ライフサイエンスコーパス: arginine methyltransferase

1 s activity as the prototype type III protein arginine methyltransferase.

2 ated an enzyme-dead knock-in of this protein arginine methyltransferase.

3 s impaired and is proposed to function as an arginine methyltransferase.

4 ally interacts with PRMT1, the major protein arginine methyltransferase.

5 product specificity displayed by the protein-arginine methyltransferases.

6 on of an array of substrates for the protein arginine methyltransferases.

7 tinguishes PRMT7 from all of the other known arginine methyltransferases.

8 ginine methylation mediated by the family of arginine methyltransferases.

9 ase, and is derived by the action of protein-arginine-methyltransferases.

10 subject to E2-induced coactivator-associated arginine methyltransferase 1 (CARM1) action are critical

11 ctly associated with co-activator-associated arginine methyltransferase 1 (CARM1) activity.

12 ic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its co

13 cells by the methyltransferases coactivator arginine methyltransferase 1 (CARM1) and protein arginin

14 Here we identify co-activator-associated arginine methyltransferase 1 (CARM1) as a crucial compon

15 The histone coactivator-associated arginine methyltransferase 1 (CARM1) is a coactivator fo

16 Coactivator-associated arginine methyltransferase 1 (CARM1) is a dual functiona

17 Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the

18 PRMT4 or coactivator-associated arginine methyltransferase 1 (CARM1) is a propitious tar

19 Coactivator-associated arginine methyltransferase 1 (CARM1) is a protein argini

20 Coactivator-associated arginine methyltransferase 1 (CARM1) is a protein methyl

21 Co-activator-associated arginine methyltransferase 1 (CARM1) is subjected to mul

22 Here we show that coactivator-associated arginine methyltransferase 1 (CARM1) methylates Arg 754

23 ere, we identify that coactivator-associated arginine methyltransferase 1 (CARM1) methylates Pontin c

24 Coactivator-associated arginine methyltransferase 1 (CARM1), a coactivator for

25 one such cofactor as coactivator-associated arginine methyltransferase 1 (CARM1), a unique coactivat

26 substrates induced by coactivator-associated arginine methyltransferase 1 (CARM1), both in in vitro a

27 eta-catenin cofactor, coactivator-associated arginine methyltransferase 1 (CARM1), providing insight

28 Coactivator-associated arginine methyltransferase 1 (CARM1), the histone argini

29 demonstrate that the coactivator-associated arginine methyltransferase 1 (CARM1), which methylates h

30 Coactivator-associated arginine methyltransferase 1 (CARM1)-mediated histone me

31 ginine (R1810) by the coactivator-associated arginine methyltransferase 1 (CARM1).

32 enzymatic coactivator coactivator-associated arginine methyltransferase 1 (CARM1).

33 lycogen synthase kinase 3 (GSK3) and protein arginine methyltransferase 1 (PRMT-1) cooperate to orche

34 We recently reported defects in protein arginine methyltransferase 1 (PRMT1) activity and argini

35 Protein arginine methyltransferase 1 (PRMT1) acts as a transcrip

36 2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetric dimet

37 Here we identified the type I protein arginine methyltransferase 1 (PRMT1) as a restrictive fa

38 Protein arginine methyltransferase 1 (PRMT1) catalyzes the mono-

39 Protein arginine methyltransferase 1 (PRMT1) catalyzing the form

40 activity of RIP140 was suppressed by protein arginine methyltransferase 1 (PRMT1) due to RIP140 methy

41 of the EGFR extracellular domain by protein arginine methyltransferase 1 (PRMT1) enhances binding to

42 Protein arginine methyltransferase 1 (PRMT1) is a key regulator

43 Protein arginine methyltransferase 1 (PRMT1) is an essential enz

44 Protein arginine methyltransferase 1 (PRMT1) is involved in many

45 Here, we report that protein arginine methyltransferase 1 (PRMT1) is required for the

46 Protein Arginine methyltransferase 1 (PRMT1) is the main enzyme

47 Protein arginine methyltransferase 1 (PRMT1) is up-regulated in

48 d receptor coactivator 1 (SRC1), and protein arginine methyltransferase 1 (PRMT1) only modestly incre

