ライフサイエンスコーパス: PRMT

1 PRMTs are a family of proteins that either monomethylate

2 PRMTs are involved in regulating gene expression, RNA sp

3 PRMTs are lost from the flagella of fla10-1 cells, which

4 PRMTs catalyze the transfer of a methyl group from S-ade

5 PRMT1 is the major type 1 PRMT in vivo, thus it is the primary producer of the com

6 Ts produce monomethyl arginine (MMA), type 1 PRMTs go on to form asymmetrically dimethylated arginine

7 3) and protein arginine methyltransferase 1 (PRMT-1) cooperate to orchestrate a series of posttransla

8 PRO is required to complement ENZ to form a PRMT dimer that is necessary, but not sufficient for PRM

9 in a variety of cellular processes, aberrant PRMT activity is associated with several disease states,

10 he PRO structure deviates from other, active PRMTs in that it lacks the conserved eta2 3(10)-helix wi

11 hibitors as well as inhibitors that alkylate PRMTs will be discussed.

12 Although all PRMTs produce monomethyl arginine (MMA), type 1 PRMTs go

13 ave a unique structure and specificity among PRMTs for methylating SF3B2 and potentially other polype

14 xamples have been reported of both PKMTs and PRMTs that are genetically altered in specific human can

15 nown, however, about the role of SWI/SNF and PRMTs in vitamin D receptor (VDR)-mediated transcription

16 , CARM1-mediated delay in tumorigenesis, and PRMTs potentiation of Her2-dependent tumors.

17 Another PRMT, PRMT7, also affects SDMA levels at the same site d

18 d mononucleosomes could be methylated by any PRMTs tested.

19 Subsequent proteomic analysis of both PRMT-inhibited chromatin and chromatin-associated polyad

20 We demonstrate that a major T. brucei PRMT, TbPRMT1, functions as a heterotetrameric enzyme-pr

21 Protein arginine methylation mediated by PRMT enzymes is an important post-translational modifica

22 in priming the substrates for methylation by PRMT enzymes.

23 cumulation occurs via increased synthesis by PRMTs and decreased degradation.

24 The nine characterized PRMT family members are divided into three types dependi

25 ENZ and PRO units adopt the highly-conserved PRMT domain architecture and form an antiparallel hetero

26 Most current PRMT inhibitors display limited specificity and selectiv

27 Attempts to develop PRMT inhibitors using receptor-based computational metho

28 s that have been generated against different PRMT substrates, and can also be used to confirm the pan

29 cleosomal substrate recognition of different PRMT members is not understood.

30 We found that we could distinguish PRMT family members by their sensitivity to these reagen

31 ermal progenitors and the most downregulated PRMT during differentiation.

32 lucidating the substrate specificity of each PRMT will promote a better understanding of which signal

33 itical need for the development of effective PRMT inhibitors as therapeutic intervention.

34 ze such methylation reactions in eukaryotes (PRMTs) works in conjunction with a changing cast of asso

35 T1 was found to be the most highly expressed PRMT in epidermal progenitors and the most downregulated

36 ys automethylation activity; it is the first PRMT to do so.

37 er that is necessary, but not sufficient for PRMT activity.

38 rst demonstration of an obligate heteromeric PRMT, and they suggest that enzyme-prozyme organization

39 ggests an additional functional role for HTT/PRMT interactions, not limited to substrate/enzyme relat

40 This novel human PRMT, which resides solely in the nucleus when fused to

41 Among the nine known human PRMTs, PRMT3 has been implicated in ribosomal biosynthes

42 se fusion protein, PRMT6 demonstrates type I PRMT activity, capable of forming both omega-N(G)-monome

43 ansferase fusion protein of PRMT8 has type I PRMT activity, catalyzing the formation of omega-NG-mono

44 maintaining the holo structure of the type I PRMT catalytic domain.

45 Type I PRMT enzymes catalyze mono- and asymmetric dimethylation

46 ly, Tyr(154) is also conserved in the type I PRMT family of enzymes, suggesting a general role of thi

47 Here, we evaluate the effect of type I PRMT inhibition on arginine methylation in normal human

48 rgistic effects of combined PRMT5 and type I PRMT inhibition, and a mechanistic basis for the therape

49 A1) as a pharmacodynamic biomarker of type I PRMT inhibition.

50 ulated the splicing changes seen with Type I PRMT inhibition.

