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 gene expression and copy number variation were meas

4 ADAR mRNA was significantly overexpressed in the tumor t

5 ADAR overexpression and amplification were significantly

6 ADAR proteins alter gene expression both by catalyzing a

7 ADAR RNA editing enzymes are high-affinity dsRNA-binding

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

9 ADARs are adenosine deaminases responsible for RNA editi

10 ADARs are adenosine deaminases responsible for RNA-editi

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

12 ADARs are also important in the development of directed

13 ADARs are also interesting in regard to the remarkable d

14 ADARs are essential for normal mammalian development, an

15 ADARs are essential in mammals and are particularly impo

16 ADARs are modular enzymes with multiple double-stranded

17 ADARs are RNA editing enzymes that target double-strande

18 ADARs capable of editing biologically relevant RNA subst

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

20 ADARs interact with Dicer to augment the processing of p

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

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

23 Also, ADAR expression level in stage IV was higher than stage

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

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

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

27 orted by single-cell RNA sequencing data and ADAR perturbation experiments in cell culture.

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

29 1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, and ADAR).

30 everal ISG including RIG-I, IRF7, STAT1, and ADAR-p150.

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

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

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

34 acting on RNA (ADAR) enzymes with associated ADAR guide RNAs (adRNAs).

35 and there was a positive correlation between ADAR copy number and expression.

36 to substrate specificity differences between ADAR family members.

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

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

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

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

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

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

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

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

45 o-inosine (A-to-I) RNA editing, catalyzed by ADAR enzymes, is a ubiquitous mechanism that generates t

46 mplications for the human diseases caused by ADAR mutations.

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

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

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

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

51 R, are required for the lethality induced by ADAR depletion.

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

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

54 after infection, suggesting modification by ADAR.

55 The central role played by ADAR, both as an enzyme and as a scaffold, sets it as a

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

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

58 hydrolytic deamination reaction catalyzed by ADARs.

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

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

61 specifically targets dsRNAs hyper-edited by ADARs.

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

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

64 Using RNA duplexes recognized by ADARs as readout of pre-messenger RNA structures, we rev

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

66 nd endogenous viral elements are silenced by ADARs [adenosine deaminases acting on double-stranded RN

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

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

69 We identified a highly conserved ADAR dimerization interface and validated the importance

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

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

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

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

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

75 DAR reaction will advance efforts to develop ADAR inhibitors and new tools for directed RNA editing.

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

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

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

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

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

81 ing by adenosine deaminases acting on dsRNA (ADAR) has become of increasing medical relevance, partic

82 zymes, adenosine deaminases acting on dsRNA (ADARs).

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

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

85 two functionally distinct human RNA editing ADARs.

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

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

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

89 roach we call RESTORE (recruiting endogenous ADAR to specific transcripts for oligonucleotide-mediate

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

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

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

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

94 BP fused to a Drosophila RNA editing enzyme (ADAR) to globally map the mRNA targets of the RBP MSI2 i

95 and FXR1P interact with RNA-editing enzymes (ADAR proteins) and modulate A-to-I editing.

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

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

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

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

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

101 ist in the rational design of guide RNAs for ADAR-mediated RNA base editing.

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

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

104 nsistent with known sequence preferences for ADARs.

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

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

107 systematically engineered adRNAs to harness ADARs, and comprehensively evaluated the specificity and

108 s RNA editing enzymes or of endogenous human ADAR (adenosine deaminase acting on RNA) enzymes.

109 SH to map RNA substrates recognized by human ADARs and uncover features that determine their binding

110 igonucleotides that recruit endogenous human ADARs to edit endogenous transcripts in a simple and pro

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

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

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

114 Despite their importance, ADAR RNA substrates have not been mapped extensively in

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

116 40% of patients showed amplification in ADAR gene and there was a positive correlation between A

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

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

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

120 defining structure-function relationships in ADAR reactions.

