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Volumn 10, Issue 8, 2011, Pages 1013-1022

Protein arginine methylation in parasitic protozoa

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; PARASITE ANTIGEN; PROTEIN ARGININE METHYLTRANSFERASE; PROTOZOAL PROTEIN;

EID: 79961043508     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.05103-11     Document Type: Article
Times cited : (45)

References (152)
  • 1
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An, W., J. Kim, and R. G. Roeder. 2004. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117: 735-748.
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 2
    • 27744501724 scopus 로고    scopus 로고
    • Involvement of a short interspersed element in epigenetic transcriptional silencing of the amoebapore gene in Entamoeba histolytica
    • Anbar, M., et al. 2005. Involvement of a short interspersed element in epigenetic transcriptional silencing of the amoebapore gene in Entamoeba histolytica. Eukaryot. Cell 4:1775-1784.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1775-1784
    • Anbar, M.1
  • 3
    • 0036920394 scopus 로고    scopus 로고
    • Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich region-mediated nucleocytoplasmic distribution
    • Aoki, K., Y. Ishii, K. Matsumoto, and M. Tsujimoto. 2002. Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich region-mediated nucleocytoplasmic distribution. Nucleic Acids Res. 30:5182-5192.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5182-5192
    • Aoki, K.1    Ishii, Y.2    Matsumoto, K.3    Tsujimoto, M.4
  • 4
    • 34250859489 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: From unicellular eukaryotes to humans
    • Bachand, F. 2007. Protein arginine methyltransferases: from unicellular eukaryotes to humans. Eukaryot. Cell 6:889-898.
    • (2007) Eukaryot. Cell , vol.6 , pp. 889-898
    • Bachand, F.1
  • 5
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits
    • Bachand, F., and P. A. Silver. 2004. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. EMBO J. 23:2641-2650.
    • (2004) EMBO J , vol.23 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 6
    • 38349035858 scopus 로고    scopus 로고
    • Arginine methylation at a glance
    • Bedford, M. T. 2007. Arginine methylation at a glance. J. Cell Sci. 120: 4243-4246.
    • (2007) J. Cell Sci , vol.120 , pp. 4243-4246
    • Bedford, M.T.1
  • 7
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • Bedford, M. T., and S. G. Clarke. 2009. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 33:1-13.
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 8
    • 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., et al. 2000. Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J. Biol. Chem. 275:16030-16036.
    • (2000) J. Biol. Chem , vol.275 , pp. 16030-16036
    • Bedford, M.T.1
  • 9
    • 79958283170 scopus 로고    scopus 로고
    • Acyl derivatives of p-aminosulfonamides and dapsone as new inhibitors of the arginine methyltransferase hPRMT1
    • Bissinger, E. M., et al. 2011. Acyl derivatives of p-aminosulfonamides and dapsone as new inhibitors of the arginine methyltransferase hPRMT1. Bioorg. Med. Chem. 19:3717-3731.
    • (2011) Bioorg. Med. Chem , vol.19 , pp. 3717-3731
    • Bissinger, E.M.1
  • 10
    • 33646163933 scopus 로고    scopus 로고
    • Protein arginine methylation in lymphocyte signaling
    • Blanchet, F., B. T. Schurter, and O. Acuto. 2006. Protein arginine methylation in lymphocyte signaling. Curr. Opin. Immunol. 18:321-328.
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 321-328
    • Blanchet, F.1    Schurter, B.T.2    Acuto, O.3
  • 11
    • 33645607060 scopus 로고    scopus 로고
    • Protein interfaces in signaling regulated by arginine methylation
    • Boisvert, F.-M., C. A. Chenard, and S. Richard. 2005. Protein interfaces in signaling regulated by arginine methylation. Sci. STKE 2005:re2.
    • (2005) Sci. STKE
    • Boisvert, F.-M.1    Chenard, C.A.2    Richard, S.3
  • 12
    • 0037164866 scopus 로고    scopus 로고
    • Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing
    • Boisvert, F.-M., et al. 2002. Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing. J. Cell Biol. 159:957-969.
