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Volumn 24, Issue C, 2006, Pages 31-50

2 The family of protein arginine metkyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 77956700786     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6047(06)80004-1     Document Type: Article
Times cited : (6)

References (112)
  • 2
    • 0014200317 scopus 로고
    • Enzymatic methylation of protein fractions from calf thymus nuclei
    • Paik W.K., and Kim S. Enzymatic methylation of protein fractions from calf thymus nuclei. Biochem Biophys Res Commun 29 (1967) 14-20
    • (1967) Biochem Biophys Res Commun , vol.29 , pp. 14-20
    • Paik, W.K.1    Kim, S.2
  • 3
    • 33947482638 scopus 로고
    • The occurrence of epsilon-N-methyl lysine in histones
    • Murray K. The occurrence of epsilon-N-methyl lysine in histones. Biochemistry 127 (1964) 10-15
    • (1964) Biochemistry , vol.127 , pp. 10-15
    • Murray, K.1
  • 5
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey V.G., Faulkner R., and Mirsky A.E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 51 (1964) 786-794
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 6
    • 0014409081 scopus 로고
    • Protein methylase I. Purification and properties of the enzyme
    • Paik W.K., and Kim S. Protein methylase I. Purification and properties of the enzyme. J Biol Chem 243 (1968) 2108-2114
    • (1968) J Biol Chem , vol.243 , pp. 2108-2114
    • Paik, W.K.1    Kim, S.2
  • 7
    • 0015239801 scopus 로고
    • Methylation of arginine and lysine residues of cerebral proteins
    • Kakimoto Y. Methylation of arginine and lysine residues of cerebral proteins. Biochim Biophys Ada 243 (1971) 31-37
    • (1971) Biochim Biophys Ada , vol.243 , pp. 31-37
    • Kakimoto, Y.1
  • 8
    • 0014940650 scopus 로고
    • Isolation and identification of N-G,N-G- and N-G, N′-G-dimethyl-arginine, N-epsilon-mono-, di-, and trimethyllysine, and glucosylgalactosyl- and galactosyl-delta-hydroxylysine from human urine
    • Kakimoto Y., and Akazawa S. Isolation and identification of N-G,N-G- and N-G, N′-G-dimethyl-arginine, N-epsilon-mono-, di-, and trimethyllysine, and glucosylgalactosyl- and galactosyl-delta-hydroxylysine from human urine. J Biol Chem 245 (1970) 5751-5758
    • (1970) J Biol Chem , vol.245 , pp. 5751-5758
    • Kakimoto, Y.1    Akazawa, S.2
  • 9
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary J.D., and Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog Nucleic Acid Res Mol Biol 61 (1998) 65-131
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 10
    • 0017624167 scopus 로고
    • Distribution of NG, NG,-dimethylarginine in nuclear protein fractions
    • Boffa L.C., Karn J., Vidali G., and Allfrey V.G. Distribution of NG, NG,-dimethylarginine in nuclear protein fractions. Biochem Biophys Res Commun 74 (1977) 969-976
    • (1977) Biochem Biophys Res Commun , vol.74 , pp. 969-976
    • Boffa, L.C.1    Karn, J.2    Vidali, G.3    Allfrey, V.G.4
  • 11
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Liu Q., and Dreyfuss G. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol Cell Biol 15 (1995) 2800-2808
    • (1995) Mol Cell Biol , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 12
    • 0015237051 scopus 로고
    • Isolation and identification of N-G-monomethyl, N-G, N-G-dimethyl- and N-G,N′ G-dimethylarginine from the hydrolysate of proteins of bovine brain
    • Nakajima T., Matsuoka Y., and Kakimoto Y. Isolation and identification of N-G-monomethyl, N-G, N-G-dimethyl- and N-G,N′ G-dimethylarginine from the hydrolysate of proteins of bovine brain. Biochim Biophys Ada 230 (1971) 212-222
    • (1971) Biochim Biophys Ada , vol.230 , pp. 212-222
    • Nakajima, T.1    Matsuoka, Y.2    Kakimoto, Y.3
  • 13
    • 0016809905 scopus 로고
    • Methylated amino acid residues of proteins of brain and other organs
    • Kakimoto Y., Matsuoka Y., Miyake M., and Konishi H. Methylated amino acid residues of proteins of brain and other organs. J Neurochem 24 (1975) 893-902
    • (1975) J Neurochem , vol.24 , pp. 893-902
    • Kakimoto, Y.1    Matsuoka, Y.2    Miyake, M.3    Konishi, H.4
  • 14
    • 0015593717 scopus 로고
