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1 lation, and we designate the enzyme as Rmt2 (protein arginine methyltransferase).
2 we generated an enzyme-dead knock-in of this protein arginine methyltransferase.
3 D physically interacts with PRMT1, the major protein arginine methyltransferase.
4 stone H4-specific methyltransferase PRMT1, a protein arginine methyltransferase.
5 nfirm its activity as the prototype type III 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 diverse product specificity displayed by the protein-arginine methyltransferases.
11 o-hydrolase, and is derived by the action of protein-arginine-methyltransferases.
12 w that glycogen synthase kinase 3 (GSK3) and protein arginine methyltransferase 1 (PRMT-1) cooperate
15 ion of E2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetr
18 logical activity of RIP140 was suppressed by protein arginine methyltransferase 1 (PRMT1) due to RIP1
19 and R200 of the EGFR extracellular domain by protein arginine methyltransferase 1 (PRMT1) enhances bi
24 , steroid receptor coactivator 1 (SRC1), and protein arginine methyltransferase 1 (PRMT1) only modest
25 As the major arginine methylation enzyme, protein arginine methyltransferase 1 (PRMT1) strictly ge
27 ty is potentiated by arginine methylation by protein arginine methyltransferase 1 (PRMT1), another nu
28 S by the class 1 arginine methyltransferase, protein arginine methyltransferase 1 (PRMT1), regulates
32 SG-nucleating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PR
33 IP45 acts as an enhancer for the assembly of protein arginine methyltransferase 1 and the protein arg
34 s of protein methylation and coexpression of protein arginine methyltransferase 1 did not influence N
35 t LANA is subject to arginine methylation by protein arginine methyltransferase 1 in vitro and in viv
36 asymmetric dimethyl H4R3 catalyzed by PRMT1 (protein arginine methyltransferase 1) facilitates histon
38 bonucleoprotein K (hnRNP K) protein by human protein arginine methyltransferase 1, variant 1 (hPRMT1v
40 protein arginine methyltransferase 1 and the protein arginine methyltransferase 1-linked histone 4 ar
42 phosphatase-transcription activator EYA1 by protein arginine methyltransferase 1: mechanistic, funct
47 hydrolase protein expression was reduced and protein-arginine-methyltransferase-1 increased in alcoho
49 ed yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ER
51 with myocardial infarction, the PRMT3 gene (protein arginine methyltransferase 3) with stroke, and t
52 we report a novel regulation of pRb through protein arginine methyltransferase 4 (PRMT4)-mediated ar
54 ase (MTAP) confers a selective dependence on protein arginine methyltransferase 5 (PRMT5) and its bin
55 UsnRNPs) requires assembly factors united in protein arginine methyltransferase 5 (PRMT5) and surviva
56 ion and characterization of a complex of the protein arginine methyltransferase 5 (Prmt5) and the met
57 cance of PDCD4 in breast cancer and identify protein arginine methyltransferase 5 (PRMT5) as a cofact
58 Here, we describe the identification of the protein arginine methyltransferase 5 (PRMT5) as an effec
59 rification and mass spectrometry to identify protein arginine methyltransferase 5 (PRMT5) as part of
61 a positive feedback loop between BCR-ABL and protein arginine methyltransferase 5 (PRMT5) in CML cell
65 evidence suggest that the methyltransferase protein arginine methyltransferase 5 (PRMT5) is responsi
66 cleaved kinases (M6CKs) bind subunits of the protein arginine methyltransferase 5 (PRMT5) molecular c
68 tumor suppressor, but its coexpression with protein arginine methyltransferase 5 (PRMT5) promotes ac
69 transformation to document the relevance of protein arginine methyltransferase 5 (PRMT5) to regulati
73 ll nuclear ribonucleoprotein D3b (SmD3b) and protein arginine methyltransferase 5 (PRMT5), which are
77 forward genetic analysis we demonstrate that protein arginine methyltransferase 5 (PRMT5; At4g31120)
78 that E2F-1 is directly methylated by PRMT5 (protein arginine methyltransferase 5), and that arginine
79 free transcriptional system and contains the protein arginine methyltransferase 5, which acts synergi
81 on of the known Ajuba binding partner Prmt5 (protein arginine methyltransferase-5) inhibited the Ajub
82 tor arginine methyltransferase 1 (CARM1) and protein arginine methyltransferase 6 (PRMT6) in vitro an
90 us are associated with blunted expression of protein arginine methyltransferase 7 (Prmt7) on chromoso
92 We found that the selective inhibitor of protein arginine methyltransferases 7,7'-carbonylbis(aza
95 +), FDH(+/-), and FDH(-/-) mice have similar protein arginine methyltransferase activities but high,
96 lts provide an example for the regulation of protein arginine methyltransferase activity by phosphory