    • (2002) J. Cell Biol , vol.159 , pp. 957-969
    • Boisvert, F.-M.1
  • 14
    • 15444374342 scopus 로고    scopus 로고
    • Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control
    • Boisvert, F.-M., U. Dery, J.-Y. Masson, and S. Richard. 2005. Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev. 19:671-676.
    • (2005) Genes Dev , vol.19 , pp. 671-676
    • Boisvert, F.-M.1    Dery, U.2    Masson, J.-Y.3    Richard, S.4
  • 15
    • 29244456155 scopus 로고    scopus 로고
    • The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity
    • Boisvert, F.-M., A. Rhie, S. Richard, and A. J. Doherty. 2005. The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Cell Cycle 4:1834-1841.
    • (2005) Cell Cycle , vol.4 , pp. 1834-1841
    • Boisvert, F.-M.1    Rhie, A.2    Richard, S.3    Doherty, A.J.4
  • 16
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms, H., L. Meheus, V. de Brabandere, U. Fischer, and R. Luhrmann. 2001. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7:1531-1542.
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    de Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 17
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • Brahms, H., et al. 2000. The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 275:17122-17129.
    • (2000) J. Biol. Chem , vol.275 , pp. 17122-17129
    • Brahms, H.1
  • 18
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • Branscombe, T. L., et al. 2001. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 276:32971-32976.
    • (2001) J. Biol. Chem , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1
  • 19
    • 25444459395 scopus 로고    scopus 로고
    • Golgi and endoplasmic reticulum functions take place in different subcellular compartments of Entamoeba histolytica
    • Bredeston, L. M., C. E. Caffaro, J. Samuelson, and C. B. Hirschberg. 2005. Golgi and endoplasmic reticulum functions take place in different subcellular compartments of Entamoeba histolytica. J. Biol. Chem. 280:32168-32176.
    • (2005) J. Biol. Chem , vol.280 , pp. 32168-32176
    • Bredeston, L.M.1    Caffaro, C.E.2    Samuelson, J.3    Hirschberg, C.B.4
  • 20
    • 33846528971 scopus 로고    scopus 로고
    • Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis
    • Carlton, J. M., et al. 2007. Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis. Science 315:207-212.
    • (2007) Science , vol.315 , pp. 207-212
    • Carlton, J.M.1
  • 21
    • 77249086700 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1)
    • Castellano, S., et al. 2010. Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1). ChemMedChem 5:398-414.
    • (2010) ChemMedChem , vol.5 , pp. 398-414
    • Castellano, S.1
  • 22
    • 77952539696 scopus 로고    scopus 로고
    • Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA
    • Ceman, S., E. Blackwell, and X. Zhang. 2010. Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA. Hum. Mol. Genet. 19:1314-1323.
    • (2010) Hum. Mol. Genet , vol.19 , pp. 1314-1323
    • Ceman, S.1    Blackwell, E.2    Zhang, X.3
  • 23
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang, B., Y. Chen, Y. Zhao, and R. K. Bruick. 2007. JMJD6 is a histone arginine demethylase. Science 318:444-447.
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 24
    • 0033603396 scopus 로고    scopus 로고
    • Regulation of transcription by a protein methyltransferase
    • Chen, D., et al. 1999. Regulation of transcription by a protein methyltransferase. Science 284:2174-2177.
    • (1999) Science , vol.284 , pp. 2174-2177
    • Chen, D.1
  • 25
    • 33846001366 scopus 로고    scopus 로고
    • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
    • Cheng, D., J. Cote, S. Shaaban, and M. T. Bedford. 2007. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol. Cell 25:71-83.
    • (2007) Mol. Cell , vol.25 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 26
    • 35349012982 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias
    • Clayton, C., and M. Shapira. 2007. Post-transcriptional regulation of gene expression in trypanosomes and leishmanias. Mol. Biochem. Parasitol. 156: 93-101.
    • (2007) Mol. Biochem. Parasitol , vol.156 , pp. 93-101
    • Clayton, C.1    Shapira, M.2
  • 27
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Cote, J., and S. Richard. 2005. Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 280:28476-28483.