49 e major arginine methylation enzyme, protein arginine methyltransferase 1 (PRMT1) strictly generates

50 Here, we show protein arginine methyltransferase 1 (PRMT1), a key enzyme that

51 tentiated by arginine methylation by protein arginine methyltransferase 1 (PRMT1), another nuclear re

52 class 1 arginine methyltransferase, protein arginine methyltransferase 1 (PRMT1), regulates nucleocy

53 Protein arginine methyltransferase 1 (PRMT1), the predominant ar

54 nt signaling through the activity of protein arginine methyltransferase 1 (PRMT1), which transfers on

55 ntation to label substrates of human protein arginine methyltransferase 1 (PRMT1).

56 of a peptide substrate by the enzyme protein arginine methyltransferase 1 (RMT1).

57 ating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PRMT5).

58 s as an enhancer for the assembly of protein arginine methyltransferase 1 and the protein arginine me

59 tein methylation and coexpression of protein arginine methyltransferase 1 did not influence Nox activ

60 When protein-arginine methyltransferase 1 expression was reduced by s

61 Protein-arginine methyltransferase 1 has much less effect on MHC

62 s subject to arginine methylation by protein arginine methyltransferase 1 in vitro and in vivo.

63 ic dimethyl H4R3 catalyzed by PRMT1 (protein arginine methyltransferase 1) facilitates histone H3 ace

64 hyltransferase CARM1 (coactivator-associated arginine methyltransferase 1) promotes the nuclear expor

65 hyltransferase CARM1 (coactivator-associated arginine methyltransferase 1).

66 a novel AE9a binding partner PRMT1 (protein arginine methyltransferase 1).

67 the methyltransferase coactivator-associated arginine methyltransferase 1, CARM1.

68 protein K (hnRNP K) protein by human protein arginine methyltransferase 1, variant 1 (hPRMT1v1), in j

69 EYA1 physically interacts with protein arginine methyltransferase 1, which methylates EYA1 at t

70 arginine methyltransferase 1 and the protein arginine methyltransferase 1-linked histone 4 arginine 3

71 tase-transcription activator EYA1 by protein arginine methyltransferase 1: mechanistic, functional, a

72 We found that both protein-arginine methyltransferases 1 and 5 methylate Arg-296 wi

73 e protein expression was reduced and protein-arginine-methyltransferase-1 increased in alcoholic hepa

74 tor, beta-catenin and coactivator-associated-arginine-methyltransferase-1.

75 Protein arginine methyltransferase 10 (PRMT10) is a type I argin

76 The mammalian protein arginine methyltransferase 3 (PRMT3) catalyzes the forma

77 ocardial infarction, the PRMT3 gene (protein arginine methyltransferase 3) with stroke, and the LHFPL

78 rt a novel regulation of pRb through protein arginine methyltransferase 4 (PRMT4)-mediated arginine m

79 We have identified a mutant, protein arginine methyltransferase 5 (atprmt5), that fails to fl

80 P) confers a selective dependence on protein arginine methyltransferase 5 (PRMT5) and its binding par

81 requires assembly factors united in protein arginine methyltransferase 5 (PRMT5) and survival motor

82 characterization of a complex of the protein arginine methyltransferase 5 (Prmt5) and the methylosome

83 PDCD4 in breast cancer and identify protein arginine methyltransferase 5 (PRMT5) as a cofactor that

84 e describe the identification of the protein arginine methyltransferase 5 (PRMT5) as an effector recr

85 on and mass spectrometry to identify protein arginine methyltransferase 5 (PRMT5) as part of the p38d

