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

1 tors PRMT1 and CARM1 (coactivator-associated arginine methyltransferase).

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

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

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

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

6 ail and allows it to act as a more efficient arginine methyltransferase.

7 -specific methyltransferase PRMT1, a protein arginine methyltransferase.

8 n kinase, and by Hsl7, a presumptive protein-arginine methyltransferase.

9 inine methyltransferase 1 (CARM1), a protein-arginine methyltransferase.

10 product specificity displayed by the protein-arginine methyltransferases.

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

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

13 into the structure and catalysis of protein arginine methyltransferases.

14 ginine methylation mediated by the family of arginine methyltransferases.

15 substrate for yeast Hmt1p and human HRMT1L2 arginine methyltransferases.

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

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

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

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

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

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

22 Methylation of KIX by coactivator-associated arginine methyltransferase 1 (CARM1) blocks CREB activat

23 tion of histone H3 by coactivator-associated arginine methyltransferase 1 (CARM1) has been proposed a

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

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

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

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

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

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

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

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

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

33 fically methylated by coactivator-associated arginine methyltransferase 1 (CARM1), a protein-arginine

34 another coactivator, coactivator-associated arginine methyltransferase 1 (CARM1), a protein-arginine

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

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

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

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

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

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

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

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

43 in methyltransferase, coactivator-associated arginine methyltransferase 1 (CARM1).

44 The coactivator-associated arginine methyltransferase 1 (CARM1/PRMT4) binds the p16

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

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

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

48 2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetric dimet

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

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

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

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

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

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

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

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

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

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

59 In the current study, protein arginine methyltransferase 1 (PRMT1), another arginine-s

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

80 e), a highly effective substrate for protein arginine methyltransferase 1.

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

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

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

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

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

86 two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ERalpha-bi

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

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

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

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

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

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

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

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

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

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

97 Protein arginine methyltransferase 5 (PRMT5) complexed with MEP5

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

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

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

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

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

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

104 Protein arginine methyltransferase 5 (PRMT5) plays multiple role

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

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

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

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

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

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

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

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

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

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

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

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

117 nscriptional system and contains the protein arginine methyltransferase 5, which acts synergistically

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

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

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

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

122 Protein arginine methyltransferase 7 (PRMT7) catalyzes the intro

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

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

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

126 Protein arginine methyltransferase 7 (PRMT7) methylates arginine

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

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

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

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

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

132 +/-), and FDH(-/-) mice have similar protein arginine methyltransferase activities but high, intermed

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

134 I (PRMT1) contributes >90% of type I protein-arginine methyltransferase activity in cells and tissues

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

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

137 In a previous study, this protein arginine methyltransferase activity was identified as an

138 Protein-arginine methyltransferases aid in the regulation of man

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

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

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

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

143 Thus, distinct arginine methyltransferases are employed at different ti

144 Multiple protein arginine methyltransferases are involved in transcriptio

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

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

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

148 The arginine methyltransferase CARM1 (coactivator-associated

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

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

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

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

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

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

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

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

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

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

159 Recent discoveries of protein arginine methyltransferases, CARM1 and PRMT1, as transcr

160 Type I protein arginine methyltransferases catalyze the formation of as

161 ve recently described a large (20 S) protein arginine methyltransferase complex, termed the methyloso

162 Both arginine methyltransferases could bind to and modify his

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

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

165 Protein arginine methyltransferase enzyme 5 (PRMT5) regulates ma

166 t PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in ma

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

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

169 zed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-con

170 Other members of the protein arginine methyltransferase family, which methylate diffe

171 is highly conserved among the entire protein arginine methyltransferase family.

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

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

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

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

176 within its RGG domain by the type I protein-arginine methyltransferase, Hmt1p.

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

178 Protein-arginine methyltransferase I (PRMT1) contributes >90% of

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

180 strate for PRMT1, the most prominent protein-arginine methyltransferase in mammalian cells, which met

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

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

183 ggest a novel mechanism by which the protein arginine methyltransferase is involved in the control of

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

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

186 can be seen as a ternary complex of protein arginine methyltransferase (one subunit) complexed with

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

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

189 inine methyltransferase 1 (CARM1), a protein-arginine methyltransferase previously shown to serve as

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

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

192 Human protein arginine methyltransferase (PRMT) 9 symmetrically dimeth

193 Protein arginine methyltransferase (PRMT) activity has been impl

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

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

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

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

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

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

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

201 r PRMT7, a recently discovered human protein-arginine methyltransferase (PRMT), was cloned and expres

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

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

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

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

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

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

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

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

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

211 was specifically associated with the protein arginine methyltransferases PRMT1 and PRMT5 and that SPT

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

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

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

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

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

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

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

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

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

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

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

223 Protein arginine methyltransferase PRMT5 interacts with human SW

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

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

226 The protein arginine methyltransferase PRMT5 is complexed with the W

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

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

229 The type II arginine methyltransferase PRMT5 is responsible for the

230 The type II protein arginine methyltransferase Prmt5 symmetrically dimethyla

231 Grg4 recruits the arginine methyltransferase PRMT5 to chromatin resulting

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

233 The arginine methyltransferase Prmt5 was required for loop f

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

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

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

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

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

239 Human protein arginine methyltransferase PRMT8 has been recently descr

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

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

242 Protein arginine methyltransferases (PRMTs) affect many processe

243 Protein arginine methyltransferases (PRMTs) aid in the regulatio

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

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

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

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

248 The arginine methyltransferases (PRMTs) are envisaged as pro

249 Protein arginine methyltransferases (PRMTs) are enzymes that are

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

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

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

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

254 Protein arginine methyltransferases (PRMTs) have been implicated

255 Protein arginine methyltransferases (PRMTs) have emerged as attr

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

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

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

259 Protein arginine methyltransferases (PRMTs) introduce arginine m

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

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

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

263 Protein arginine methyltransferases (PRMTs) mediate the AdoMet-d

264 Protein arginine methyltransferases (PRMTs) mediate the transfer

265 Protein arginine methyltransferases (PRMTs) play an important ro

266 Protein arginine methyltransferases (PRMTs) play important roles

267 Protein arginine methyltransferases (PRMTs) represent an emergin

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

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

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

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

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

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

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

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

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

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

281 The protein arginine methyltransferase, TbPRMT1, interacts with DRBD

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

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

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

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

298 Protein arginine methyltransferases, which catalyze the transfer

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