51 Type I PRMT inhibitor (MS023) or substitution of R95 or R177 wi

52 We also show that the capacity of the type I PRMT inhibitor MS023 to inhibit leukemia cell viability

53 715 (EPZ019997), a potent, reversible type I PRMT inhibitor with anti-tumor effects in human cancer m

54 cocrystal structure of PRMT6-MS023 (a type I PRMT inhibitor), we discovered the first potent and cell

55 erstanding the antitumor mechanism of type I PRMT inhibitors and provide a rationale and biomarker ap

56 Because type I PRMT inhibitors are already undergoing clinical trials f

57 roach that, starting from a series of type I PRMT inhibitors previously identified by us, allowed for

58 roach for the clinical development of type I PRMT inhibitors.

59 broad proteomic approach to identify type I PRMT substrates.

60 Inhibition of type I PRMT triggers an interferon response through the antivir

61 product: asymmetric dimethylarginine (Type I PRMT), symmetric dimethylarginine (Type II PRMT), or mon

62 to aspartate converts TbPRMT7 into a type I PRMT, producing asymmetric dimethylarginine (ADMA).

63 These three enzymes are the primary type I PRMTs and are responsible for the majority of the asymme

64 Type I PRMTs and their substrates have been implicated in human

65 8715 is a small molecule inhibitor of type I PRMTs currently in clinical development.

66 Our findings show that inhibition of type I PRMTs increased the proliferation capabilities of MuSCs

67 man cancers, suggesting inhibition of type I PRMTs may offer a therapeutic approach for oncology.

68 ed on 4, a fragment-like inhibitor of type I PRMTs, we conducted structure-activity relationship (SAR

69 We thus performed a screen of type I PRMTs, which revealed that PRMT6 can also deposit the H3

70 ar, the most successful strategy to identify PRMT inhibitors has been to screen large to medium-size

71 ited abundant expression of PRMT5, a type II PRMT enzyme that promotes transcriptional silencing of t

72 pitulated splicing changes seen with Type II PRMT inhibition, without disrupting snRNP assembly.

73 PRMT5, a type II PRMT that interacts with BRG1, repressed Cyp24a1 transcr

74 I PRMT), symmetric dimethylarginine (Type II PRMT), or monomethylated arginine (Type III PRMT).

75 the involvement of PRMT5, the major type II PRMT, in cell survival and differentiation pathways that

76 Inhibition of PRMT5, the predominant type II PRMT, produces synergistic cancer cell growth inhibition

77 icing regulation, we inhibited Type I and II PRMTs and probed their transcriptomic consequences.

78 dimethylarginine (SDMA) residues as type II PRMTs.

79 hromatin modifier PRMT7 is the only Type III PRMT found in higher eukaryotes and a restricted number

80 y representing the only exclusively type III PRMT identified to date.

81 PRMT7 is the single type III PRMT solely capable of arginine monomethylation.

82 PRMT), or monomethylated arginine (Type III PRMT).

83 studies indicate that TbPRMT7 is a Type III PRMT, and its robust activity and presence in numerous c

84 ubstrates reveals that TbPRMT7 is a type III PRMT, catalyzing the formation of only monomethylarginin

85 ubstrates, thus classifying it as a type III PRMT.

86 f how the so-far developed inhibitors impact PRMT functions and cellular physiology.

87 d a general model for product specificity in PRMTs, which will be useful for the rational design of s

88 The inactive PRMT paralog, TbPRMT1(PRO), is essential for catalytic a

89 velopment of inhibitors targeting individual PRMTs, we initiated studies to characterize the molecula

90 gher inhibition activity than the well-known PRMT inhibitors AMI-1.

91 This work introduces Leishmania PRMTs as epigenetic regulators of mRNA metabolism with m

92 PRMT5 is the main PRMT responsible for symmetric dimethylation of arginine

93 thyltransferase activity of PRMT1, the major PRMT isoform in humans, is impaired under oxidative cond

94 The expression of one of the nine mammalian PRMTs, PRMT5, affects the levels of symmetric dimethylar

95 Although many PRMT substrates have been identified, and their methylat

96 , through Sm and CHTOP arginine methylation, PRMTs regulate the post-transcriptional processing of nu

97 idues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain.