    • Protein methylation by cerebral tissue
    • Miyake M., and Kakimoto Y. Protein methylation by cerebral tissue. J Neurochem 20 (1973) 859-871
    • (1973) J Neurochem , vol.20 , pp. 859-871
    • Miyake, M.1    Kakimoto, Y.2
  • 15
    • 1642284876 scopus 로고    scopus 로고
    • Automated identification of putative methyltransferases from genomic open reading frames
    • Katz J.E., Dlakic M., and Clarke S. Automated identification of putative methyltransferases from genomic open reading frames. Mol Cell Proteomics 2 (2003) 525-540
    • (2003) Mol Cell Proteomics , vol.2 , pp. 525-540
    • Katz, J.E.1    Dlakic, M.2    Clarke, S.3
  • 16
    • 0033534476 scopus 로고    scopus 로고
    • S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase
    • Niewmierzycka A., and Clarke S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J Biol Chem 274 (1999) 814-824
    • (1999) J Biol Chem , vol.274 , pp. 814-824
    • Niewmierzycka, A.1    Clarke, S.2
  • 17
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., and Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J Biol Chem 277 (2002) 3537-3543
    • (2002) J Biol Chem , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 18
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: protein methylation at arginine comes of age
    • McBride A.E., and Silver P.A. State of the arg: protein methylation at arginine comes of age. Cell 106 (2001) 5-8
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 20
    • 4744340527 scopus 로고    scopus 로고
    • Identification and phylogenetic analyses of the protein arginine methyltransferase gene family in fish and ascidians
    • Hung C.M., and Li C. Identification and phylogenetic analyses of the protein arginine methyltransferase gene family in fish and ascidians. Gene 340 (2004) 179-187
    • (2004) Gene , vol.340 , pp. 179-187
    • Hung, C.M.1    Li, C.2
  • 21
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin W.J., Gary J.D., Yang M.C., Clarke S., and Herschman H.R. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem 271 (1996) 15034-15044
    • (1996) J Biol Chem , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 23
    • 0031025092 scopus 로고    scopus 로고
    • A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
    • Abramovich C., Yakobson B., Chebath J., and Revel M. A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. Embo J 16 (1997) 260-266
    • (1997) Embo J , vol.16 , pp. 260-266
    • Abramovich, C.1    Yakobson, B.2    Chebath, J.3    Revel, M.4
  • 24
    • 0034687558 scopus 로고    scopus 로고
    • Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene [in-process citation]
    • Scorilas A., Black M.H., Talieri M., and Diamandis E.P. Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene [in-process citation]. Biochem Biophys Res Commun 278 (2000) 349-359
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 349-359
    • Scorilas, A.1    Black, M.H.2    Talieri, M.3    Diamandis, E.P.4
  • 25
    • 0037244282 scopus 로고    scopus 로고
    • Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1
    • Cote J., Boisvert F.M., Boulanger M.C., Bedford M.T., and Richard S. Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. Mol Biol Cell 14 (2003) 274-287
    • (2003) Mol Biol Cell , vol.14 , pp. 274-287
    • Cote, J.1    Boisvert, F.M.2    Boulanger, M.C.3    Bedford, M.T.4    Richard, S.5
  • 26
    • 10344243548 scopus 로고    scopus 로고
    • Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1
    • Herrmann F., Bossert M., Schwander A., Akgun E., and Fackelmayer F.O. Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1. J Biol Chem 279 (2004) 48774-48779
    • (2004) J Biol Chem , vol.279 , pp. 48774-48779
    • Herrmann, F.1    Bossert, M.2    Schwander, A.3    Akgun, E.4    Fackelmayer, F.O.5
  • 27
    • 0034717290 scopus 로고    scopus 로고
    • Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains
    • Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., and Richard S. Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J Biol Chem 275 (2000) 16030-16036
    • (2000) J Biol Chem , vol.275 , pp. 16030-16036
    • Bedford, M.T.1    Frankel, A.2    Yaffe, M.B.3    Clarke, S.4    Leder, P.5    Richard, S.6
