ライフサイエンスコーパス: ADAR

1 ADAR (adenosine deaminase that acts on RNA) editing enzy

2 ADAR edits also non-coding sequences of target RNAs, suc

3 ADAR proteins alter gene expression both by catalyzing a

4 ADAR-b was a 5'-splice site variant that possessed a 26-

5 ADARs act on RNA that is largely double-stranded and con

6 ADARs are adenosine deaminases responsible for RNA editi

7 ADARs are adenosine deaminases responsible for RNA-editi

8 ADARs are adenosine deaminases that act on RNA and are r

9 ADARs are also interesting in regard to the remarkable d

10 ADARs are essential for normal mammalian development, an

11 ADARs are essential in mammals and are particularly impo

12 ADARs are modular enzymes with multiple double-stranded

13 ADARs are RNA editing enzymes that target double-strande

14 ADARs capable of editing biologically relevant RNA subst

15 ADARs have also been shown to affect RNA interference (R

16 ADARs interact with Dicer to augment the processing of p

17 ssed a 26-amino acid deletion within exon 7; ADAR-c was a 3'-splice site variant that possessed an ad

18 binding is understood, little is known about ADAR catalytic domain/RNA interactions.

19 splice site variants of the 1226-amino acid ADAR-a protein, designated b and c, were identified that

20 r2, are known to encode enzymatically active ADARs in mammalian cells.

21 Although ADARs deaminate perfectly base-paired dsRNA promiscuousl

22 indicate that a tight binding ligand for an ADAR can be generated by incorporation of 8-azanebularin

23 Nascent RNA from an ADAR-null strain was also sequenced, indicating that alm

24 T (adjusted odds ratio, 1.66; P = 0.04); and ADAR Ex9+14A (adjusted odds ratio, 1.67; P = 0.03).

25 al expression of importin alpha proteins and ADAR protein variants.

26 1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, and ADAR).

27 ing, comparing small RNAs from wild-type and ADAR mutant Caenorhabditis elegans.

28 carried out by a cellular activity known as ADAR (adenosine deaminase), which acts on RNA substrates

29 show that mutations in ADAR1 (also known as ADAR) cause the autoimmune disorder Aicardi-Goutieres sy

30 to substrate specificity differences between ADAR family members.

31 By enhancing the linkage between ADAR's catalytic domain and the guide RNA, and by introd

32 investigations into the relationship between ADAR levels, target transcripts, and complex behaviors.

33 ere we uncover an unanticipated link between ADARs (ADAR1 and ADAR2) and the expression of target gen

34 Using chemotaxis assays, we show that both ADARs are important for normal behavior.

35 We found that both ADARs dramatically increased RNA editing, which was corr

36 However, once bound, ADARs deaminate certain adenosines more efficiently than

37 supports deamination of the R/G adenosine by ADAR-2.

38 o-inosine (A-to-I) RNA editing, catalysed by ADAR enzymes conserved in metazoans, plays an important

39 denosine to inosine RNA editing catalyzed by ADAR enzymes is common in humans, and altered editing is

40 mplications for the human diseases caused by ADAR mutations.

41 sine-to-inosine (A-to-I) editing of dsRNA by ADAR proteins is a pervasive epitranscriptome feature.

42 The specificity and extent of RNA editing by ADAR enzymes is determined largely by local primary sequ

43 uide RNA strands for directed DNA editing by ADAR were used to target six different 2-deoxyadenosines

44 rid substrates are deaminated efficiently by ADAR deaminase domains at dA-C mismatches and with E to

45 scriptional modification of RNA, mediated by ADAR (adenosine deaminase acting on RNA) enzymes.

46 d post-transcriptional mechanism mediated by ADAR enzymes that diversifies the transcriptome by alter

47 after infection, suggesting modification by ADAR.

48 ptional alteration of double-stranded RNA by ADAR deaminases that is crucial for homeostasis and deve

49 of endo-siRNAs was significantly affected by ADARs, and many altered 26G loci had intronic reads and

50 hydrolytic deamination reaction catalyzed by ADARs.

51 ng minimal substrates for RNAs deaminated by ADARs in vivo.

52 cells may involve hyper-editing of dsRNA by ADARs, followed by targeted cleavage.

53 specifically targets dsRNAs hyper-edited by ADARs.

54 nally, we propose a model whereby editing by ADARs results in downregulation of gene expression via S

55 t editing of a microRNA (miRNA) precursor by ADARs can modulate the target specificity of the mature

56 te that its expression could be repressed by ADARs beyond their RNA editing and double-stranded RNA (

57 as A's embedded in RNA stems are targeted by ADARs, RNA editing inF.

