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1 lation, and we designate the enzyme as Rmt2 (protein arginine methyltransferase).
2 nfirm its activity as the prototype type III protein arginine methyltransferase.
3 we generated an enzyme-dead knock-in of this protein arginine methyltransferase.
4 D physically interacts with PRMT1, the major protein arginine methyltransferase.
5 stone H4-specific methyltransferase PRMT1, a protein arginine methyltransferase.
6 d protein kinase, and by Hsl7, a presumptive protein-arginine methyltransferase.
7 ated arginine methyltransferase 1 (CARM1), a protein-arginine methyltransferase.
8 tification of an array of substrates for the protein arginine methyltransferases.
9 insight into the structure and catalysis of protein arginine methyltransferases.
10 nd was highly selective for CARM1 over other protein arginine methyltransferases.
11 diverse product specificity displayed by the protein-arginine methyltransferases.
12 o-hydrolase, and is derived by the action of protein-arginine-methyltransferases.
13 w that glycogen synthase kinase 3 (GSK3) and protein arginine methyltransferase 1 (PRMT-1) cooperate
16 ion of E2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetr
20 logical activity of RIP140 was suppressed by protein arginine methyltransferase 1 (PRMT1) due to RIP1
21 and R200 of the EGFR extracellular domain by protein arginine methyltransferase 1 (PRMT1) enhances bi
29 , steroid receptor coactivator 1 (SRC1), and protein arginine methyltransferase 1 (PRMT1) only modest
30 As the major arginine methylation enzyme, protein arginine methyltransferase 1 (PRMT1) strictly ge
33 ty is potentiated by arginine methylation by protein arginine methyltransferase 1 (PRMT1), another nu
34 S by the class 1 arginine methyltransferase, protein arginine methyltransferase 1 (PRMT1), regulates
36 during Wnt signaling through the activity of protein arginine methyltransferase 1 (PRMT1), which tran
39 SG-nucleating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PR
40 deletion of the arginine methyltransferases protein arginine methyltransferase 1 and protein arginin
41 IP45 acts as an enhancer for the assembly of protein arginine methyltransferase 1 and the protein arg
42 s of protein methylation and coexpression of protein arginine methyltransferase 1 did not influence N
43 t LANA is subject to arginine methylation by protein arginine methyltransferase 1 in vitro and in viv
44 asymmetric dimethyl H4R3 catalyzed by PRMT1 (protein arginine methyltransferase 1) facilitates histon
45 asonuclin 1 physically interacts with PRMT1 (protein arginine methyltransferase 1) to activate cell c
47 bonucleoprotein K (hnRNP K) protein by human protein arginine methyltransferase 1, variant 1 (hPRMT1v
49 protein arginine methyltransferase 1 and the protein arginine methyltransferase 1-linked histone 4 ar
51 phosphatase-transcription activator EYA1 by protein arginine methyltransferase 1: mechanistic, funct
56 s used to validate the interactions of BRD4, protein arginine methyltransferase-1 (PRMT1), and Snail.
57 hydrolase protein expression was reduced and protein-arginine-methyltransferase-1 increased in alcoho
59 ed yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ER
62 with myocardial infarction, the PRMT3 gene (protein arginine methyltransferase 3) with stroke, and t
64 we report a novel regulation of pRb through protein arginine methyltransferase 4 (PRMT4)-mediated ar
65 en ASXL2 and MLL3 is negatively regulated by protein arginine methyltransferase 4 (PRMT4/CARM1), whic
67 mpairs T cell function via the inhibition of protein arginine methyltransferase 5 (PRMT5) and by aden
68 ase (MTAP) confers a selective dependence on protein arginine methyltransferase 5 (PRMT5) and its bin
69 UsnRNPs) requires assembly factors united in protein arginine methyltransferase 5 (PRMT5) and surviva
70 ion and characterization of a complex of the protein arginine methyltransferase 5 (Prmt5) and the met
71 cance of PDCD4 in breast cancer and identify protein arginine methyltransferase 5 (PRMT5) as a cofact
72 Here, we describe the identification of the protein arginine methyltransferase 5 (PRMT5) as an effec
73 rification and mass spectrometry to identify protein arginine methyltransferase 5 (PRMT5) as part of
84 a positive feedback loop between BCR-ABL and protein arginine methyltransferase 5 (PRMT5) in CML cell
85 duces a synthetic lethal phenotype involving protein arginine methyltransferase 5 (PRMT5) inhibition.
