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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
13              We recently reported defects in protein arginine methyltransferase 1 (PRMT1) activity an
14                                              Protein arginine methyltransferase 1 (PRMT1) acts as a t
15 ion of E2F-1 by the asymmetric dimethylating protein arginine methyltransferase 1 (PRMT1) and symmetr
16                Here we identified the type I protein arginine methyltransferase 1 (PRMT1) as a restri
17                                              Protein arginine methyltransferase 1 (PRMT1) catalyzes t
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
20                                              Protein arginine methyltransferase 1 (PRMT1) is an essen
21                                              Protein arginine methyltransferase 1 (PRMT1) is involved
22                         Here, we report that protein arginine methyltransferase 1 (PRMT1) is required
23                                              Protein arginine methyltransferase 1 (PRMT1) is up-regul
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
26                        In the current study, protein arginine methyltransferase 1 (PRMT1), another ar
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
29                                              Protein arginine methyltransferase 1 (PRMT1), the predom
30  implementation to label substrates of human protein arginine methyltransferase 1 (PRMT1).
31 e chain of a peptide substrate by the enzyme protein arginine methyltransferase 1 (RMT1).
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
37 overy of a novel AE9a binding partner PRMT1 (protein arginine methyltransferase 1).
38 bonucleoprotein K (hnRNP K) protein by human protein arginine methyltransferase 1, variant 1 (hPRMT1v
39               EYA1 physically interacts with protein arginine methyltransferase 1, which methylates E
40 protein arginine methyltransferase 1 and the protein arginine methyltransferase 1-linked histone 4 ar
41 FGG-amide), a highly effective substrate for protein arginine methyltransferase 1.
42  phosphatase-transcription activator EYA1 by protein arginine methyltransferase 1: mechanistic, funct
43                                         When protein-arginine methyltransferase 1 expression was redu
44                                              Protein-arginine methyltransferase 1 has much less effec
45 transferase (EC 2.1.1.23) gene "PRMT1, " for protein-arginine methyltransferase 1.
46                           We found that both protein-arginine methyltransferases 1 and 5 methylate Ar
47 hydrolase protein expression was reduced and protein-arginine-methyltransferase-1 increased in alcoho
48                                              Protein arginine methyltransferase 10 (PRMT10) is a type
49 ed yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ER
50                                The mammalian protein arginine methyltransferase 3 (PRMT3) catalyzes t
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
53                 We have identified a mutant, protein arginine methyltransferase 5 (atprmt5), that fai
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
60                                              Protein arginine methyltransferase 5 (PRMT5) complexed w
61 a positive feedback loop between BCR-ABL and protein arginine methyltransferase 5 (PRMT5) in CML cell
62                                              Protein arginine methyltransferase 5 (PRMT5) is a key ep
63                                              Protein arginine methyltransferase 5 (PRMT5) is an argin
64                                              Protein arginine methyltransferase 5 (PRMT5) is an emerg
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
67                                              Protein arginine methyltransferase 5 (PRMT5) plays multi
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
70                Menin directly interacts with protein arginine methyltransferase 5 (PRMT5), a negative
71                                              Protein arginine methyltransferase 5 (PRMT5), a protein
72                         Here, we report that protein arginine methyltransferase 5 (PRMT5), an enzyme
73 ll nuclear ribonucleoprotein D3b (SmD3b) and protein arginine methyltransferase 5 (PRMT5), which are
74 y posttranslational methylation at Arg-57 by protein arginine methyltransferase 5 (PRMT5).
75 sphorylation through an association with the protein arginine methyltransferase 5 (PRMT5).
76 cted requirement for arginine methylation by protein arginine methyltransferase 5 (PRMT5).
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
80 ppaB is dimethylated on arginine 30 (R30) by protein-arginine methyltransferase 5 (PRMT5).
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
83                                              Protein arginine methyltransferase 6 (PRMT6) is a nuclea
84                            We show here that protein arginine methyltransferase 6 (PRMT6) is a specif
85                                              Protein arginine methyltransferase 7 (PRMT7) catalyzes t
86                            Full-length human protein arginine methyltransferase 7 (PRMT7) expressed a
87                                The mammalian protein arginine methyltransferase 7 (PRMT7) has been im
88                       Here, we show that the protein arginine methyltransferase 7 (PRMT7) is a plurip
89                                              Protein arginine methyltransferase 7 (PRMT7) methylates
90 us are associated with blunted expression of protein arginine methyltransferase 7 (Prmt7) on chromoso
91                                          The protein arginine methyltransferase 7 (PRMT7), but not PR
92     We found that the selective inhibitor of protein arginine methyltransferases 7,7'-carbonylbis(aza
93                     Here we use mice lacking protein arginine methyltransferase 8 (PRMT8) in the brai
94                          The multifunctional protein arginine methyltransferase 8 (PRMT8) possesses b
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
99                    In a previous study, this protein arginine methyltransferase activity was identifi
100 ediate-early protein, was then shown to have protein arginine methyltransferase activity.
101 sferase I (PRMT1) contributes >90% of type I protein-arginine methyltransferase activity in cells and
102                                              Protein-arginine methyltransferases aid in the regulatio
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
105                                     Multiple protein arginine methyltransferases are involved in tran
106                        Recent discoveries of protein arginine methyltransferases, CARM1 and PRMT1, as
107                                       Type I protein arginine methyltransferases catalyze the formati
108    We have recently described a large (20 S) protein arginine methyltransferase complex, termed the m
109                                              Protein arginine methyltransferase enzyme 5 (PRMT5) regu
110 lude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity prese
111                              We identify the protein arginine methyltransferase enzymes that catalyze
112                        Our data suggest that protein arginine methyltransferases exert key regulatory
113 s catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-do
114                         Other members of the protein arginine methyltransferase family, which methyla
115 , which is highly conserved among the entire protein arginine methyltransferase family.