  • 30
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by pi60 coactivators and two coactivators with protein methyltransferase activities
    • Koh S.S., Chen D., Lee Y.H., and Stallcup M.R. Synergistic enhancement of nuclear receptor function by pi60 coactivators and two coactivators with protein methyltransferase activities. J Biol Chem 276 (2001) 1089-1098
    • (2001) J Biol Chem , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 31
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W., Kim J., and Roeder R.G. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117 (2004) 735-748
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 32
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 34
    • 0034045559 scopus 로고    scopus 로고
    • Arginine N-methyltransferase 1 is required for early postimplantation mousedevelopment, but cells deficient in the enzyme are viable
    • Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., and Ruley H.E. Arginine N-methyltransferase 1 is required for early postimplantation mousedevelopment, but cells deficient in the enzyme are viable. Mol Cell Biol 20 (2000) 4859-4869
    • (2000) Mol Cell Biol , vol.20 , pp. 4859-4869
    • Pawlak, M.R.1    Scherer, C.A.2    Chen, J.3    Roshon, M.J.4    Ruley, H.E.5
  • 35
    • 0036031888 scopus 로고    scopus 로고
    • Protein arginine methyltransferase I: substrate specificity and role in hnRNP assembly
    • Pawlak M.R., Banik-Maiti S., Pietenpol J.A., and Ruley H.E. Protein arginine methyltransferase I: substrate specificity and role in hnRNP assembly. J Cell Biochem 87 (2002) 394-407
    • (2002) J Cell Biochem , vol.87 , pp. 394-407
    • Pawlak, M.R.1    Banik-Maiti, S.2    Pietenpol, J.A.3    Ruley, H.E.4
  • 36
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1and analysis of its binding to substrate peptides
    • Zhang X., and Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1and analysis of its binding to substrate peptides. Structure (Camb) 11 (2003) 509-520
    • (2003) Structure (Camb) , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 37
    • 0031177791 scopus 로고    scopus 로고
    • Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene
    • Katsanis N., Yaspo M.L., and Fisher E.M. Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene. Mamm Genome 8 (1997) 526-529
    • (1997) Mamm Genome , vol.8 , pp. 526-529
    • Katsanis, N.1    Yaspo, M.L.2    Fisher, E.M.3
  • 38
    • 0032521176 scopus 로고    scopus 로고
    • Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)
    • Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., and Henry M.F. Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Gerwmics 48 (1998) 330-340
    • (1998) Gerwmics , vol.48 , pp. 330-340
    • Scott, H.S.1    Antonarakis, S.E.2    Lalioti, M.D.3    Rossier, C.4    Silver, P.A.5    Henry, M.F.6
  • 39
    • 0028915798 scopus 로고
    • Proline-rich sequences that bind to Src homology 3 domains with individual specificities
    • Alexandropoulos K., Cheng G., and Baltimore D. Proline-rich sequences that bind to Src homology 3 domains with individual specificities. Proc Natl Acad Sci USA 92 (1995) 3110-3114
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3110-3114
    • Alexandropoulos, K.1    Cheng, G.2    Baltimore, D.3
  • 40
    • 0035447135 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1
    • Kzhyshkowska J., Schutt H., Liss M., Kremmer E., Stauber R., Wolf H., and Dobner T. Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1. Biochem J 358 (2001) 305-314
    • (2001) Biochem J , vol.358 , pp. 305-314
    • Kzhyshkowska, J.1    Schutt, H.2    Liss, M.3    Kremmer, E.4    Stauber, R.5    Wolf, H.6    Dobner, T.7
  • 41
    • 0037047399 scopus 로고    scopus 로고
    • Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha
    • Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., and Zhu Y.J. Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J Biol Chem 277 (2002) 28624-28630
    • (2002) J Biol Chem , vol.277 , pp. 28624-28630
    • Qi, C.1    Chang, J.2    Zhu, Y.3    Yeldandi, A.V.4    Rao, S.M.5    Zhu, Y.J.6
  • 42
    • 0032479171 scopus 로고    scopus 로고
    • PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
    • Tang J., Gary J.D., Clarke S., and Herschman H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem 273 (1998) 16935-16945
    • (1998) J Biol Chem , vol.273 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 43
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., and Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J Biol Chem 277 (2002) 3537-3543
    • (2002) J Biol Chem , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 44
    • 0034693140 scopus 로고    scopus 로고
    • PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain
    • Frankel A., and Clarke S. PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain. J Biol Chem 275 (2000) 32974-32982
    • (2000) J Biol Chem , vol.275 , pp. 32974-32982
    • Frankel, A.1    Clarke, S.2
  • 45
    • 14244255860 scopus 로고    scopus 로고
    • Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)
    • Swiercz R., Person M.D., and Bedford M.T. Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Biochem J 386 (2005) 85-91
    • (2005) Biochem J , vol.386 , pp. 85-91
    • Swiercz, R.1    Person, M.D.2    Bedford, M.T.3
  • 46
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits
    • Bachand F., and Silver P.A. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. Embo J 23 (2004) 2641-2650
    • (2004) Embo J , vol.23 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 47
    • 7644222810 scopus 로고    scopus 로고
    • DAL-1/4.IB tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in viv
    • Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., and Newsham I.F. DAL-1/4.IB tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in viv. Oncogene 23 (2004) 7761-7771
    • (2004) Oncogene , vol.23 , pp. 7761-7771
    • Singh, V.1    Miranda, T.B.2    Jiang, W.3    Frankel, A.4    Roemer, M.E.5    Robb, V.A.6    Gutmann, D.H.7    Herschman, H.R.8    Clarke, S.9    Newsham, I.F.10
  • 50
    • 0037107417 scopus 로고    scopus 로고
    • Control of CBP co-activating activity by arginine methylation
    • Chevillard-Briet M., Trouche D., and Vandel L. Control of CBP co-activating activity by arginine methylation. Embo J 21 (2002) 5457-5466
    • (2002) Embo J , vol.21 , pp. 5457-5466
    • Chevillard-Briet, M.1    Trouche, D.2    Vandel, L.3
  • 51
    • 14844360649 scopus 로고    scopus 로고
    • Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination
    • Lee Y.H., Coonrod S.A., Kraus W.L., Jelinek M.A., and Stallcup M.R. Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Proc Natl Acad Sci USA 102 (2005) 3611-3616
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3611-3616
    • Lee, Y.H.1    Coonrod, S.A.2    Kraus, W.L.3    Jelinek, M.A.4    Stallcup, M.R.5
  • 53
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities
    • Lee Y.H., Koh S.S., Zhang X., Cheng X., and Stallcup M.R. Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities. Mol Cell Biol 22 (2002) 3621-3632
    • (2002) Mol Cell Biol , vol.22 , pp. 3621-3632
    • Lee, Y.H.1    Koh, S.S.2    Zhang, X.3    Cheng, X.4    Stallcup, M.R.5
  • 54
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between CARM1 methylation and CBP acetylation on histone H3
    • Daujat S., Bauer U.M., Shah V., Turner B., Berger S., and Kouzarides T. Crosstalk between CARM1 methylation and CBP acetylation on histone H3. Curr Biol 12 (2002) 2090-2097
    • (2002) Curr Biol , vol.12 , pp. 2090-2097
    • Daujat, S.1    Bauer, U.M.2    Shah, V.3    Turner, B.4    Berger, S.5    Kouzarides, T.6
  • 55
    • 0036205436 scopus 로고    scopus 로고
    • PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays
    • Lee J., and Bedford M.T. PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays. EMBO Rep 3 (2002) 268-273
    • (2002) EMBO Rep , vol.3 , pp. 268-273
    • Lee, J.1    Bedford, M.T.2
  • 56
    • 0037040245 scopus 로고    scopus 로고
    • The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2
    • Chen S.L., Loffler K.A., Chen D., Stallcup M.R., and Muscat G.E. The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2. J Biol Chem 277 (2002) 4324-4333
    • (2002) J Biol Chem , vol.277 , pp. 4324-4333