86 NS-penetrant methylthioadenosine-cooperative protein arginine methyltransferase 5 (PRMT5) inhibitor,
97 evidence suggest that the methyltransferase protein arginine methyltransferase 5 (PRMT5) is responsi
100 cleaved kinases (M6CKs) bind subunits of the protein arginine methyltransferase 5 (PRMT5) molecular c
103 tumor suppressor, but its coexpression with protein arginine methyltransferase 5 (PRMT5) promotes ac
104 transformation to document the relevance of protein arginine methyltransferase 5 (PRMT5) to regulati
109 ll nuclear ribonucleoprotein D3b (SmD3b) and protein arginine methyltransferase 5 (PRMT5), which are
116 forward genetic analysis we demonstrate that protein arginine methyltransferase 5 (PRMT5; At4g31120)
119 that E2F-1 is directly methylated by PRMT5 (protein arginine methyltransferase 5), and that arginine
120 ses protein arginine methyltransferase 1 and protein arginine methyltransferase 5, suggesting that th
121 free transcriptional system and contains the protein arginine methyltransferase 5, which acts synergi
125 on of the known Ajuba binding partner Prmt5 (protein arginine methyltransferase-5) inhibited the Ajub
126 ors lysine-specific demethylase 1 (LSD1) and protein arginine methyltransferase 6 (PRMT6) are overexp
128 tor arginine methyltransferase 1 (CARM1) and protein arginine methyltransferase 6 (PRMT6) in vitro an
139 us are associated with blunted expression of protein arginine methyltransferase 7 (Prmt7) on chromoso
142 We found that the selective inhibitor of protein arginine methyltransferases 7,7'-carbonylbis(aza
147 +), FDH(+/-), and FDH(-/-) mice have similar protein arginine methyltransferase activities but high,
148 lts provide an example for the regulation of protein arginine methyltransferase activity by phosphory
149 most 80% identical to human PRMT1, the major protein arginine methyltransferase activity in mammalian
150 uential recruitment of CARM1 not only adds a protein arginine methyltransferase activity to the ER-co
153 sferase I (PRMT1) contributes >90% of type I protein-arginine methyltransferase activity in cells and
155 nd demonstrate that the activity of PRMT5, a protein arginine methyltransferase and indirect target o
156 identify PRMT3 as the first type I ribosomal protein arginine methyltransferase and suggest that it r
157 t specificity and the catalytic mechanism of protein arginine methyltransferases and have important i
159 s study showed that the Arabidopsis thaliana protein arginine methyltransferase AtPRMT3 regulates pre
162 We have recently described a large (20 S) protein arginine methyltransferase complex, termed the m
164 lude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity prese
167 s catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-do
172 tone deacetylases, BET bromodomain proteins, protein arginine methyltransferases, histone lysine meth
176 the JCI, Liao et al. investigate the role of protein arginine methyltransferase I (PRMT1) in regulati
178 ot a substrate for PRMT1, the most prominent protein-arginine methyltransferase in mammalian cells, w
179 data suggest a novel mechanism by which the protein arginine methyltransferase is involved in the co
181 tructure can be seen as a ternary complex of protein arginine methyltransferase (one subunit) complex
184 ated arginine methyltransferase 1 (CARM1), a protein-arginine methyltransferase previously shown to s
185 methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in
193 ttranslational modification catalyzed by the protein arginine methyltransferase (PRMT) enzyme family.