    • (2005) J. Biol. Chem , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 28
    • 77956802116 scopus 로고    scopus 로고
    • Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum
    • Cui, L., and J. Miao. 2010. Chromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum. Eukaryot. Cell 9:1138-1149.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1138-1149
    • Cui, L.1    Miao, J.2
  • 29
    • 4444372638 scopus 로고    scopus 로고
    • Histone deimination antagonizes arginine methylation
    • Cuthbert, G. L., et al. 2004. Histone deimination antagonizes arginine methylation. Cell 118:545-553.
    • (2004) Cell , vol.118 , pp. 545-553
    • Cuthbert, G.L.1
  • 30
    • 0035900653 scopus 로고    scopus 로고
    • Reconstructing/deconstructing the earliest eukaryotes: How comparative genomics can help
    • Dacks, J. B., and W. F. Doolittle. 2001. Reconstructing/deconstructing the earliest eukaryotes: how comparative genomics can help. Cell 107:419-425.
    • (2001) Cell , vol.107 , pp. 419-425
    • Dacks, J.B.1    Doolittle, W.F.2
  • 32
    • 67049119810 scopus 로고    scopus 로고
    • A straightforward and highly efficient precipitation/ on-pellet digestion procedure coupled with a long gradient nano-LC separation and Orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome
    • Duan, X., et al. 2009. A straightforward and highly efficient precipitation/ on-pellet digestion procedure coupled with a long gradient nano-LC separation and Orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome. J. Proteome Res. 8:2838-2850.
    • (2009) J. Proteome Res , vol.8 , pp. 2838-2850
    • Duan, X.1
  • 33
    • 33846025995 scopus 로고    scopus 로고
    • Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen
    • El-Andaloussi, N., et al. 2007. Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen. FASEB J. 21:26-34.
    • (2007) FASEB J , vol.21 , pp. 26-34
    • El-Andaloussi, N.1
  • 34
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • Embley, T. M., and W. Martin. 2006. Eukaryotic evolution, changes and challenges. Nature 440:623-630.
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 35
    • 67650334164 scopus 로고    scopus 로고
    • Characterization of PRMT1 from Plasmodium falciparum
    • Fan, Q., J. Miao, and L. Cui. 2009. Characterization of PRMT1 from Plasmodium falciparum. Biochem. J. 421:107-118.
    • (2009) Biochem. J , vol.421 , pp. 107-118
    • Fan, Q.1    Miao, J.2    Cui, L.3
  • 36
    • 67649397588 scopus 로고    scopus 로고
    • Epigenetic regulation in African trypanosomes: A new kid on the block
    • Figueiredo, L. M., G. A. M. Cross, and C. J. Janzen. 2009. Epigenetic regulation in African trypanosomes: a new kid on the block. Nat. Rev. Microbiol. 7:504-513.
    • (2009) Nat. Rev. Microbiol , vol.7 , pp. 504-513
    • Figueiredo, L.M.1    Cross, G.A.M.2    Janzen, C.J.3
  • 37
    • 66449092553 scopus 로고    scopus 로고
    • A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei
    • Fisk, J. C., et al. 2009. A type III protein arginine methyltransferase from the protozoan parasite Trypanosoma brucei. J. Biol. Chem. 284:11590-11600.
    • (2009) J. Biol. Chem , vol.284 , pp. 11590-11600
    • Fisk, J.C.1
  • 38
    • 77953801717 scopus 로고    scopus 로고
    • TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei
    • Fisk, J. C., et al. 2010. TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei. Eukaryot. Cell 9:866-877.
    • (2010) Eukaryot. Cell , vol.9 , pp. 866-877
    • Fisk, J.C.1
  • 39
    • 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 S. Clarke. 2000. PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain. J. Biol. Chem. 275:32974-32982.
    • (2000) J. Biol. Chem , vol.275 , pp. 32974-32982
    • Frankel, A.1    Clarke, S.2
  • 40
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel, A., et al. 2002. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277:3537-3543.
    • (2002) J. Biol. Chem , vol.277 , pp. 3537-3543
    • Frankel, A.1
  • 41
    • 33646580357 scopus 로고    scopus 로고
    • Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis
    • Ganesh, L., et al. 2006. Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis. Mol. Cell. Biol. 26:3864-3874.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 3864-3874
    • Ganesh, L.1
  • 42
    • 17544376743 scopus 로고    scopus 로고
    • The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae
    • Gary, J. D., W. J. Lin, M. C. Yang, H. R. Herschman, and S. Clarke. 1996. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J. Biol. Chem. 271:12585-12594.