86 Protein arginine methyltransferase 5 (PRMT5) catalyzes symmetric

87 Protein arginine methyltransferase 5 (PRMT5) catalyzes the symme

88 Protein arginine methyltransferase 5 (PRMT5) complexed with MEP5

89 Here we demonstrate that protein arginine methyltransferase 5 (PRMT5) functions as an epi

90 The aberrant expression of protein arginine methyltransferase 5 (PRMT5) has been associated

91 Protein arginine methyltransferase 5 (PRMT5) has emerged as a pr

92 ve feedback loop between BCR-ABL and protein arginine methyltransferase 5 (PRMT5) in CML cells.

93 Protein arginine methyltransferase 5 (PRMT5) is a key epigenetic

94 Protein arginine methyltransferase 5 (PRMT5) is an arginine meth

95 Protein arginine methyltransferase 5 (PRMT5) is an emerging epig

96 e suggest that the methyltransferase protein arginine methyltransferase 5 (PRMT5) is responsible for

97 Protein arginine methyltransferase 5 (PRMT5) is the major methyl

98 kinases (M6CKs) bind subunits of the protein arginine methyltransferase 5 (PRMT5) molecular complex t

99 Protein arginine methyltransferase 5 (PRMT5) plays multiple role

100 uppressor, but its coexpression with protein arginine methyltransferase 5 (PRMT5) promotes accelerate

101 rmation to document the relevance of protein arginine methyltransferase 5 (PRMT5) to regulation of ep

102 Menin directly interacts with protein arginine methyltransferase 5 (PRMT5), a negative regulat

103 Protein arginine methyltransferase 5 (PRMT5), a protein arginine

104 Here, we report that protein arginine methyltransferase 5 (PRMT5), an enzyme that cat

105 ar ribonucleoprotein D3b (SmD3b) and protein arginine methyltransferase 5 (PRMT5), which are required

106 tion through an association with the protein arginine methyltransferase 5 (PRMT5).

107 dimethylated on arginine 30 (R30) by protein-arginine methyltransferase 5 (PRMT5).

108 eraction between NF-kappaB, YBX1 and protein arginine methyltransferase 5 (PRMT5).

109 uirement for arginine methylation by protein arginine methyltransferase 5 (PRMT5).

110 anslational methylation at Arg-57 by protein arginine methyltransferase 5 (PRMT5).

111 genetic analysis we demonstrate that protein arginine methyltransferase 5 (PRMT5; At4g31120) is a cri

112 F-1 is directly methylated by PRMT5 (protein arginine methyltransferase 5), and that arginine methyla

113 Protein arginine methyltransferase-5 (PRMT5) is overexpressed in

114 e known Ajuba binding partner Prmt5 (protein arginine methyltransferase-5) inhibited the Ajuba/RAR in

115 nine methyltransferase 1 (CARM1) and protein arginine methyltransferase 6 (PRMT6) in vitro and in viv

116 Protein arginine methyltransferase 6 (PRMT6) is a nuclear enzyme

117 We show here that protein arginine methyltransferase 6 (PRMT6) is a specific co-ac

118 Protein arginine methyltransferase 6 (PRMT6) plays important rol

119 Protein arginine methyltransferase 7 (PRMT7) catalyzes the intro

120 Full-length human protein arginine methyltransferase 7 (PRMT7) expressed as a fusi

121 The mammalian protein arginine methyltransferase 7 (PRMT7) has been implicated

122 Here, we show that the protein arginine methyltransferase 7 (PRMT7) is a pluripotent fa

123 Protein arginine methyltransferase 7 (PRMT7) methylates arginine

124 ssociated with blunted expression of protein arginine methyltransferase 7 (Prmt7) on chromosome 8, a

125 The protein arginine methyltransferase 7 (PRMT7), but not PRMT5, rep

126 ound that the selective inhibitor of protein arginine methyltransferases 7,7'-carbonylbis(azanediyl)b

127 Here we use mice lacking protein arginine methyltransferase 8 (PRMT8) in the brain to exa

128 The multifunctional protein arginine methyltransferase 8 (PRMT8) possesses both meth

129 ide an example for the regulation of protein arginine methyltransferase activity by phosphorylation.

