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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
Estrogen receptor signal in regulation of B cell activation during diverse immune responses.
Dasgupta et al., Vũng Tàu, Vietnam. In Int J Biochem Cell Biol, 30 Nov 2015
The mode of signalling action of this single chain nuclear receptor protein molecule depends on its ability to bind to the promoters of Pax5, HOXC4 and apolipoprotein B RNA-editing enzyme activation-induced cytidine deaminase (AID) genes.
Differential regulation of expression of RNA-editing enzymes, ADAR1 and ADAR2, by 5-aza-2'-deoxycytidine and trichostatin A in human neuronal SH-SY5Y cells.
Ito et al., Ōsaka, Japan. In Neuroreport, 19 Nov 2015
UNASSIGNED: Adenosine deaminase acting on RNA (ADAR) enzymes, ADAR1 and ADAR2, mediates adenosine-to-inosine RNA editing, and their mRNA expressions are altered during developmental, physiological, and pathophysiological processes in the nervous system.
A Phenotypic Screen for Functional Mutants of Human Adenosine Deaminase acting on RNA 1.
Beal et al., In Acs Chem Biol, 15 Oct 2015
ADAR1 and ADAR2 are two members of the family that have been shown to be catalytically active.
Androgen receptor, androgen-producing enzymes and their transcription factors in extramammary Paget disease.
Sasano et al., Sendai, Japan. In Hum Pathol, Aug 2015
AR, 5α-red1, 17β-HSD5, and β-catenin immunoreactivity was evaluated by using the modified H-score method while cyclin D1, p53, forkhead box protein P1, and a proliferation marker, Ki-67, were quantified using labeling index.
Acquisition of conditioned fear is followed by region-specific changes in RNA editing of glutamate receptors.
Gaisler-Salomon et al., New York City, United States. In Stress, May 2015
Additionally, we observed experience-dependent changes in mRNA expression of the RNA editing enzymes ADAR2 and ADAR1 in amygdala and hippocampus, and a learning-dependent increase in the alternatively spliced inactive form of ADAR2 in the amygdala.
The molecular link between inefficient GluA2 Q/R site-RNA editing and TDP-43 pathology in motor neurons of sporadic amyotrophic lateral sclerosis patients.
Kwak et al., Japan. In Brain Res, Nov 2014
TAR DNA-binding protein (TDP-43) pathology and reduced expression of adenosine deaminase acting on RNA 2 (ADAR2), which is the RNA editing enzyme responsible for adenosine-to-inosine conversion at the GluA2 glutamine/arginine (Q/R) site, concomitantly occur in the same motor neurons of amyotrophic lateral sclerosis (ALS) patients; this finding suggests a link between these two ALS-specific molecular abnormalities.
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.
Biological function of activation-induced cytidine deaminase (AID).
Evans et al., New York City, United States. In Biomed J, Sep 2014
Based on homology, it was originally proposed to be an RNA-editing enzyme, but so far, no RNA substrates are known.
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).
[Calpain plays a crucial role in TDP-43 pathology].
Kwak et al., Tokyo, Japan. In Rinsho Shinkeigaku, 2013
ALS-specific molecular abnormalities other than TDP-43 pathology in the motor neurons of sporadic ALS patients include inefficient RNA editing at the GluA2 glutamine/arginine (Q/R) site, which is specifically catalyzed by adenosine deaminase acting on RNA 2 (ADAR2).
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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