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

122 ity to infer RNA editing patterns, including ADAR editing, and inclusion of Guttman scale patterns fo

123 Increased ADAR expression was clearly correlated with poorer survi

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

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

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

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

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

129 eamination mechanisms distinct from metazoan ADARs.

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

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

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

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

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

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

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

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

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

139 Our transcriptome-wide atlas of ADAR substrates and the features governing RNA editing o

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

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

142 ased results show importance of diversity of ADAR isoforms, key RNA editing enzymes linked with the i

143 at amplification leads to over expression of ADAR and it could be used as a prognostic biomarker for

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

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

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

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

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

149 Here, we report a high level of ADAR-mediated RNA editing in the bumblebee, despite the

150 king differences in the expression levels of ADAR genes.

151 ve cancer cells are sensitive to the loss of ADAR, a dsRNA-editing enzyme that is also an ISG.

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

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

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

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

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

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

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

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

160 gs offer insights into the potential role of ADAR editing dysregulation in the disease mechanisms, in

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

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

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

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

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

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

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

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

169 coincide with observed expression levels of ADARs.

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

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

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

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

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

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

176 xpected to accelerate mechanistic studies of ADARs.

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

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

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

180 dentify a molecular mechanism that regulates ADAR substrate recognition and editing efficiency.

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

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

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

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

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

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

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

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

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

190 ting via adenosine deaminases acting on RNA (ADAR) enzymes with associated ADAR guide RNAs (adRNAs).

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

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

193 er of the adenosine deaminase acting on RNA (ADAR) family, is competing with ADR-2 for binding to spe

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

195 er of the Adenosine Deaminase Acting on RNA (ADAR) protein family, whose active members catalyze A-to

196 9CT) and adenosine deaminases acting on RNA (ADAR)(rs1127309TC) genes were analyzed by real-time PCR.

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

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

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

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

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

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

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

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

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

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

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

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

209 Adenosine Deaminases that act on RNA (ADARs) are enzymes that catalyze adenosine to inosine co

210 Adenosine deaminases acting on RNA (ADARs) are enzymes that convert adenosine to inosine in

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

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

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

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

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

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

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

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

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

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

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

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

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

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

225 Adenosine deaminases acting on RNA (ADARs) convert adenosine to inosine in double-stranded R

226 Adenosine deaminases acting on RNA (ADARs) convert adenosines to inosines in double-stranded

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

247 ing enzyme adenosine deaminase RNA specific (ADAR), the RNase DICER1, and the dsRNA-activated kinase

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

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

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

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

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

253 Moreover, we unexpectedly discovered that ADAR proteins bind dsRNA substrates tandemly in vivo, ea

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

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

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

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

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

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

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

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

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

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

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

265 ine structure/activity relationships for the ADAR reaction.

266 The activation of retrotransposons in the ADAR- and ERI-6/7/MOV10-defective mutant is associated w

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

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

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

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

271 expression and copy number variation of the ADAR gene in advanced GC and clarify its correlation wit

272 muscles by enhancing the degradation of the ADAR proteins.

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

274 erstanding of the molecular mechanism of the ADAR reaction will advance efforts to develop ADAR inhib

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

276 Therapeutic approaches focusing on the ADAR p150 isoform and its Z-DNA- and Z-RNA-specific Zalp

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

278 o palindromic repeats are independent of the ADARs and ERI-6/7, and are in fact increased in adar- an

279 not to DNA transposons, are dependent on the ADARs and ERI-6/7.

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

281 Therefore, ADAR and differentially edited transcripts may be promis

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

283 rendering ISG-positive tumors susceptible to ADAR loss.

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

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

286 n brain and identified 19 previously unknown ADAR substrates.

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

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

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

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

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

292 utionary ancestor of the multiple vertebrate ADARs.

293 ese tumor-intrinsic responses, with in vitro ADAR dependency varying by tumor type (range 11-80%).

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

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

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

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

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

299 dominance of long-range interactions within ADAR substrates and analyze differences between ADAR1 an

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