130 identical to human PRMT1, the major protein arginine methyltransferase activity in mammalian cells.

131 recruitment of CARM1 not only adds a protein arginine methyltransferase activity to the ER-coactivato

132 Protein-arginine methyltransferases aid in the regulation of man

133 stingly, loss of PRMT1, the major asymmetric arginine methyltransferase, also sensitizes cells to PRM

134 ine methyltransferase 1 (CARM1), the histone arginine methyltransferase and coactivator for many tran

135 strate that the activity of PRMT5, a protein arginine methyltransferase and indirect target of CDK4,

136 PRMT3 as the first type I ribosomal protein arginine methyltransferase and suggest that it regulates

137 icity and the catalytic mechanism of protein arginine methyltransferases and have important implicati

138 Cell, comprehensively examined the nature of arginine methyltransferases and histone modifications in

139 Thus, distinct arginine methyltransferases are employed at different ti

140 Multiple protein arginine methyltransferases are involved in transcriptio

141 showed that the Arabidopsis thaliana protein arginine methyltransferase AtPRMT3 regulates pre-rRNA pr

142 methyltransferase 1 (PRMT1), the predominant arginine methyltransferase, can act as a transcriptional

143 K6/K16 repression involved beta-catenin and arginine methyltransferase (CARM-1) acting as co-repress

144 how one mechanism of such regulation via the arginine methyltransferase CARM1 (coactivator-associated

145 The arginine methyltransferase CARM1 (coactivator-associated

146 prediction by overexpressing the H3-specific arginine methyltransferase CARM1 in individual blastomer

147 The coactivator-associated arginine methyltransferase CARM1 is a positive regulator

148 The coactivator-associated arginine methyltransferase CARM1 is recruited by many di

149 Finally, we show that the arginine methyltransferase CARM1 methylates BAF155, whic

150 ed the requirement for Prmt5 and the class I arginine methyltransferase Carm1/Prmt4 in the temporal c

151 found that a small molecule inhibitor of the arginine methyltransferases CARM1 and PRMT6 was able to

152 one methyltransferase coactivator-associated arginine methyltransferase (CARM1) depends on the methyl

153 Coactivator-associated arginine methyltransferase (CARM1) is a transcriptional

154 ne methyltransferase, coactivator-associated arginine methyltransferase (CARM1/PRMT4), during IFN-gam

155 Coactivator-associated arginine methyltransferase (CARM1/PRMT4)-mediated transc

156 The coactivator-associated arginine methyltransferase, CARM1, is a positive regulat

157 Both arginine methyltransferases could bind to and modify his

158 anscription and synergy is abrogated when an arginine methyltransferase-defective CARM1 mutant is use

159 on of PAPI to the nuage does not require the arginine methyltransferase dPRMT5 or AGO3.

160 Protein arginine methyltransferase enzyme 5 (PRMT5) regulates ma

161 We identify the protein arginine methyltransferase enzymes that catalyze this mo

162 Our data suggest that protein arginine methyltransferases exert key regulatory roles i

163 four other representative histone lysine and arginine methyltransferases, G9a, SUV39H1, PRMT1 and CAR

164 The approach revealed protein arginine methyltransferase gene 5 (PRMT5) as an effectiv

165 Prmt5, an arginine methyltransferase, has multiple roles in germ c

166 cetylases, BET bromodomain proteins, protein arginine methyltransferases, histone lysine methyltransf