58 editing in noncoding regions was a conserved ADAR function, we applied our method to poly(A)+ RNA of

59 sines by dsRNA-specific adenosine deaminase (ADAR) can lead to the nuclear retention of edited transc

60 e-stranded RNA-specific adenosine deaminase (ADAR) is an interferon-inducible RNA-editing enzyme impl

61 The RNA-editing adenosine deaminases (ADARs) catalyze deamination of adenosine to inosine in a

62 by one of the host RNA adenosine deaminases (ADARs).

63 to-I editing has not been precisely defined, ADARs have been shown to act before splicing, suggesting

64 Our results demonstrated ADAR dimerization independent of their binding to dsRNA,

65 eterodimer complex formation among different ADAR gene family members was detected.

66 denosines are minimally affected by dramatic ADAR reduction, whereas editing of others is severely cu

67 Here we show that RNA editing by Drosophila ADAR modulates the expression of three co-transcribed mi

68 In this report, we establish that Drosophila ADAR (adenosine deaminase acting on RNA) forms a dimer o

69 y the adenosine deaminase that act on dsRNA (ADAR) family of enzymes.

70 inases acting on double-stranded RNA(dsRNA) (ADAR), occurs predominantly in the 3' untranslated regio

71 nderstanding of substrate recognition during ADAR-catalyzed RNA editing and are important for structu

72 two functionally distinct human RNA editing ADARs.

73 We describe the two C.elegans ADAR genes, adr-1 and adr-2, and characterize strains co

74 ing per se and that even genomically encoded ADARs that are catalytically inactive may have such func

75 ins with deletions in the two genes encoding ADARs, adr-1 and adr-2.

76 domain of the Drosophila RNA-editing enzyme ADAR and expresses the fusion protein in vivo.

77 The RNA editing enzyme ADAR chemically modifies adenosine (A) to inosine (I), w

78 e catalytic domain of the RNA editing enzyme ADAR to an antisense guide RNA, specific adenosines can

79 d RNA-binding protein and RNA-editing enzyme ADAR was found to bind to oriPtLs, likely facilitating e

80 containing RNAs and used it to identify five ADAR substrates in Caenorhabditis elegans.

81 RNA regulatory sites as a novel function for ADAR activity.

82 Here, we engineer Drosophila hypomorphic for ADAR expression using homologous recombination.

83 We propose a model for ADAR dimerization whereby ADAR monomers first contact ds

84 Homodimer formation may be necessary for ADAR to act as active deaminases.

85 e findings unravel a new regulatory role for ADAR and raise the possibility that ADAR mediates the di

86 ribonucleoside in RNA is not a substrate for ADAR, in contrast to adenosine deaminase (ADA), which ca

87 nsistent with known sequence preferences for ADARs.

88 tation hot spots were confirmed in 15 genes; ADAR, DCAF12L2, GLT1D1, ITGA7, MAP1B, MRGPRX4, PSRC1, RA

89 is important, the underlying rules governing ADAR substrate recognition are not well understood.

90 entification and characterization of a human ADAR protein, hADAT1, that specifically deaminates adeno

91 te of SDRE was compared with those for human ADARs on various substrates and found to be within an or

92 A hybrids may be a natural function of human ADARs.

93 The identities of the newly identified ADAR substrates suggest that RNA editing may influence m

94 oped a method for systematically identifying ADAR substrates.

95 Importantly, ADAR reaction progress can be monitored by following the

96 s of mutant mice and Drosophila deficient in ADAR activities provide further evidence that pre-mRNA e

97 Mutations in ADAR, which encodes the ADAR1 RNA-editing enzyme, cause

98 A substantial reduction in ADAR activity (>80%) leads to altered circadian motor pa

99 defining structure-function relationships in ADAR reactions.

100 Several ISGs, including ADAR, FAM46C, LY6E and MCOLN2, enhanced the replication

101 f ADAR1 has the highest affinity among known ADARs, with a subnanomolar dissociation constant.

102 we describe dADAR deletion mutants that lack ADAR activity in extracts.

103 Caenorhabditis elegans lacking ADARs exhibit reduced chemotaxis, but the targets respon

104 Three mammalian ADAR gene family members (ADAR1-3) have been identified.

105 The observation of many ADAR-edited dsRNAs in mammalian immune cells, a subset o

106 eamination mechanisms distinct from metazoan ADARs.