116                                    The RMT1 (protein-arginine methyltransferase), formerly ODP1, gene
117           Here we demonstrate a role for the protein arginine methyltransferase Hmt1 in this process.
118         Previously, we demonstrated that the protein arginine methyltransferase Hmt1 plays a role in
119 modified within its RGG domain by the type I protein-arginine methyltransferase, Hmt1p.
120 the JCI, Liao et al. investigate the role of protein arginine methyltransferase I (PRMT1) in regulati
121                                              Protein-arginine methyltransferase I (PRMT1) contributes
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
125 tion, which is catalyzed by a family of nine protein arginine methyltransferases, or PRMTs.
126          It is the first to demonstrate that protein arginine methyltransferases participate in the D
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
129                                              Protein arginine methyltransferase (PRMT) 8 is unique am
130                                        Human protein arginine methyltransferase (PRMT) 9 symmetricall
131                                              Protein arginine methyltransferase (PRMT) activity has b
132                   CARM1 contains a conserved protein arginine methyltransferase (PRMT) catalytic core
133           However, a conclusive role for the protein arginine methyltransferase (PRMT) enzymes that c
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,
137      Trypanosoma brucei PRMT7 (TbPRMT7) is a protein arginine methyltransferase (PRMT) that strictly
138                    AtPRMT5 encodes a type II protein arginine methyltransferase (PRMT) that, in winte
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
151                            The major type II protein arginine methyltransferase PRMT5 catalyzes the f
152               Here, we show that the type-II protein arginine methyltransferase PRMT5 controls H4R3me
153                                              Protein arginine methyltransferase PRMT5 interacts with
154     Among the target genes, we confirmed the protein arginine methyltransferase Prmt5 is a direct tar
155                                          The protein arginine methyltransferase PRMT5 is complexed wi
156                                  The type II protein arginine methyltransferase Prmt5 symmetrically d
157 cancer cells is impaired by depletion of the protein arginine methyltransferase PRMT5.
158  we have functionally analyzed two different protein arginine methyltransferases, Prmt5 and Prmt4, bo
159                                        Human protein arginine methyltransferase PRMT8 has been recent
160 ion during flagellar dynamics, we focused on protein arginine methyltransferases (PRMTs) 1, 3, 5, and
161                                              Protein arginine methyltransferases (PRMTs) affect many
162                                              Protein arginine methyltransferases (PRMTs) aid in the r
163  proteins methylated on arginine residues by protein arginine methyltransferases (PRMTs) and is degra
164                                              Protein arginine methyltransferases (PRMTs) are (S)-aden
165                                          The protein arginine methyltransferases (PRMTs) are a family
166                                              Protein arginine methyltransferases (PRMTs) are a group
167                                              Protein arginine methyltransferases (PRMTs) are enzymes
168   Well-characterized selective inhibitors of protein arginine methyltransferases (PRMTs) are invaluab
169                                              Protein arginine methyltransferases (PRMTs) are proved t
170                                              Protein arginine methyltransferases (PRMTs) are SAM-depe
171                             Misregulation of protein arginine methyltransferases (PRMTs) has been lin
172                                              Protein arginine methyltransferases (PRMTs) have been im
173                                              Protein arginine methyltransferases (PRMTs) have emerged
174         Covalent modification of histones by protein arginine methyltransferases (PRMTs) impacts geno
175 stone lysine methyltransferases (HKMTs), and protein arginine methyltransferases (PRMTs) in pancreati
176                                          The protein arginine methyltransferases (PRMTs) include a fa
177                                              Protein arginine methyltransferases (PRMTs) introduce ar
178                               Malfunction of protein arginine methyltransferases (PRMTs) is correlate
179 oper epigenetic modification of chromatin by protein arginine methyltransferases (PRMTs) is crucial f
180                                              Protein arginine methyltransferases (PRMTs) mediate the
181                                              Protein arginine methyltransferases (PRMTs) mediate the
182                                              Protein arginine methyltransferases (PRMTs) play an impo
183                                              Protein arginine methyltransferases (PRMTs) play importa
184                                              Protein arginine methyltransferases (PRMTs) represent an
185 onal modification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs) that are typ
186                             In the family of protein arginine methyltransferases (PRMTs) that predomi
187                   Using purified recombinant protein arginine methyltransferases (PRMTs), we showed t
188 ication of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs).
189  unrelated Rossman-fold enzymes that include protein arginine methyltransferases (PRMTs).
190 rotein lysine methyltransferases (PKMTs) and protein arginine methyltransferases (PRMTs).
191 in lysine methyltransferases (PKMTs) and the protein arginine methyltransferases (PRMTs).
192 an interplay between the SWI/SNF complex and protein-arginine methyltransferases (PRMTs).
193              Depletion of PRMT5, the primary protein arginine methyltransferase responsible for symme
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
196                                          The protein arginine methyltransferase, TbPRMT1, interacts w
197 id not cooperate with PRMT1, a CARM1-related protein arginine methyltransferase that also functions a
198                      PRMT5 encodes a type II protein arginine methyltransferase that catalyzes the sy
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
201                         CARM1 is one of nine protein arginine methyltransferases that methylate argin
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
205           IL-4 upregulates the expression of protein arginine methyltransferases, which are essential
206                                              Protein arginine methyltransferases, which catalyze the
207 omolog of a recently characterized mammalian protein-arginine methyltransferase whose activity may be
208                           PRMT5 is a type II protein arginine methyltransferase with roles in stem ce

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