98 Protein arginine methyltransferase (PRMT) 5 is an essential arginine methyltransferase respo

99 Protein arginine methyltransferase (PRMT) 5 is over-expressed in a variety of cancers and th

100 ort that protein arginine methyltransferase (PRMT) 6 activity is required for the proliferation, stem

101 Protein arginine methyltransferase (PRMT) 8 is unique among the PRMTs, as it has a highly re

102 Human protein arginine methyltransferase (PRMT) 9 symmetrically dimethylates arginine residues on

103 Protein arginine methyltransferase (PRMT) activity has been implicated in stem cell pluripot

104 onserved protein arginine methyltransferase (PRMT) catalytic core flanked by unique pre- and post-cor

105 d by the protein arginine methyltransferase (PRMT) enzyme family.

106 for the protein arginine methyltransferase (PRMT) enzymes that catalyze these reactions has been lac

107 r of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukar

108 e type I protein arginine methyltransferase (PRMT) family of enzymes.

109 s of the protein arginine methyltransferase (PRMT) family: PRMT1, PRMT3, and PRMT6.

110 RM1 is a protein arginine methyltransferase (PRMT) that acts as a coactivator in a number of transcri

111 T7) is a protein arginine methyltransferase (PRMT) that strictly monomethylates various substrates, t

112 type II protein arginine methyltransferase (PRMT) that, in winter-annual strains, is required for ep

113 ed human protein-arginine methyltransferase (PRMT), was cloned and expressed in Escherichia coli and

114 nding to protein arginine methyltransferase (PRMT)-1, and nuclear asymmetrical dimethylarginine modif

115 nhibit protein arginine N-methyltransferase (PRMT) activity.

116 me for protein arginine N-methyltransferase (PRMT) family members, a novel gene has been found on chr

117 of the protein arginine N-methyltransferase (PRMT) family of enzymes has identified a gene on chromos

118 Protein Arginine Methyltransferases (PRMT) 1 and 5 dimethylate their substrates on R residues

119 type I protein arginine methyltransferases (PRMT) are directly involved in mammary gland transformat

120 Protein arginine methyltransferases (PRMT) are generally not mutated in diseased states, but

121 Protein arginine N-methyltransferases (PRMT) are a family of S-adenosyl-l-methionine (SAM)-depe

122 ype I protein arginine N-methyltransferases (PRMT), has been known for some time, members of this enz

123 used on protein arginine methyltransferases (PRMTs) 1, 3, 5, and 10.

124 Protein arginine methyltransferases (PRMTs) affect many processes; however, their role in pro

125 Protein arginine methyltransferases (PRMTs) aid in the regulation of many biological processe

126 tors of protein arginine methyltransferases (PRMTs) among the top hits reducing DMG cell viability.

127 dues by protein arginine methyltransferases (PRMTs) and is degraded by dimethylarginine dimethylamino

128 Protein arginine methyltransferases (PRMTs) are (S)-adenosylmethionine (SAM)-dependent methyl

129 The protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the mono- a

130 Protein arginine methyltransferases (PRMTs) are a family of enzymes that modify proteins by m

131 Protein arginine methyltransferases (PRMTs) are a group of eukaryotic enzymes that catalyze t

132 The arginine methyltransferases (PRMTs) are envisaged as promising druggable targets, but

133 Protein arginine methyltransferases (PRMTs) are enzymes that are involved in many biological

134 Protein arginine methyltransferases (PRMTs) are enzymes that catalyze the methylation of argi

135 Protein arginine methyltransferases (PRMTs) are important posttranslational modifying enzymes

136 Protein arginine methyltransferases (PRMTs) are important therapeutic targets, playing a cruc

137 tors of protein arginine methyltransferases (PRMTs) are invaluable chemical tools for testing biologi

138 Protein arginine methyltransferases (PRMTs) are proved to play vital roles in chromatin remod

139 Protein arginine methyltransferases (PRMTs) are required for the regulation of RNA processing

140 Protein arginine methyltransferases (PRMTs) are S-adenosylmethionine-dependent enzymes that t

141 Protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono-

142 Protein arginine methyltransferases (PRMTs) are the driving force for the process of arginine

143 Protein arginine methyltransferases (PRMTs) catalyze arginine methylation on both chromatin-b

144 Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric dimethylation of arginines on

145 tion of protein arginine methyltransferases (PRMTs) has been linked to many pathological conditions.