107 iver or spleen after oral infection of mice, ADAR, PKR, Mx, and CIITA expression levels were elevated

108 te the feasibility of structurally mimicking ADAR substrates as a method to regulate protein expressi

109 rminus (amino acids 1-46) yields a monomeric ADAR that retains the ability to bind dsRNA but is inact

110 In Drosophila, multiple ADAR isoforms are generated from a single locus (dAdar)

111 The mutant ADAR dimer complexes were intact, as demonstrated by the

112 As expected, these mutant ADARs could no longer perform their catalytic function d

113 To identify critical neural ADAR targets in C. elegans, we performed an unbiased ass

114 ian cells, as highlighted by the analysis of ADAR-null mutants.

115 on and new tools for biophysical analysis of ADAR-RNA complexes.

116 ll RNA binding, as tested for two classes of ADAR ligands, long and short dsRNA.

117 ed cis elements associated with a cluster of ADAR modification sites within the endogenous Drosophila

118 revealed that the exon 6 and 7 deletions of ADAR-b and -c variants altered the functional importance

119 editing of METTL7A is merely a footprint of ADAR binding, and there are a subset of target genes tha

120 ies have identified key in vivo functions of ADAR enzymes, informing our understanding of the biologi

121 ts ADAR function since the edited isoform of ADAR is less active in vitro and in vivo than the genome

122 Different isoforms of ADAR with different editing activities can form heterodi

123 and selective editing and that the level of ADAR expression can play an important role: overexpressi

124 king differences in the expression levels of ADAR genes.

125 fic levels that correlate with the levels of ADAR mRNA expression.

126 g of neuronal transcripts is the key mode of ADAR activity for normal behavior in Drosophila.

127 e first evidence that neuronal phenotypes of ADAR mutants can be caused by altered gene expression.

128 Among a mixed population of ADAR substrates, ADAR2 preferentially favors its own tra

129 work-wide temporal and spatial regulation of ADAR activity can tune the complex system of RNA-editing

130 rstanding of the functions and regulation of ADAR-mediated RNA editing.

131 This is the first report of ADAR's involvement in a potent antiviral pathway and its

132 led by an unexpected dichotomous response of ADAR target transcripts, i.e. certain adenosines are min

133 measles virus, although the precise role of ADAR during measles virus infection remains unknown.

134 To test the role of ADAR in PyV infection, we used genetically null mouse em

135 sis approach which allows rapid screening of ADAR variants in single yeast cells and provides quantit

136 and are important for structural studies of ADAR.RNA complexes.

137 In the 12 years since the discovery of ADARs only a few natural substrates have been identified

138 To evaluate effects of ADARs on small RNAs that derive from dsRNA precursors, w

139 The expression of ADARs, the editing enzymes, is ubiquitous among true met

140 n of HDV RNA replication by mutated forms of ADARs defective for deaminase activity.

141 eciated and this gene regulatory function of ADARs is most likely to be of high biological importance

142 The functions of ADARs in known substrates suggest that the enzymes serve

143 coincide with observed expression levels of ADARs.

144 rough controlled subcellular localization of ADARs, which in turn is governed by the coordinated loca

145 Loss of ADARs affects neuronal function in all animals studied t

146 an play an important role: overexpression of ADARs inhibits HDV RNA replication and compromises virus

147 our understanding of the biological roles of ADARs, we developed a method for systematically identify

148 This non-editing side of ADARs opens another door to target cancer.

149 The functional significance of ADARs is much more diverse than previously appreciated a

150 out the intrinsic deamination specificity of ADARs derives from analyses of Xenopus ADAR1.

151 xpected to accelerate mechanistic studies of ADARs.

152 o understand the effects of the mutations on ADAR reactivity.

153 microRNAs had altered levels in at least one ADAR mutant strain, and miRNAs with significantly altere

154 lytic domain is closely related to the other ADAR proteins.

155 reactions of these substrates by recombinant ADAR-2, an RNA-editing adenosine deaminase.

156 cating that almost all A-to-I events require ADAR.

157 We show that editing restricts ADAR function since the edited isoform of ADAR is less a

158 mmals are adenosine deaminase acting on RNA (ADAR) 1 and 2.

159 ng enzyme adenosine deaminase acting on RNA (ADAR) 2, as deduced from analysis of ADAR2 self-editing.

160 rgets of adenosine deaminases acting on RNA (ADAR) and validation by means of capillary sequencing.

161 ession of adenosine deaminase acting on RNA (ADAR) contribute to cis- and trans-regulatory mechanisms

162 Adenosine deaminases acting on RNA (ADAR) convert adenosine residues into inosines in double

163 diated by adenosine deaminase acting on RNA (ADAR) enzymes that regulate stem cell maintenance.