    • (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
  • 43
    • 34347334624 scopus 로고    scopus 로고
    • Epigenomic modifications predict active promoters and gene structure in Toxoplasma gondii
    • Gissot, M., K. A. Kelly, J. W. Ajioka, J. M. Greally, and K. Kim. 2007. Epigenomic modifications predict active promoters and gene structure in Toxoplasma gondii. PLoS Pathog. 3:e77.
    • (2007) PLoS Pathog , vol.e77 , pp. 3
    • Gissot, M.1    Kelly, K.A.2    Ajioka, J.W.3    Greally, J.M.4    Kim, K.5
  • 44
    • 33746581154 scopus 로고    scopus 로고
    • Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins
    • Goulah, C. C., M. Pelletier, and L. K. Read. 2006. Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins. RNA 12:1545-1555.
    • (2006) RNA , vol.12 , pp. 1545-1555
    • Goulah, C.C.1    Pelletier, M.2    Read, L.K.3
  • 45
    • 34147094091 scopus 로고    scopus 로고
    • Differential effects of arginine methylation on RBP16 mRNA binding, guide RNA (gRNA) binding, and gRNA-containing ribonucleoprotein complex (gRNP) formation
    • Goulah, C. C., and L. K. Read. 2007. Differential effects of arginine methylation on RBP16 mRNA binding, guide RNA (gRNA) binding, and gRNA-containing ribonucleoprotein complex (gRNP) formation. J. Biol. Chem. 282:7181-7190.
    • (2007) J. Biol. Chem , vol.282 , pp. 7181-7190
    • Goulah, C.C.1    Read, L.K.2
  • 46
    • 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., et al. 2002. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J. Biol. Chem. 277:7752-7760.
    • (2002) J. Biol. Chem , vol.277 , pp. 7752-7760
    • Green, D.M.1
  • 47
    • 79959381350 scopus 로고    scopus 로고
    • A role for the arginine methylation of Rad9 in checkpoint control and cellular sensitivity to DNA damage
    • He, W., et al. 2011. A role for the arginine methylation of Rad9 in checkpoint control and cellular sensitivity to DNA damage. Nucleic Acids Res. 39:4719-4727.
    • (2011) Nucleic Acids Res , vol.39 , pp. 4719-4727
    • He, W.1
  • 49
    • 66149108467 scopus 로고    scopus 로고
    • Human protein arginine methyltransferases in vivo-distinct properties of eight canonical members of the PRMT family
    • Herrmann, F., P. Pably, C. Eckerich, M. T. Bedford, and F. O. Fackelmayer. 2009. Human protein arginine methyltransferases in vivo-distinct properties of eight canonical members of the PRMT family. J. Cell Sci. 122:667-677.
    • (2009) J. Cell Sci , vol.122 , pp. 667-677
    • Herrmann, F.1    Pably, P.2    Eckerich, C.3    Bedford, M.T.4    Fackelmayer, F.O.5
  • 50
    • 77957061888 scopus 로고    scopus 로고
    • Interaction of JMJD6 with single-stranded RNA
    • Hong, X., et al. 2010. Interaction of JMJD6 with single-stranded RNA. Proc. Natl. Acad. Sci. U. S. A. 107:14568-14572.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 14568-14572
    • Hong, X.1
  • 51
    • 79551606798 scopus 로고    scopus 로고
    • Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation
    • Hsu, J. M., et al. 2011. Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation. Nat. Cell Biol. 13:174-181.
    • (2011) Nat. Cell Biol , vol.13 , pp. 174-181
    • Hsu, J.M.1
  • 52
  • 53
    • 37249026306 scopus 로고    scopus 로고
    • PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation
    • Hyllus, D., et al. 2007. PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. Genes Dev. 21:3369-3380.