146 Protein arginine methyltransferases (PRMTs) have been implicated in transcriptional activatio

147 Protein arginine methyltransferases (PRMTs) have emerged as attractive therapeutic targets fo

148 ones by protein arginine methyltransferases (PRMTs) impacts genome organization and gene expression.

149 s), and protein arginine methyltransferases (PRMTs) in pancreatic alpha- and beta-cell lines.

150 The protein arginine methyltransferases (PRMTs) include a family of proteins with related putativ

151 Protein arginine methyltransferases (PRMTs) introduce arginine methylation, a post-translatio

152 on by protein N-arginine methyltransferases (PRMTs) is an important posttranslational modification in

153 tion of protein arginine methyltransferases (PRMTs) is correlated with many human diseases.

154 atin by protein arginine methyltransferases (PRMTs) is crucial for normal cell growth and health.

155 Protein arginine methyltransferases (PRMTs) mediate the AdoMet-dependent methylation of many

156 Protein arginine methyltransferases (PRMTs) mediate the transfer of methyl groups to arginine

157 Protein arginine methyltransferases (PRMTs) modify diverse protein targets and regulate numer

158 by host protein arginine methyltransferases (PRMTs) necessary for the viral life cycle, but it remain

159 Protein arginine methyltransferases (PRMTs) play an important role in diverse biological proc

160 Protein arginine methyltransferases (PRMTs) play important roles in several cellular processe

161 Protein arginine methyltransferases (PRMTs) regulate many physiological processes, including

162 Protein arginine methyltransferases (PRMTs) represent an emerging target class in oncology an

163 Protein arginine methyltransferases (PRMTs) represent promising drug targets.

164 yzed by protein arginine methyltransferases (PRMTs) that are typically thought to function as homodim

165 mily of protein arginine methyltransferases (PRMTs) that predominantly generate either asymmetric or

166 type I protein arginine methyltransferases (PRMTs) with MS023 increases the proliferative capacity o

167 icating protein arginine methyltransferases (PRMTs), enzymes that deposit arginine methylation, in tr

168 tion of protein arginine methyltransferases (PRMTs), have been shown to enhance and impair their enzy

169 yzed by protein arginine methyltransferases (PRMTs), is increased in human asthmatic lungs.

170 type I protein arginine methyltransferases (PRMTs), respectively, reduces splicing fidelity and resu

171 quently protein arginine methyltransferases (PRMTs), the writers of arginine methylation, have rapidl

172 mbinant protein arginine methyltransferases (PRMTs), we showed that the C-terminal domain could be me

173 vity of protein arginine methyltransferases (PRMTs), which catalyze the formation of various methylat

174 type I protein arginine methyltransferases (PRMTs), which has antitumor growth activity in TNBC.

175 Ts) and protein arginine methyltransferases (PRMTs).

176 lex and protein-arginine methyltransferases (PRMTs).

177 and the protein arginine methyltransferases (PRMTs).

178 mily of protein arginine methyltransferases (PRMTs).

179 yzed by protein arginine methyltransferases (PRMTs).

180 of nine protein arginine methyltransferases (PRMTs).

181 include protein arginine methyltransferases (PRMTs).

182 ETs), protein arginine N-methyltransferases (PRMTs) and isocitrate dehydrogenases (IDHs), and highlig

183 ndent protein arginine N-methyltransferases (PRMTs) catalyze the methylation of arginine residues wit

184 pathways that involve specific HTT-modifying PRMT enzymes and modulate HTT biochemical and toxic prop

185 evelopment and application of small molecule PRMT inhibitors will provide new avenues for therapeutic

186 ns have been shown to be substrates for most PRMT family members.

187 he optimal target motif for each of the nine PRMTs has not been systematically addressed.

188 cule directly targets the substrates but not PRMTs for the observed inhibition.

189 These findings about novel PRMT inhibitors and their unique inhibition mechanism pr

190 portunities of developing and applying novel PRMT inhibitors for clinical advancement.

191 for proteomic applications to identify novel PRMT substrates.

192 eric structures, but the structural basis of PRMT oligomerization and its functional consequence are

193 Accurate control of PRMT activity includes recognition of specific arginyl g

194 an serve as a warhead for the development of PRMT chemical probes.