167 Here we demonstrate a role for the protein arginine methyltransferase Hmt1 in this process.

168 Previously, we demonstrated that the protein arginine methyltransferase Hmt1 plays a role in the form

169 Coactivator-associated arginine methyltransferase I (CARM1; PRMT4) regulates ge

170 Liao et al. investigate the role of protein arginine methyltransferase I (PRMT1) in regulating EGFR

171 an important functional role of this histone arginine methyltransferase in reprogramming ERalpha-regu

172 Hmt1 is the major type I arginine methyltransferase in the yeast Saccharomyces ce

173 These studies suggest that arginine methyltransferases may be important for hypoxic

174 Our data show that Hmt1, the major type I arginine methyltransferase, methylates Snp1, a U1 small

175 ich is catalyzed by a family of nine protein arginine methyltransferases, or PRMTs.

176 It is the first to demonstrate that protein arginine methyltransferases participate in the DNA methy

177 ted on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG

178 Protein arginine methyltransferase (PRMT) 8 is unique among the

179 Human protein arginine methyltransferase (PRMT) 9 symmetrically dimeth

180 Protein arginine methyltransferase (PRMT) activity has been impl

181 CARM1 contains a conserved protein arginine methyltransferase (PRMT) catalytic core flanked

182 However, a conclusive role for the protein arginine methyltransferase (PRMT) enzymes that catalyze

183 sferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates

184 e completely conserved in the type I protein arginine methyltransferase (PRMT) family of enzymes.

185 A1b proteins by three members of the protein arginine methyltransferase (PRMT) family: PRMT1, PRMT3,

186 CARM1 is a protein arginine methyltransferase (PRMT) that acts as a coactiv

187 panosoma brucei PRMT7 (TbPRMT7) is a protein arginine methyltransferase (PRMT) that strictly monometh

188 AtPRMT5 encodes a type II protein arginine methyltransferase (PRMT) that, in winter-annual

189 ctrometry identified LRP6 binding to protein arginine methyltransferase (PRMT)-1, and nuclear asymmet

190 Protein Arginine Methyltransferases (PRMT) 1 and 5 dimethylate t

191 d colleagues demonstrate that type I protein arginine methyltransferases (PRMT) are directly involved

192 Protein arginine methyltransferases (PRMT) are generally not mut

193 oter through the interaction of YY1 with the arginine methyltransferase PRMT1 and evidence of its act

194 lls induced rapid ERalpha methylation by the arginine methyltransferase PRMT1 and triggered the bindi

195 Here, we have identified the arginine methyltransferase PRMT1 as a coactivator for HN

196 h an shRNA screen, we identified the protein arginine methyltransferase Prmt1 as a vulnerable interve

197 tified as inhibitors against the predominant arginine methyltransferase PRMT1 within micromolar poten

198 RUNX1 is arginine-methylated in vivo by the arginine methyltransferase PRMT1, and that PRMT1 serves

199 ignaling increased expression of the protein arginine methyltransferase PRMT1, which in turn methylat

200 , RACO-1 is identified as a substrate of the arginine methyltransferase PRMT1, which methylates RACO-

201 te (1) the additional involvement of protein arginine methyltransferases PRMT1 and CARM1 in p53 funct

202 how that S-HDAg can be methylated by protein arginine methyltransferase (PRMT1) in vitro and in vivo.

203 uman genome encodes a family of nine protein arginine methyltransferases (PRMT1-9), whose members can

204 re-activated mouse models of three different arginine methyltransferases, PRMT1, CARM1, and PRMT6, wh

205 beta-catenin recruits the arginine methyltransferase Prmt2 to target promoters, th

206 m an extraribosomal complex with the protein arginine methyltransferase PRMT3 that is conserved from

207 tional analysis, we demonstrate that protein arginine methyltransferase PRMT4 (CARM1) methylates TP2

208 Here we identify the arginine methyltransferase PRMT5 as a key regulator of h

209 the selective overexpression of the protein arginine methyltransferase PRMT5 as a novel candidate th

210 ponents and identify the ortholog of protein arginine methyltransferase PRMT5 as the enzyme responsib