    • Chen, S.L.1    Loffler, K.A.2    Chen, D.3    Stallcup, M.R.4    Muscat, G.E.5
  • 57
    • 0037135602 scopus 로고    scopus 로고
    • Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptional activators
    • Koh S.S., Li H., Lee Y.H., Widelitz R.B., Chuong C.M., and Stallcup M.R. Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptional activators. J Biol Chem 277 (2002) 26031-26035
    • (2002) J Biol Chem , vol.277 , pp. 26031-26035
    • Koh, S.S.1    Li, H.2    Lee, Y.H.3    Widelitz, R.B.4    Chuong, C.M.5    Stallcup, M.R.6
  • 60
    • 0038313055 scopus 로고    scopus 로고
    • Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
    • Yadav N., Lee J., Kim J., Shen J., Hu M.C., Aldaz C.M., and Bedford M.T. Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice. Proc Natl Acad Sci USA 100 (2003) 6464-6468
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6464-6468
    • Yadav, N.1    Lee, J.2    Kim, J.3    Shen, J.4    Hu, M.C.5    Aldaz, C.M.6    Bedford, M.T.7
  • 61
    • 2942537778 scopus 로고    scopus 로고
    • Loss of CARM1 results in hypomethylation of TARPP and deregulated early T cell development
    • Kim J., Lee J., Yadav N., Wu Q., Carter C., Richard S., Richie E., and Bedford M.T. Loss of CARM1 results in hypomethylation of TARPP and deregulated early T cell development. J Biol Chem 279 (2004) 25339-25344
    • (2004) J Biol Chem , vol.279 , pp. 25339-25344
    • Kim, J.1    Lee, J.2    Yadav, N.3    Wu, Q.4    Carter, C.5    Richard, S.6    Richie, E.7    Bedford, M.T.8
  • 62
    • 2442614108 scopus 로고    scopus 로고
    • An arginine-histone methyltransferase, CARMER, coordinates ecdysone-mediated apoptosis in Drosophila cells
    • Cakouros D., Daish T.J., Mills K., and Kumar S. An arginine-histone methyltransferase, CARMER, coordinates ecdysone-mediated apoptosis in Drosophila cells. J Biol Chem 279 (2004) 18467-18471
    • (2004) J Biol Chem , vol.279 , pp. 18467-18471
    • Cakouros, D.1    Daish, T.J.2    Mills, K.3    Kumar, S.4
  • 63
    • 3042536209 scopus 로고    scopus 로고
    • Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status
    • Hong H., Kao C., Jeng M.H., Eble J.N., Koch M.O., Gardner T.A., Zhang S., Li L., Pan C.X., Hu Z., Maclennan G.T., and Cheng L. Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status. Cancer 101 (2004) 83-89
    • (2004) Cancer , vol.101 , pp. 83-89
    • Hong, H.1    Kao, C.2    Jeng, M.H.3    Eble, J.N.4    Koch, M.O.5    Gardner, T.A.6    Zhang, S.7    Li, L.8    Pan, C.X.9    Hu, Z.10    Maclennan, G.T.11    Cheng, L.12
  • 64
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skbl and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., and Pestka S. The human homologue of the yeast proteins Skbl and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J Biol Chem 274 (1999) 31531-31542
    • (1999) J Biol Chem , vol.274 , pp. 31531-31542
    • Pollack, B.P.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 65
    • 0035980018 scopus 로고    scopus 로고
    • Prmt5 (janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • Branscombe T.L., Frankel A., Lee J.H., Cook J.R., Yang Z., Pestka S., and Clarke S. Prmt5 (janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J Biol Chem 276 (2001) 32971-32976
    • (2001) J Biol Chem , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1    Frankel, A.2    Lee, J.H.3    Cook, J.R.4    Yang, Z.5    Pestka, S.6    Clarke, S.7
  • 66
    • 0035815625 scopus 로고    scopus 로고
    • Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
    • Rho J., Choi S., Seong Y.R., Cho W.K., Kim S.H., and Im D.S. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. J Biol Chem 276 (2001) 11393-11401
    • (2001) J Biol Chem , vol.276 , pp. 11393-11401
    • Rho, J.1    Choi, S.2    Seong, Y.R.3    Cho, W.K.4    Kim, S.H.5    Im, D.S.6
  • 68
    • 0037623333 scopus 로고    scopus 로고
    • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties
    • Kwak Y.T., Guo J., Prajapati S., Park K.J., Surabhi R.M., Miller B., Gehrig P., and Gaynor R.B. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell 11 (2003) 1055-1066
    • (2003) Mol Cell , vol.11 , pp. 1055-1066