    • (2007) Genes Dev , vol.21 , pp. 3369-3380
    • Hyllus, D.1
  • 54
    • 41249088464 scopus 로고    scopus 로고
    • Arginine methylation of the histone H3 tail impedes effector binding
    • Iberg, A. N., et al. 2008. Arginine methylation of the histone H3 tail impedes effector binding. J. Biol. Chem. 283:3006-3010.
    • (2008) J. Biol. Chem , vol.283 , pp. 3006-3010
    • Iberg, A.N.1
  • 55
    • 34147223386 scopus 로고    scopus 로고
    • Arginine methylation of the HIV-1 nucleocapsid protein results in its diminished function
    • Invernizzi, C. F., et al. 2007. Arginine methylation of the HIV-1 nucleocapsid protein results in its diminished function. AIDS 21:795-805.
    • (2007) AIDS , vol.21 , pp. 795-805
    • Invernizzi, C.F.1
  • 56
    • 33846708629 scopus 로고    scopus 로고
    • PRMT6 diminishes HIV-1Rev binding to and export of viral RNA
    • Invernizzi, C. F., B. Xie, S. Richard, and M. A. Wainberg. 2006. PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA. Retrovirology 3:93.
    • (2006) Retrovirology , vol.3 , pp. 93
    • Invernizzi, C.F.1    Xie, B.2    Richard, S.3    Wainberg, M.A.4
  • 57
    • 77958471611 scopus 로고    scopus 로고
    • Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation
    • Iwasaki, H., et al. 2010. Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation. Circ. Res. 107:992-1001.
    • (2010) Circ. Res , vol.107 , pp. 992-1001
    • Iwasaki, H.1
  • 58
    • 36048994078 scopus 로고    scopus 로고
    • Protein arginine methylation regulates insulin signaling in L6 skeletal muscle cells
    • Iwasaki, H., and T. Yada. 2007. Protein arginine methylation regulates insulin signaling in L6 skeletal muscle cells. Biochem. Biophys. Res. Comm. 364:1015-1021.
    • (2007) Biochem. Biophys. Res. Comm , vol.364 , pp. 1015-1021
    • Iwasaki, H.1    Yada, T.2
  • 59
    • 37049002223 scopus 로고    scopus 로고
    • Comparative genomics of transcription factors and chromatin proteins in parasitic protists and other eukaryotes
    • Iyer, L. M., V. Anantharaman, M. Y. Wolf, and L. Aravind. 2008. Comparative genomics of transcription factors and chromatin proteins in parasitic protists and other eukaryotes. Int. J. Parasitol. 38:1-31.
    • (2008) Int. J. Parasitol , vol.38 , pp. 1-31
    • Iyer, L.M.1    Anantharaman, V.2    Wolf, M.Y.3    Aravind, L.4
  • 60
    • 57049087451 scopus 로고    scopus 로고
    • Arginine methylation regulates the p53 response
    • Jansson, M., et al. 2008. Arginine methylation regulates the p53 response. Nat. Cell Biol. 10:1431-1439.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1431-1439
    • Jansson, M.1
  • 61
    • 33645987019 scopus 로고    scopus 로고
    • Unusual histone modifications in Trypanosoma brucei
    • Janzen, C. J., et al. 2006. Unusual histone modifications in Trypanosoma brucei. FEBS Lett. 580:2306-2310.
    • (2006) FEBS Lett , vol.580 , pp. 2306-2310
    • Janzen, C.J.1
  • 62
    • 33751029979 scopus 로고    scopus 로고
    • The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation
    • Jelinic, P., J.-C. Stehle, and P. Shaw. 2006. The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation. PLoS Biol. 4:e355.
    • (2006) PLoS Biol , vol.4
    • Jelinic, P.1    Stehle, J.-C.2    Shaw, P.3
  • 63
    • 70450253253 scopus 로고    scopus 로고
    • Widespread variation in transcript abundance within and across developmental stages of Trypanosoma brucei
    • Jensen, B. C., D. Sivam, C. T. Kifer, P. Myler, and M. Parsons. 2009. Widespread variation in transcript abundance within and across developmental stages of Trypanosoma brucei. BMC Genomics 10:482-506.