195 To aid the development of PRMT inhibitors, we characterized the substrate specific

196 anistic interrogation and the development of PRMT-directed therapies.See related article by Bao et al

197 nistic basis for the therapeutic efficacy of PRMT inhibition in cancer.

198 cate that motions are a conserved element of PRMT function.

199 The field of PRMT inhibitors is in the rapidly growing phase and it i

200 MTV-NIC mouse, we investigated the impact of PRMT overexpression alone or in the context of a HER2-dr

201 trometry confirmed significant inhibition of PRMT activity in cells.

202 ate bisubstrate analogue-based inhibitors of PRMT isozymes that are potent and highly selective for a

203 hromatography combined with the knowledge of PRMT crystal structures suggests a model where the size

204 To understand the specific mechanisms of PRMT activity in splicing regulation, we inhibited Type

205 to characterize the molecular mechanisms of PRMT catalysis.

206 biological roles and molecular mechanisms of PRMT overexpression in the mammary gland.

207 our knowledge on the molecular mechanisms of PRMT substrate recognition and has important implication

208 T1 prozyme, which represents a novel mode of PRMT regulation.

209 Given the transient nature of PRMT-substrate complexes, such transition state mimics r

210 y to neuronal cells, while overexpression of PRMT 4 and 6 was beneficial for neuronal survival.

211 Aberrant regulation of PRMT activity is associated with various pathological st

212 To address the possible roles of PRMT overexpression in mammary gland tumorigenesis, we g

213 his recent progress and the current state of PRMT inhibitors, some in clinical trials, as promising d

214 , providing a valuable tool for the study of PRMT function in tumorigenesis.See related commentary by

215 vious reports of the enzymatic activities of PRMTs on histones in the context of nucleosomes seem con

216 sitively regulates the enzymatic activity of PRMTs in biology.

217 the histone arginine methylation activity of PRMTs.

218 mechanistic understanding of the biology of PRMTs is required.

219 implications for the rational (re)design of PRMTs.

220 These results suggest that native forms of PRMTs can have different properties than their GST-catal

221 The importance of PRMTs in the incidence and progression of a wide range o

222 However, few selective inhibitors of PRMTs have been discovered.

223 ific compounds that block the interaction of PRMTs with their targets.

224 so suggest a general model for regulation of PRMTs.

225 help us understand the physiological role of PRMTs have not been fully established.

226 However, the role of PRMTs in colorectal cancer (CRC) progression is not well

227 focus on advances made regarding the role of PRMTs in stem cell biology, epigenetics, splicing, immun

228 ion tag affects the substrate selectivity of PRMTs.

229 a detailed exploration of the active site of PRMTs.

230 ly illuminates the intricate active sites of PRMTs to facilitate the discovery of highly potent and i

231 ossible overlapping substrate specificity of PRMTs, 17 and 46 are valuable chemical tools for dissect

232 the biological roles in cells and in vivo of PRMTs.

233 Notably, PRMT5 is the only PRMT that requires an obligate cofactor, methylosome pro

234 s, and peptides that are bisubstrate, and/or PRMT transition state mimic inhibitors as well as inhibi

235 Inhibition of GSK3 or PRMT-1 or overexpression of the AC-associated mutant R28

236 nine protein arginine methyltransferases, or PRMTs.

237 ow that these motions are conserved in other PRMT enzymes.

238 ignificantly decrease, indicating that other PRMT(s) may compensate for this loss.

239 of a catalytic core sequence common to other PRMT enzymes.

240 light differences between AtPRMT10 and other PRMTs but also indicate that motions are a conserved ele

241 T2, histone peptides and proteins, and other PRMTs using analytical and enzymatic approaches.

242 3 substrate that cannot be modified by other PRMTs.

243 e region (C-extension), not present in other PRMTs.

244 e methyltransferase 5 (PRMT5), but not other PRMTs, promotes AKT activation by catalyzing symmetric d

245 intracellular signaling, the roles of other PRMTs in diverse cellular processes have not been fully

246 was selective for PRMT4 and PRMT6 over other PRMTs and a broad range of other epigenetic modifiers an

247 ore than hundred-fold selectivity over other PRMTs.

248 cus on its N-terminus and predict that other PRMTs may employ similar mechanism for substrate recogni

249 f 38 methyltransferases, including the other PRMTs.