164 ing by adenosine deaminases that act on RNA (ADAR) enzymes was quantified over time using RNA-seq dat

165 diting by adenosine deaminase acting on RNA (ADAR) enzymes, but the functional significance of this a

166 diated by adenosine deaminase acting on RNA (ADAR) enzymes.

167 not have adenosine deaminase acting on RNA (ADAR) orthologs and are believed to lack A-to-I RNA edit

168 9CT) and adenosine deaminases acting on RNA (ADAR)(rs1127309TC) genes were analyzed by real-time PCR.

169 Staufen, adenosine deaminase acting on RNA (ADAR), and spermatid perinuclear RNA binding protein (SP

170 ted by adenosine deaminases that act on RNA (ADAR), we quantified expression of ADAR1 transcripts in

171 undergoes adenosine deaminase acting on RNA (ADAR)-dependent adenosine-to-inosine RNA editing.

172 study of adenosine deaminase acting on RNA (ADAR)-mediated RNA editing in Drosophila.

173 iated by adenosine deaminases acting on RNA (ADAR).

174 ction of adenosine deaminases acting on RNA (ADAR).

175 alyzed by adenosine deaminase acting on RNA (ADAR).

176 Adenosine deaminase that acts on RNA (ADAR)1 and ADAR2 are enzymes that catalyze such reaction

177 A editase adenosine deaminase acting on RNA (ADAR)1 gene, occurs in 30-50% of MM patients and portend

178 ine deAminase acting on double-stranded RNA (ADAR) family of enzymes.

179 deaminases that act on double-stranded RNA (ADAR).

180 Adenosine deaminases that act on RNA (ADARs) are a family of RNA editing enzymes that convert

181 Adenosine deaminases acting on RNA (ADARs) are best known for altering the coding sequences

182 Adenosine deaminases acting on RNA (ADARs) are involved in RNA editing that converts adenosi

183 Adenosine deaminases that act on RNA (ADARs) are RNA editing enzymes that convert adenosine to

184 Adenosine deaminases that act on RNA (ADARs) are RNA-editing enzymes that convert adenosine to

185 Adenosine deaminases that act on RNA (ADARs) are RNA-editing enzymes that deaminate adenosines

186 Adenosine deaminases that act on RNA (ADARs) carry out adenosine (A) to inosine (I) editing re

187 Adenosine deaminases acting on RNA (ADARs) catalyze the C-6 deamination of adenosine (A) to

188 Adenosine deaminases acting on RNA (ADARs) catalyze the deamination of adenosine to inosine

189 Adenosine deaminases acting on RNA (ADARs) catalyze the editing of adenosine residues to ino

190 Adenosine deaminases acting on RNA (ADARs) catalyze the hydrolytic deamination of adenosine

191 The adenosine deaminases that act on RNA (ADARs) catalyze the site-specific conversion of adenosin

192 own as adenosine deaminases that act on RNA (ADARs) catalyzes adenosine deamination in RNA.

193 The adenosine deaminases acting on RNA (ADARs) comprise a family of RNA editing enzymes that sel

194 Adenosine deaminases that act on RNA (ADARs) constitute a family of RNA-editing enzymes that c

195 ammalian adenosine deaminases acting on RNA (ADARs) constitute a family of sequence-related proteins

196 Adenosine deaminases that act on RNA (ADARs) deaminate adenosines in dsRNA to produce inosines

197 Adenosine deaminases that act on RNA (ADARs) deaminate adenosines to produce inosines within R

198 Adenosine deaminases acting on RNA (ADARs) hydrolytically deaminate adenosines (A) in a wide

199 iting by adenosine deaminases acting on RNA (ADARs) provides an additional mechanism for introducing

200 s that adenosine deaminases that act on RNA (ADARs) require a cofactor, we show that IP6 is required

201 ng) by adenosine deaminases that act on RNA (ADARs), where up to 50% of adenosine (A) residues are ch

202 ing by adenosine deaminases that act on RNA (ADARs), where up to 50% of adenosine residues may be con

203 ng) by adenosine deaminases that act on RNA (ADARs), whereby up to 50-60% of adenosine residues are c

204 osine by adenosine deaminases acting on RNA (ADARs).

205 iting by adenosine deaminases acting on RNA (ADARs).

206 d by the adenosine deaminases acting on RNA (ADARs).

207 own as adenosine deaminases that act on RNA (ADARs).

208 ted by adenosine deaminases that act on RNA (ADARs).

209 own as adenosine deaminases that act on RNA (ADARs).

210 ery of adenosine deaminases that act on RNA (ADARs).