    • (2009) BMC Genomics , vol.10 , pp. 482-506
    • Jensen, B.C.1    Sivam, D.2    Kifer, C.T.3    Myler, P.4    Parsons, M.5
  • 64
    • 0030979290 scopus 로고    scopus 로고
    • Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly- Gly/Phe is a preferred recognition motif
    • Kim, S., et al. 1997. Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly- Gly/Phe is a preferred recognition motif. Biochemistry 36:5185-5192.
    • (1997) Biochemistry , vol.36 , pp. 5185-5192
    • Kim, S.1
  • 65
    • 67349281394 scopus 로고    scopus 로고
    • Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability
    • Kirino, Y., et al. 2009. Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability. Nat. Cell Biol. 11:652-658.
    • (2009) Nat. Cell Biol , vol.11 , pp. 652-658
    • Kirino, Y.1
  • 66
    • 64049102668 scopus 로고    scopus 로고
    • Distinct transcriptional outputs associated with mono- and dimethylated histone H3 arginine 2
    • Kirmizis, A., et al. 2009. Distinct transcriptional outputs associated with mono- and dimethylated histone H3 arginine 2. Nat. Struct. Mol. Biol. 16:449-451.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 449-451
    • Kirmizis, A.1
  • 67
    • 35348986412 scopus 로고    scopus 로고
    • Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation
    • Kirmizis, A., et al. 2007. Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation. Nature 449:928-932.
    • (2007) Nature , vol.449 , pp. 928-932
    • Kirmizis, A.1
  • 68
    • 45549102968 scopus 로고    scopus 로고
    • The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation
    • Kleinschmidt, M. A., G. Streubel, B. Samans, M. Krause, and U.-M. Bauer. 2008. The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation. Nucleic Acids Res. 36:3202-3213.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3202-3213
    • Kleinschmidt, M.A.1    Streubel, G.2    Samans, B.3    Krause, M.4    Bauer, U.-M.5
  • 69
    • 77149151571 scopus 로고    scopus 로고
    • The RNA helicase DHH1 is central to the correct expression of many developmentally regulated mRNAs in trypanosomes
    • Kramer, S., et al. 2010. The RNA helicase DHH1 is central to the correct expression of many developmentally regulated mRNAs in trypanosomes. J. Cell Sci. 123:699-711.
    • (2010) J. Cell Sci , vol.123 , pp. 699-711
    • Kramer, S.1
  • 70
    • 33845896853 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: Evolution and assessment of their pharmacological and therapeutic potential
    • Krause, C. D., et al. 2007. Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol. Ther. 113:50-87.
    • (2007) Pharmacol. Ther , vol.113 , pp. 50-87
    • Krause, C.D.1
  • 71
    • 33645649005 scopus 로고    scopus 로고
    • Signal-dependent control of gluconeogenic key enzyme genes through coactivator-associated arginine methyltransferase 1
    • Krones-Herzig, A., et al. 2006. Signal-dependent control of gluconeogenic key enzyme genes through coactivator-associated arginine methyltransferase 1. J. Biol. Chem. 281:3025-3029.
    • (2006) J. Biol. Chem , vol.281 , pp. 3025-3029
    • Krones-Herzig, A.1
  • 72
    • 0037623333 scopus 로고    scopus 로고
    • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties
    • Kwak, Y. T., et al. 2003. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol. Cell 11:1055-1066.
    • (2003) Mol. Cell , vol.11 , pp. 1055-1066
    • Kwak, Y.T.1
  • 73
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M., and T. Jenuwein. 2002. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14:286-298.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 74
    • 67650882496 scopus 로고    scopus 로고
    • Kinetic analysis of human protein arginine N-methyltransferase 2: Formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4
    • Lakowski, T. M., and A. Frankel. 2009. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem. J. 421:253-261.
    • (2009) Biochem. J , vol.421 , pp. 253-261
    • Lakowski, T.M.1    Frankel, A.2
  • 75
    • 44349099853 scopus 로고    scopus 로고
    • A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism
    • Lakowski, T. M., and A. Frankel. 2008. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism. J. Biol. Chem. 283:10015-10025.