250 ontrast to what had been observed with other PRMTs and their physiological substrates, a peptide cont

251 Here, by deconstructing potent PRMT inhibitors, we find that chemical moieties occupyin

252 The predominant PRMT in vivo, PRMT1, has wide substrate specificity and

253 PRMT1 is the predominant PRMT isoform in mammalian cells and acts in pathways reg

254 R95 and R177 within RGG/RG motifs, preferred PRMT target sequences.

255 Trypanosoma brucei, possesses five putative PRMTs, a relatively large number for a single-celled euk

256 not covalently modify other closely related PRMTs, potently inhibited PRMT6 in cells, and was select

257 omodimer observed in all previously reported PRMTs.

258 e useful for the rational design of specific PRMT inhibitors.

259 The data define the distribution of specific PRMTs and their target proteins in flagella and demonstr

260 cription of cancer-related genes, suggesting PRMT family members may be valid therapeutic targets.

261 However, cleavage of tagged PRMTs has been problematic.

262 recognition, it is imperative that a tagless PRMT be used.

263 Although all the tested PRMTs methylate multiple free histones individually, the

264 resolution crystal structure of A. thaliana PRMT 10 (AtPRMT10) in complex with a reaction product, S

265 ation arm that is 12-20 residues longer than PRMT structures elucidated previously; as a result, the

266 o-transcriptional splicing demonstrated that PRMT inhibition resulted in altered splicing rates.

267 In addition, we found that PRMT 1 and 3 are also highly enriched at the base of the

268 et proteins in flagella and demonstrate that PRMTs are cargo for translocation within flagella by the

269 it ongoing transcription, we determined that PRMTs post-transcriptionally regulate RI.

270 her, these results open the possibility that PRMTs respond in cells undergoing temperature, salt, or

271 Increasing evidence supports that PRMTs exhibit the capacity to form higher-order oligomer

272 The PRMT overexpression transgenic mouse models should encou

273 up the active site are conserved across the PRMT family, consisting of a double-E loop containing tw

274 ct biological outputs, as highlighted in the PRMT-dependent epigenetic control of transcription.

275 As the only known member of the PRMT enzyme family to catalyze the formation of mono- an

276 of AtPRMT10, as well as other members of the PRMT family of enzymes.

277 e methyltransferase 9 (PRMT9) is part of the PRMT family, and it is suspected to function in pathways

278 RMT9) is a recently identified member of the PRMT family, yet its biological function remains largely

279 basis for functional characterization of the PRMT family.

280 thyltransferase (PRMT) 8 is unique among the PRMTs, as it has a highly restricted tissue expression p

281 uct formation by active site residues in the PRMTs.

282 cterize the mechanisms and regulation of the PRMTs and develop chemical probes targeting these enzyme

283 ted the methylation efficiency of all of the PRMTs toward HMGA1 proteins.

284 In the future, these PRMT (Tg) lines can be leveraged to investigate the role

285 mmarize molecular action mechanisms of these PRMT inhibitors and particularly elaborate their trigger

286 small molecule inhibitors that target these PRMT.

287 These PRMTs localize to the tip of flagella and in a punctate

288 lagella, and the basal localization of these PRMTs changes during flagellar regeneration and resorpti

289 The overexpression of all three PRMTs induced hyper-branching of the mammary glands and

290 e implicating elevated levels of these three PRMTs in mammary gland tumorigenesis, albeit with variab

291 subsets of cancer most likely to respond to PRMT inhibition, synergistic effects of combined PRMT5 a

292 The predominant methyl transferase PRMT-1 is highly expressed in T helper cells, and ligati

293 zed by Protein aRginine Methyl Transferases (PRMTs).

294 report the characterization of a trypanosome PRMT, TbPRMT7, which is homologous to human PRMT7.

295 /9 inhibitor and its binding mode to the two PRMT enzymes.

296 and are structurally different from typical PRMT substrates, for example, histone H4 and glycine- an

297 eloped a successful method by which untagged PRMTs can be made using a tobacco etch virus (TEV) cleav

298 However, the direct roles of the various PRMTs during autophagosome formation remain unclear.

299 To explore whether PRMTs modulate p53 function, we generated multiple cell

300 rucial to understand the mechanisms by which PRMT product specificity is conferred.