211 d enhanced expression of the type II protein arginine methyltransferase PRMT5 as well as the polycomb

212 The major type II protein arginine methyltransferase PRMT5 catalyzes the formation

213 Here, we show that the type-II protein arginine methyltransferase PRMT5 controls H4R3me2s in mo

214 Here, we report that the arginine methyltransferase PRMT5 has a crucial role in m

215 Protein arginine methyltransferase PRMT5 interacts with human SW

216 g the target genes, we confirmed the protein arginine methyltransferase Prmt5 is a direct target that

217 Taken together, we uncovered that arginine methyltransferase PRMT5 is a major pro-survival

218 The protein arginine methyltransferase PRMT5 is complexed with the W

219 In this study, we show that the arginine methyltransferase PRMT5 is critical for CXCL10

220 of Cancer Cell, Braun et al. report that the arginine methyltransferase PRMT5 is critical for tumor c

221 The type II arginine methyltransferase PRMT5 is responsible for the

222 The type II protein arginine methyltransferase Prmt5 symmetrically dimethyla

223 Grg4 recruits the arginine methyltransferase PRMT5 to chromatin resulting

224 histone acetyltransferase 1 and the histone arginine methyltransferase PRMT5 was decreased by 17AAG.

225 The arginine methyltransferase Prmt5 was required for loop f

226 We previously demonstrated that the class II arginine methyltransferase Prmt5 was required for skelet

227 ells is impaired by depletion of the protein arginine methyltransferase PRMT5.

228 ly relevant ERG interactors, we identify the arginine methyltransferase PRMT5.

229 Epigenetic regulation by the type II protein arginine methyltransferase, PRMT5, plays an essential ro

230 functionally analyzed two different protein arginine methyltransferases, Prmt5 and Prmt4, both of wh

231 rom degradation, with methylation of GPS2 by arginine methyltransferase PRMT6 regulating the interact

232 Human protein arginine methyltransferase PRMT8 has been recently descr

233 oexpression of Nav1.2 with the primary brain arginine methyltransferase PRMT8 led to a surprising 3-f

234 ng flagellar dynamics, we focused on protein arginine methyltransferases (PRMTs) 1, 3, 5, and 10.

235 Protein arginine methyltransferases (PRMTs) affect many processe

236 Protein arginine methyltransferases (PRMTs) aid in the regulatio

237 s methylated on arginine residues by protein arginine methyltransferases (PRMTs) and is degraded by d

238 Protein arginine methyltransferases (PRMTs) are (S)-adenosylmeth

239 The protein arginine methyltransferases (PRMTs) are a family of enzy

240 Protein arginine methyltransferases (PRMTs) are a family of enzy

241 Protein arginine methyltransferases (PRMTs) are a group of eukar

242 The arginine methyltransferases (PRMTs) are envisaged as pro

243 Protein arginine methyltransferases (PRMTs) are enzymes that are

244 haracterized selective inhibitors of protein arginine methyltransferases (PRMTs) are invaluable chemi

245 Protein arginine methyltransferases (PRMTs) are proved to play v

246 Protein arginine methyltransferases (PRMTs) are SAM-dependent en

247 Protein arginine methyltransferases (PRMTs) catalyze arginine me

248 Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric

249 Misregulation of protein arginine methyltransferases (PRMTs) has been linked to m

250 Protein arginine methyltransferases (PRMTs) have emerged as attr

251 Covalent modification of histones by protein arginine methyltransferases (PRMTs) impacts genome organ

252 sine methyltransferases (HKMTs), and protein arginine methyltransferases (PRMTs) in pancreatic alpha-

253 The protein arginine methyltransferases (PRMTs) include a family of

254 Protein arginine methyltransferases (PRMTs) introduce arginine m

255 Arginine methylation by protein N-arginine methyltransferases (PRMTs) is an important post

256 Malfunction of protein arginine methyltransferases (PRMTs) is correlated with m

257 genetic modification of chromatin by protein arginine methyltransferases (PRMTs) is crucial for norma