211 ne deaminases acting on double-stranded RNA (ADARs) catalyze the deamination of adenosine (A) to prod

212 Adenosine deaminases acting on RNAs (ADARs) convert adenosine residues to inosines in primary

213 ly of adenosine deaminases that act on RNAs (ADARs).

214 relation was found between VDR rs1544410CT, ADAR rs1127309TC, OASL rs1169279CT polymorphisms and tre

215 tion to ADAR1, mammalian cells have a second ADAR, named ADAR2; the deamination specificity of this e

216 the HDV amber/W site represents the smallest ADAR substrate yet identified.

217 hat might control nuclear import of specific ADARs and, in turn, nuclear RNA editing.

218 on via an adenosine deaminase, RNA-specific (ADAR)-like activity.

219 plexes between differentially epitope-tagged ADAR monomers by sequential affinity chromatography and

220 We conclude that ADAR-mediated editing is more widespread than previously

221 es of cancer transcriptomes demonstrate that ADAR (adenosine deaminase, RNA-specific)-mediated RNA ed

222 tive in an editing assay, demonstrating that ADAR is only active as a dimer.

223 bind and edit its substrate, indicating that ADAR dimers require two subunits with functional dsRBDs

224 role for ADAR and raise the possibility that ADAR mediates the differential expression characteristic

225 Here, we show that ADAR proteins can affect RNA processing independently of

226 Here we demonstrate that ADARs are not required for RNA interference (RNAi) and t

227 Our data indicate that ADARs, through both direct and indirect mechanisms, are

228 Here, we show that ADARs also react with DNA/RNA hybrid duplexes.

229 Early studies showed that ADARs preferentially target adenosines with certain 5' a

230 n at C6 of adenosine in RNA catalyzed by the ADAR enzymes generates inosine at the corresponding posi

231 y distinct tissue-specific regulation by the ADAR enzymes in vivo.

232 structures that lead to hyperediting by the ADAR enzymes, and at least 333 human genes contain such

233 eosides to inosine (A-to-I), mediated by the ADAR family of enzymes.

234 ine structure/activity relationships for the ADAR reaction.

235 The members of the ADAR (adenosine deaminase acting on RNA) gene family are

236 One or several members of the ADAR (adenosine deaminases that act on RNA) family are t

237 tudies provide a deeper understanding of the ADAR catalytic domain-RNA interaction and new tools for

238 osine deaminase human ADAT1, a member of the ADAR family of RNA editing enzymes.

239 nd characterized human genomic clones of the ADAR gene and cDNA clones encoding splice site variants

240 clones encoding splice site variants of the ADAR protein.

241 muscles by enhancing the degradation of the ADAR proteins.

242 ites are useful for defining features of the ADAR reaction mechanism.

243 al, thermodynamic and kinetic studies of the ADAR-2 reaction.

244 derstanding of the chemical mechanism of the ADAR-catalyzed adenosine deamination in RNA is lagging.

245 serine to glycine substitution close to the ADAR active site.

246 similarities and differences in the way the ADARs recognize the edited nucleotide.

247 Therefore, ADAR and differentially edited transcripts may be promis

248 The catalytic domain of all three ADAR gene family members is very similar to that of Esch

249 Vertebrates have two ADAR-editing enzymes that are catalytically active; ADAR

250 amined the role of A-to-I RNA editing by two ADARs, ADAR1 and ADAR2, in the sensing of self-RNA in th

251 The wild-type ADAR-a, -b, and -c proteins all possessed comparable dou

252 n brain and identified 19 previously unknown ADAR substrates.

253 mental verification of 16 previously unknown ADAR target genes in the fruit fly Drosophila and one in

254 nd also internal modifications or variation (ADAR editing or single nucleotide polymorphisms).

255 trate that ADAR2, a member of the vertebrate ADAR family, is concentrated in the nucleolus, a subnucl

256 Three vertebrate ADAR gene family members, ADAR1, ADAR2, and ADAR3, have

257 ptic and autistic conditions, and vertebrate ADARs may have a relevant evolutionarily conserved contr

258 utionary ancestor of the multiple vertebrate ADARs.

259 ropose a model for ADAR dimerization whereby ADAR monomers first contact dsRNA; however, it is only w

260 ificity, and aid in efforts to predict which ADAR deaminates a given editing site adenosine in vivo.

261 erved at least two additional means by which ADARs can suppress HDV replication.

262 fied substrates of other organisms, in which ADARs target codons.

263 ting activity does not always correlate with ADAR expression levels, suggesting posttranscriptional o

264 vestigated the role of internal loops within ADAR substrates.

265 rmation about how secondary structure within ADAR substrates dictates selectivity, and suggests a rat