97 most 80% identical to human PRMT1, the major protein arginine methyltransferase activity in mammalian
98 uential recruitment of CARM1 not only adds a protein arginine methyltransferase activity to the ER-co
101 sferase I (PRMT1) contributes >90% of type I protein-arginine methyltransferase activity in cells and
103 identify PRMT3 as the first type I ribosomal protein arginine methyltransferase and suggest that it r
104 t specificity and the catalytic mechanism of protein arginine methyltransferases and have important i
108 We have recently described a large (20 S) protein arginine methyltransferase complex, termed the m
110 lude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity prese
113 s catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-do
120 the JCI, Liao et al. investigate the role of protein arginine methyltransferase I (PRMT1) in regulati
122 ot a substrate for PRMT1, the most prominent protein-arginine methyltransferase in mammalian cells, w
123 data suggest a novel mechanism by which the protein arginine methyltransferase is involved in the co
124 tructure can be seen as a ternary complex of protein arginine methyltransferase (one subunit) complex
127 ated arginine methyltransferase 1 (CARM1), a protein-arginine methyltransferase previously shown to s
128 methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in
134 thyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and met
135 a residue completely conserved in the type I protein arginine methyltransferase (PRMT) family of enzy
136 and HMGA1b proteins by three members of the protein arginine methyltransferase (PRMT) family: PRMT1,
139 Mass spectrometry identified LRP6 binding to protein arginine methyltransferase (PRMT)-1, and nuclear
140 cDNA for PRMT7, a recently discovered human protein-arginine methyltransferase (PRMT), was cloned an
141 Through an shRNA screen, we identified the protein arginine methyltransferase Prmt1 as a vulnerable
142 ceptor signaling increased expression of the protein arginine methyltransferase PRMT1, which in turn
143 emonstrate (1) the additional involvement of protein arginine methyltransferases PRMT1 and CARM1 in p
144 at SPT5 was specifically associated with the protein arginine methyltransferases PRMT1 and PRMT5 and
145 ere we show that S-HDAg can be methylated by protein arginine methyltransferase (PRMT1) in vitro and
146 The human genome encodes a family of nine protein arginine methyltransferases (PRMT1-9), whose mem
147 and mutational analysis, we demonstrate that protein arginine methyltransferase PRMT4 (CARM1) methyla
148 e report the selective overexpression of the protein arginine methyltransferase PRMT5 as a novel cand
149 body components and identify the ortholog of protein arginine methyltransferase PRMT5 as the enzyme r
150 esis, and enhanced expression of the type II protein arginine methyltransferase PRMT5 as well as the
154 Among the target genes, we confirmed the protein arginine methyltransferase Prmt5 is a direct tar
158 we have functionally analyzed two different protein arginine methyltransferases, Prmt5 and Prmt4, bo
160 ion during flagellar dynamics, we focused on protein arginine methyltransferases (PRMTs) 1, 3, 5, and
163 proteins methylated on arginine residues by protein arginine methyltransferases (PRMTs) and is degra
168 Well-characterized selective inhibitors of protein arginine methyltransferases (PRMTs) are invaluab
175 stone lysine methyltransferases (HKMTs), and protein arginine methyltransferases (PRMTs) in pancreati
179 oper epigenetic modification of chromatin by protein arginine methyltransferases (PRMTs) is crucial f
185 onal modification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs) that are typ
194 ll, Wang and colleagues report that CARM1, a protein arginine methyltransferase, specifically methyla
195 n-regulation of the major trypanosome type 1 protein arginine methyltransferase, TbPRMT1, disrupts fo
197 id not cooperate with PRMT1, a CARM1-related protein arginine methyltransferase that also functions a
199 tein arginine methyltransferase 5 (PRMT5), a protein arginine methyltransferase that catalyzes the sy
200 ed arginine methyltransferase 1 (CARM1) is a protein arginine methyltransferase that methylates histo
202 4 substrates suggest that type I and type II protein-arginine methyltransferases use distinct molecul
203 4 have been methylated in vitro by a nuclear protein arginine methyltransferase using recombinant (un
204 electively modulates enzymatic activity of a protein arginine methyltransferase vital to abiotic stre
207 omolog of a recently characterized mammalian protein-arginine methyltransferase whose activity may be
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