258 Protein arginine methyltransferases (PRMTs) mediate the transfer

259 Protein arginine methyltransferases (PRMTs) play an important ro

260 Protein arginine methyltransferases (PRMTs) play important roles

261 Protein arginine methyltransferases (PRMTs) regulate many physio

262 Protein arginine methyltransferases (PRMTs) represent an emergin

263 ification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs) that are typically t

264 In the family of protein arginine methyltransferases (PRMTs) that predominantly g

265 ginine, mediated by PRMT5 and type I protein arginine methyltransferases (PRMTs), respectively, reduc

266 Consequently protein arginine methyltransferases (PRMTs), the writers of argi

267 Using purified recombinant protein arginine methyltransferases (PRMTs), we showed that the

268 es aimed at blocking the activity of protein arginine methyltransferases (PRMTs), which catalyze the

269 ysine methyltransferases (PKMTs) and protein arginine methyltransferases (PRMTs).

270 play between the SWI/SNF complex and protein-arginine methyltransferases (PRMTs).

271 e methyltransferases (PKMTs) and the protein arginine methyltransferases (PRMTs).

272 of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs).

273 ed Rossman-fold enzymes that include protein arginine methyltransferases (PRMTs).

274 c arginine methylation of FUS by the class 1 arginine methyltransferase, protein arginine methyltrans

275 on of protein methyltransferases, especially arginine methyltransferases, relieve the repression of E

276 Depletion of PRMT5, the primary protein arginine methyltransferase responsible for symmetric arg

277 and colleagues report that CARM1, a protein arginine methyltransferase, specifically methylates BAF1

278 The major Trypanosoma brucei protein arginine methyltransferase, TbPRMT1 enzyme (ENZ), requir

279 tion of the major trypanosome type 1 protein arginine methyltransferase, TbPRMT1, disrupts formation

280 The protein arginine methyltransferase, TbPRMT1, interacts with DRBD

281 PRMT5 is an arginine methyltransferase that accounts for the vast ma

282 ooperate with PRMT1, a CARM1-related protein arginine methyltransferase that also functions as an NR

283 C1 recruits the chromatin modifier PRMT5, an arginine methyltransferase that catalyzes symmetric dime

284 PRMT5 encodes a type II protein arginine methyltransferase that catalyzes the symmetric

285 inine methyltransferase 5 (PRMT5), a protein arginine methyltransferase that catalyzes the symmetrica

286 PRMT5 was the only arginine methyltransferase that coprecipitated with p65,

287 ne methyltransferase 10 (PRMT10) is a type I arginine methyltransferase that is essential for regulat

288 PRMT8 is thus an active arginine methyltransferase that is membrane-associated a

289 ine methyltransferase 1 (CARM1) is a protein arginine methyltransferase that methylates histones and

290 PRMT3 is a type I arginine methyltransferase that resides in the cytoplasm

291 PRMT5 is an arginine methyltransferase that symmetrically dimethylat

292 n arginine methyltransferase 5 (PRMT5) is an arginine methyltransferase that symmetrically dimethylat

293 CARM1 is one of nine protein arginine methyltransferases that methylate arginine resi

294 we show that UHRF1 interacts with PRMT5, an arginine methyltransferase, to regulate the repressive h

295 We found that PRMT5, an arginine methyltransferase, translocates from the cytopl

296 ates suggest that type I and type II protein-arginine methyltransferases use distinct molecular deter

297 ly modulates enzymatic activity of a protein arginine methyltransferase vital to abiotic stress toler

298 IL-4 upregulates the expression of protein arginine methyltransferases, which are essential for ADM

299 CARM1 is an arginine methyltransferase with diverse histone and non-

300 PRMT5 is a type II protein arginine methyltransferase with roles in stem cell biolo