    • Kwak, Y.T.1    Guo, J.2    Prajapati, S.3    Park, K.J.4    Surabhi, R.M.5    Miller, B.6    Gehrig, P.7    Gaynor, R.B.8
  • 69
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., and Sif S. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 24 (2004) 9630-9645
    • (2004) Mol Cell Biol , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 70
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • Friesen W.J., Massenet S., Paushkin S., Wyce A., and Dreyfuss G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol Cell 7 (2001) 1111-1117
    • (2001) Mol Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 74
    • 4644288470 scopus 로고    scopus 로고
    • Techniques in protein methylation
    • Lee J., Cheng D., and Bedford M.T. Techniques in protein methylation. Methods Mol Biol 284 (2004) 195-208
    • (2004) Methods Mol Biol , vol.284 , pp. 195-208
    • Lee, J.1    Cheng, D.2    Bedford, M.T.3
  • 76
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • Miranda T.B., Miranda M., Frankel A., and Clarke S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J Biol Chem (2004)
    • (2004) J Biol Chem
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 78
    • 0037224585 scopus 로고    scopus 로고
    • Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents
    • Gros L., Delaporte C., Frey S., Decesse J., de Saint-Vincent B.R., Cavarec L., Dubart A., Gudkov A.V., and Jacquemin-Sablon A. Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents. Cancer Res 63 (2003) 164-171
    • (2003) Cancer Res , vol.63 , pp. 164-171
    • Gros, L.1    Delaporte, C.2    Frey, S.3    Decesse, J.4    de Saint-Vincent, B.R.5    Cavarec, L.6    Dubart, A.7    Gudkov, A.V.8    Jacquemin-Sablon, A.9
  • 80
    • 25444463928 scopus 로고    scopus 로고
    • PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family
    • (in press)
    • (in press). Lee J., Sayegh J., Daniel J., Clarke S., and Bedford M.T. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem (2005)
    • (2005) J Biol Chem
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 81
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation an emerging regulator of protein function
    • Bedford M.T., and Richard S. Arginine methylation an emerging regulator of protein function. Mol Cell 18 (2005) 263-272
    • (2005) Mol Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 82
    • 33645607060 scopus 로고    scopus 로고
    • Protein interfaces in signaling regulated by arginine methylation
    • Boisvert F.M., Chenard C.A., and Richard S. Protein interfaces in signaling regulated by arginine methylation. Sci STKE 271 2 (2005) 1-10
    • (2005) Sci STKE , vol.271 , Issue.2 , pp. 1-10
    • Boisvert, F.M.1    Chenard, C.A.2    Richard, S.3
  • 83
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
    • Blatch G.L., and Lassie M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 21 (1999) 932-939
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassie, M.2
  • 84
    • 17544376743 scopus 로고    scopus 로고
    • The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae
    • Gary J.D., Lin W.J., Yang M.C., Herschman H.R., and Clarke S. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J Biol Chem 271 (1996) 12585-12594
    • (1996) J Biol Chem , vol.271 , pp. 12585-12594
    • Gary, J.D.1    Lin, W.J.2    Yang, M.C.3    Herschman, H.R.4    Clarke, S.5
  • 85
    • 0029927085 scopus 로고    scopus 로고
    • A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins
    • Henry M.F., and Silver P.A. A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins. Mol Cell Biol 16 (1996) 3668-3678
    • (1996) Mol Cell Biol , vol.16 , pp. 3668-3678
    • Henry, M.F.1    Silver, P.A.2
  • 87
    • 0037040895 scopus 로고    scopus 로고
    • Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p
    • Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., and Corbett A.H. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J Biol Chem 277 (2002) 7752-7760
    • (2002) J Biol Chem , vol.277 , pp. 7752-7760
    • Green, D.M.1    Marfatia, K.A.2    Crafton, E.B.3    Zhang, X.4    Cheng, X.5    Corbett, A.H.6
  • 88
    • 0034602960 scopus 로고    scopus 로고
    • Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions
    • McBride A.E., Weiss V.H., Kim H.K., Hogle J.M., and Silver P.A. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J Biol Chem 275 (2000) 3128-3136
    • (2000) J Biol Chem , vol.275 , pp. 3128-3136
    • McBride, A.E.1    Weiss, V.H.2    Kim, H.K.3    Hogle, J.M.4    Silver, P.A.5
  • 90
    • 0034693216 scopus 로고    scopus 로고
    • Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p
    • Inoue K., Mizuno T., Wada K., and Hagiwara M. Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and inhibit the arginine methylation of Npl3p. J Biol Chem 275 (2000) 32793-32799
    • (2000) J Biol Chem , vol.275 , pp. 32793-32799
    • Inoue, K.1    Mizuno, T.2    Wada, K.3    Hagiwara, M.4
  • 91
    • 0034698665 scopus 로고    scopus 로고
    • Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae
    • Yun C.Y., and Fu X.D. Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. J Cell Biol 150 (2000) 707-718
    • (2000) J Cell Biol , vol.150 , pp. 707-718
    • Yun, C.Y.1    Fu, X.D.2
  • 92
    • 10044237933 scopus 로고    scopus 로고
    • Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p
    • Xu C., and Henry M.F. Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p. Mol Cell Biol 24 (2004) 10742-10756
    • (2004) Mol Cell Biol , vol.24 , pp. 10742-10756
    • Xu, C.1    Henry, M.F.2
  • 93
    • 24744432516 scopus 로고    scopus 로고
    • Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export and intranuclear protein interactions
    • (in press)
    • (in press). McBride A.E., Cook J.T., Stemmler E.A., Rutledge K.L., Mcgrath K.A., and Rubens J.A. Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export and intranuclear protein interactions. J Biol Chem (2005)
    • (2005) J Biol Chem
    • McBride, A.E.1    Cook, J.T.2    Stemmler, E.A.3    Rutledge, K.L.4    Mcgrath, K.A.5    Rubens, J.A.6
  • 94
    • 4043129097 scopus 로고    scopus 로고
    • Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors
    • Yu M.C., Bachand R., McBride A.E., Komili S., Casolari J.M., and Silver P.A. Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors. Genes Dev 18 (2004) 2024-2035
    • (2004) Genes Dev , vol.18 , pp. 2024-2035
    • Yu, M.C.1    Bachand, R.2    McBride, A.E.3    Komili, S.4    Casolari, J.M.5    Silver, P.A.6
  • 95
    • 0038813707 scopus 로고    scopus 로고
    • In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p
    • Xu C., Henry P.A., Setya A., and Henry M.F. In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p. RNA 9 (2003) 746-759
    • (2003) RNA , vol.9 , pp. 746-759
    • Xu, C.1    Henry, P.A.2    Setya, A.3    Henry, M.F.4
  • 96
    • 0014938842 scopus 로고
    • Omega-N-methylarginine in protein
    • Paik W.K., and Kim S. Omega-N-methylarginine in protein. J Biol Chem 245 (1970) 88-92
    • (1970) J Biol Chem , vol.245 , pp. 88-92
    • Paik, W.K.1    Kim, S.2
  • 97
    • 0032491583 scopus 로고    scopus 로고
    • delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins
    • Zobel-Thropp P., Gary J.D., and Clarke S. delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins. J Biol Chem 273 (1998) 29283-29286
    • (1998) J Biol Chem , vol.273 , pp. 29283-29286
    • Zobel-Thropp, P.1    Gary, J.D.2    Clarke, S.3
  • 98
    • 0037013283 scopus 로고    scopus 로고
    • Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2
    • Chern M.K., Chang K.N., Liu L.F., Tarn T.C., Liu Y.C., Liang Y.L., and Tarn M.F. Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2. J Biol Chem 277 (2002) 15345-15353
    • (2002) J Biol Chem , vol.277 , pp. 15345-15353
    • Chern, M.K.1    Chang, K.N.2    Liu, L.F.3    Tarn, T.C.4    Liu, Y.C.5    Liang, Y.L.6    Tarn, M.F.7
  • 100
    • 0030474356 scopus 로고    scopus 로고
    • The highly conserved skb1 gene encodes a protein that interacts with Shk1,a fission yeast Ste20/PAK homolog
    • Gilbreth M., Yang P., Wang D., Frost J., Polverino A., Cobb M.H., and Marcus S. The highly conserved skb1 gene encodes a protein that interacts with Shk1,a fission yeast Ste20/PAK homolog. Proc Natl Acad Sci USA 93 (1996) 13802-13807
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13802-13807
    • Gilbreth, M.1    Yang, P.2    Wang, D.3    Frost, J.4    Polverino, A.5    Cobb, M.H.6    Marcus, S.7