    • (2008) J. Biol. Chem , vol.283 , pp. 10015-10025
    • Lakowski, T.M.1    Frankel, A.2
  • 76
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation in regulation of transcription
    • Lee, D. Y., C. Teyssier, B. D. Strahl, and M. R. Stallcup. 2005. Role of protein methylation in regulation of transcription. Endocrine Rev. 26:147-170.
    • (2005) Endocrine Rev , vol.26 , pp. 147-170
    • Lee, D.Y.1    Teyssier, C.2    Strahl, B.D.3    Stallcup, M.R.4
  • 77
    • 13544277696 scopus 로고    scopus 로고
    • PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine
    • Lee, J.-H., et al. 2005. PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. J. Biol. Chem. 280:3656-3664.
    • (2005) J. Biol. Chem , vol.280 , pp. 3656-3664
    • Lee, J.-H.1
  • 78
    • 25444463928 scopus 로고    scopus 로고
    • PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family
    • Lee, J., J. Sayegh, J. Daniel, S. Clarke, and M. T. Bedford. 2005. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J. Biol. Chem. 280:32890-32896.
    • (2005) J. Biol. Chem , vol.280 , pp. 32890-32896
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 79
    • 0033916067 scopus 로고    scopus 로고
    • Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase
    • Lee, J. H., et al. 2000. Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase. Biochem. Biophys. Res. Comm. 274:105-111.
    • (2000) Biochem. Biophys. Res. Comm , vol.274 , pp. 105-111
    • Lee, J.H.1
  • 80
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: Protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Lee, Y. H., and M. R. Stallcup. 2009. Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation. Mol. Endocrinol. 23:425-433.
    • (2009) Mol. Endocrinol , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 81
    • 0348150716 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase
    • Li, H., et al. 2002. Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. J. Biol. Chem. 277:44623-44630.
    • (2002) J. Biol. Chem , vol.277 , pp. 44623-44630
    • Li, H.1
  • 82
    • 77950390899 scopus 로고    scopus 로고
    • H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation
    • Li, X., et al. 2010. H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation. Blood 115: 2028-2037.
    • (2010) Blood , vol.115 , pp. 2028-2037
    • Li, X.1
  • 83
    • 8644292540 scopus 로고    scopus 로고
    • Hepatitis delta virus antigen is methylated at arginine residues, and methylation regulates subcellular localization and RNA replication
    • Li, Y.-J., M. R. Stallcup, and M. M. C. Lai. 2004. Hepatitis delta virus antigen is methylated at arginine residues, and methylation regulates subcellular localization and RNA replication. J. Virol. 78:13325-13334.
    • (2004) J. Virol , vol.78 , pp. 13325-13334
    • Li, Y.-J.1    Stallcup, M.R.2    Lai, M.M.C.3
  • 84
    • 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., J. D. Gary, M. C. Yang, S. Clarke, and H. R. Herschman. 1996. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 271:15034-15044.
    • (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
  • 85
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Liu, Q., and G. Dreyfuss. 1995. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell. Biol. 15:2800-2808.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 86
    • 79961058405 scopus 로고    scopus 로고
    • The remarkable mitochondrion of trypanosomes and related flagellates
    • In W. de Souza (ed.), Springer-Verlag, Berlin, Germany
    • Lukes, J., H. Hashimi, Z. Verner, and Z. Cicova. 2010. The remarkable mitochondrion of trypanosomes and related flagellates, p. 227-252. In W. de Souza (ed.), Structures and organelles in pathogenic protists, vol. 17. Springer-Verlag, Berlin, Germany.
    • (2010) Structures and Organelles In Pathogenic Protists , vol.17 , pp. 227-252
    • Lukes, J.1    Hashimi, H.2    Verner, Z.3    Cicova, Z.4
  • 87
    • 41849112166 scopus 로고    scopus 로고
    • Synthesis and biological validation of novel synthetic histone/protein methyltransferase inhibitors
    • Mai, A., et al. 2007. Synthesis and biological validation of novel synthetic histone/protein methyltransferase inhibitors. ChemMedChem 2:987-991.
