Cell Dev Biol, 2012
A key role in this regulatory function of RNA editing is played by ADAR1, an interferon inducible RNA editing enzyme.
Profound downregulation of the RNA editing enzyme ADAR2 in ALS spinal motor neurons.
GeneRIF
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.
ADAR proteins: structure and catalytic mechanism.
Review
Beal et al., Davis, United States. In Curr Top Microbiol Immunol, 2011
While a crystal structure of the catalytic domain of human ADAR2 has been solved, we still lack structural data for an ADAR catalytic domain bound to RNA, and we lack any structural data for other ADARs.
Pin1 and WWP2 regulate GluR2 Q/R site RNA editing by ADAR2 with opposing effects.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
RNA editing catalyzed by ADAR1 and its function in mammalian cells.
Review
Wang, Pittsburgh, United States. In Biochemistry (mosc), 2011
In mammalian cells two active enzymes, ADAR1 and ADAR2, carry out A-to-I RNA editing.
The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove.
Impact
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.
Impact
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.
Impact
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.
Impact
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.
Impact
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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