  • 101
    • 0029741095 scopus 로고    scopus 로고
    • A search for proteins that interact genetically with histone H3 and H4 aminotermini uncovers novel regulators of the Swel kinase in Saccharomyces cerevisiae
    • Ma X.J., Lu Q., and Grunstein M. A search for proteins that interact genetically with histone H3 and H4 aminotermini uncovers novel regulators of the Swel kinase in Saccharomyces cerevisiae. Genes Dev 10 (1996) 1327-1340
    • (1996) Genes Dev , vol.10 , pp. 1327-1340
    • Ma, X.J.1    Lu, Q.2    Grunstein, M.3
  • 102
    • 0032874877 scopus 로고    scopus 로고
    • The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cyclecontrol of Swe1p degradation by Hsl1p and Hsl7p
    • Mcmillan J.N., Longtine M.S., Sia R.A., Theesfeld C.L., Bardes E.S., Pringle J.R., and Lew D.J. The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cyclecontrol of Swe1p degradation by Hsl1p and Hsl7p. Mol Cell Biol 19 (1999) 6929-6939
    • (1999) Mol Cell Biol , vol.19 , pp. 6929-6939
    • Mcmillan, J.N.1    Longtine, M.S.2    Sia, R.A.3    Theesfeld, C.L.4    Bardes, E.S.5    Pringle, J.R.6    Lew, D.J.7
  • 103
    • 0035158034 scopus 로고    scopus 로고
    • Dynamic localization of the Swel regulator Hsl7 during the Saccharornyces cerevisiae cell cycle
    • Cid V.J., Shulewitz M.J., McDonald K.L., and Thorner J. Dynamic localization of the Swel regulator Hsl7 during the Saccharornyces cerevisiae cell cycle. Mol Biol Cell 12 (2001) 1645-1669
    • (2001) Mol Biol Cell , vol.12 , pp. 1645-1669
    • Cid, V.J.1    Shulewitz, M.J.2    McDonald, K.L.3    Thorner, J.4
  • 104
    • 0027156138 scopus 로고
    • Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins
    • Najbauer J., Johnson B.A., Young A.L., and Aswad D.W. Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins. J Biol Chem 268 (1993) 10501-10509
    • (1993) J Biol Chem , vol.268 , pp. 10501-10509
    • Najbauer, J.1    Johnson, B.A.2    Young, A.L.3    Aswad, D.W.4
  • 105
    • 0348150716 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase
    • Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., and Laird-Offringa I.A. Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. J Biol Chem 277 (2002) 44623-44630
    • (2002) J Biol Chem , vol.277 , pp. 44623-44630
    • Li, H.1    Park, S.2    Kilburn, B.3    Jelinek, M.A.4    Henschen-Edman, A.5    Aswad, D.W.6    Stallcup, M.R.7    Laird-Offringa, I.A.8
  • 106
    • 0026697169 scopus 로고
    • Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62
    • Wong G., Muller O., Clark R., Conroy L., Moran M.F., Polakis P., and McCormick F. Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62. Cell 69 (1992) 551-558
    • (1992) Cell , vol.69 , pp. 551-558
    • Wong, G.1    Muller, O.2    Clark, R.3    Conroy, L.4    Moran, M.F.5    Polakis, P.6    McCormick, F.7
  • 107
    • 0037135695 scopus 로고    scopus 로고
    • Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy
    • Wada K., Inoue K., and Hagiwara M. Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy. Biochim Biophys Acta 1591 (2002) 1-10
    • (2002) Biochim Biophys Acta , vol.1591 , pp. 1-10
    • Wada, K.1    Inoue, K.2    Hagiwara, M.3
  • 109
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong S.-E., Mittler G., and Mann M. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nature Methods 1 (2004) 119-126
    • (2004) Nature Methods , vol.1 , pp. 119-126
    • Ong, S.-E.1    Mittler, G.2    Mann, M.3
  • 110
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang X., Zhou L., and Cheng X. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. Embo J 19 (2000) 3509-3519
    • (2000) Embo J , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 111
    • 0035965747 scopus 로고    scopus 로고
    • Design of allele-specific protein methyltransferase inhibitors
    • Lin Q., Jiang F., Schultz P.G., and Gray N.S. Design of allele-specific protein methyltransferase inhibitors. J Am Chem Soc 123 (2001) 11608-11613
    • (2001) J Am Chem Soc , vol.123 , pp. 11608-11613
    • Lin, Q.1    Jiang, F.2    Schultz, P.G.3    Gray, N.S.4


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