195 thyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and met
196 a residue completely conserved in the type I protein arginine methyltransferase (PRMT) family of enzy
197 and HMGA1b proteins by three members of the protein arginine methyltransferase (PRMT) family: PRMT1,
201 Mass spectrometry identified LRP6 binding to protein arginine methyltransferase (PRMT)-1, and nuclear
203 Bao and colleagues demonstrate that type I protein arginine methyltransferases (PRMT) are directly
205 cDNA for PRMT7, a recently discovered human protein-arginine methyltransferase (PRMT), was cloned an
206 Through an shRNA screen, we identified the protein arginine methyltransferase Prmt1 as a vulnerable
207 ceptor signaling increased expression of the protein arginine methyltransferase PRMT1, which in turn
208 emonstrate (1) the additional involvement of protein arginine methyltransferases PRMT1 and CARM1 in p
209 at SPT5 was specifically associated with the protein arginine methyltransferases PRMT1 and PRMT5 and
210 ere we show that S-HDAg can be methylated by protein arginine methyltransferase (PRMT1) in vitro and
211 The human genome encodes a family of nine protein arginine methyltransferases (PRMT1-9), whose mem
213 n to form an extraribosomal complex with the protein arginine methyltransferase PRMT3 that is conserv
214 and mutational analysis, we demonstrate that protein arginine methyltransferase PRMT4 (CARM1) methyla
215 e report the selective overexpression of the protein arginine methyltransferase PRMT5 as a novel cand
216 body components and identify the ortholog of protein arginine methyltransferase PRMT5 as the enzyme r
217 esis, and enhanced expression of the type II protein arginine methyltransferase PRMT5 as well as the
221 Among the target genes, we confirmed the protein arginine methyltransferase Prmt5 is a direct tar
226 we have functionally analyzed two different protein arginine methyltransferases, Prmt5 and Prmt4, bo
228 ion during flagellar dynamics, we focused on protein arginine methyltransferases (PRMTs) 1, 3, 5, and
231 hibitor library and identified inhibitors of protein arginine methyltransferases (PRMTs) among the to
232 proteins methylated on arginine residues by protein arginine methyltransferases (PRMTs) and is degra
241 Well-characterized selective inhibitors of protein arginine methyltransferases (PRMTs) are invaluab
253 stone lysine methyltransferases (HKMTs), and protein arginine methyltransferases (PRMTs) in pancreati
257 oper epigenetic modification of chromatin by protein arginine methyltransferases (PRMTs) is crucial f
266 onal modification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs) that are typ
268 Herein, we show that inhibition of type I protein arginine methyltransferases (PRMTs) with MS023 i
270 Increased arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), is increase
271 on of arginine, mediated by PRMT5 and type I protein arginine methyltransferases (PRMTs), respectivel
274 strategies aimed at blocking the activity of protein arginine methyltransferases (PRMTs), which catal
275 we identified MS023, an inhibitor of type I protein arginine methyltransferases (PRMTs), which has a
284 ll, Wang and colleagues report that CARM1, a protein arginine methyltransferase, specifically methyla
286 n-regulation of the major trypanosome type 1 protein arginine methyltransferase, TbPRMT1, disrupts fo
288 id not cooperate with PRMT1, a CARM1-related protein arginine methyltransferase that also functions a
289 tein arginine methyltransferase 5 (PRMT5), a protein arginine methyltransferase that catalyzes the sy
291 ed arginine methyltransferase 1 (CARM1) is a protein arginine methyltransferase that methylates histo
294 4 substrates suggest that type I and type II protein-arginine methyltransferases use distinct molecul
295 4 have been methylated in vitro by a nuclear protein arginine methyltransferase using recombinant (un
296 electively modulates enzymatic activity of a protein arginine methyltransferase vital to abiotic stre
299 omolog of a recently characterized mammalian protein-arginine methyltransferase whose activity may be