    • (2007) ChemMedChem , vol.2 , pp. 987-991
    • Mai, A.1
  • 88
    • 34548300050 scopus 로고    scopus 로고
    • Histone modifications in Trypanosoma brucei
    • Mandava, V., et al. 2007. Histone modifications in Trypanosoma brucei. Mol. Biochem. Parasitol. 156:41-50.
    • (2007) Mol. Biochem. Parasitol , vol.156 , pp. 41-50
    • Mandava, V.1
  • 89
    • 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., V. H. Weiss, H. K. Kim, J. M. Hogle, and P. A. Silver. 2000. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. 275:3128-3136.
    • (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
    • 34447560908 scopus 로고    scopus 로고
    • Protein arginine methylation in Candida albicans: Role in nuclear transport
    • McBride, A. E., et al. 2007. Protein arginine methylation in Candida albicans: role in nuclear transport. Eukaryot. Cell 6:1119-1129.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1119-1129
    • McBride, A.E.1
  • 91
    • 77956792283 scopus 로고    scopus 로고
    • Epigenetics in Plasmodium: What do we really know
    • Merrick, C. J., and M. T. Duraisingh. 2010. Epigenetics in Plasmodium: what do we really know? Eukaryot. Cell 9:1150-1158.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1150-1158
    • Merrick, C.J.1    Duraisingh, M.T.2
  • 92
    • 33644656442 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum histones: Organization, expression, and acetylation
    • Miao, J., Q. Fan, L. Cui, and J. Li. 2006. The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation. Gene 369: 53-65.
    • (2006) Gene , vol.369 , pp. 53-65
    • Miao, J.1    Fan, Q.2    Cui, L.3    Li, J.4
  • 93
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • Miranda, T. B., M. Miranda, A. Frankel, and S. Clarke. 2004. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 279:22902-22907.
    • (2004) J. Biol. Chem , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 94
    • 34848894621 scopus 로고    scopus 로고
    • Genomic minimalism in the early diverging intestinal parasite Giardia lamblia
    • Morrison, H. G., et al. 2007. Genomic minimalism in the early diverging intestinal parasite Giardia lamblia. Science 317:1921-1926.
    • (2007) Science , vol.317 , pp. 1921-1926
    • Morrison, H.G.1
  • 95
    • 4344629701 scopus 로고    scopus 로고
    • Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes
    • Mowen, K. A., B. T. Schurter, J. W. Fathman, M. David, and L. H. Glimcher. 2004. Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes. Mol. Cell 15:559-571.
    • (2004) Mol. Cell , vol.15 , pp. 559-571
    • Mowen, K.A.1    Schurter, B.T.2    Fathman, J.W.3    David, M.4    Glimcher, L.H.5
  • 96
    • 0035831040 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription
    • Mowen, K. A., et al. 2001. Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription. Cell 104:731-741.
    • (2001) Cell , vol.104 , pp. 731-741
    • Mowen, K.A.1
  • 97
    • 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., B. A. Johnson, A. L. Young, and D. W. Aswad. 1993. 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. 268:10501-10509.
    • (1993) J. Biol. Chem , vol.268 , pp. 10501-10509
    • Najbauer, J.1    Johnson, B.A.2    Young, A.L.3    Aswad, D.W.4
  • 98
    • 0343963070 scopus 로고    scopus 로고
    • The RGG domain in hnRNP A2 affects subcellular localization
    • Nichols, R. C., et al. 2000. The RGG domain in hnRNP A2 affects subcellular localization. Exp. Cell Res. 256:522-532.
    • (2000) Exp. Cell Res , vol.256 , pp. 522-532
    • Nichols, R.C.1
  • 99
    • 0033534476 scopus 로고    scopus 로고
    • S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase
    • Niewmierzycka, A., and S. Clarke. 1999. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274:814-824.
    • (1999) J. Biol. Chem , vol.274 , pp. 814-824
    • Niewmierzycka, A.1    Clarke, S.2
  • 100
    • 23844435269 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase 1, CARM1, affects pre-mRNA splicing in an isoform-specific manner
    • Ohkura, N., M. Takahashi, H. Yaguchi, Y. Nagamura, and T. Tsukada. 2005. Coactivator-associated arginine methyltransferase 1, CARM1, affects pre-mRNA splicing in an isoform-specific manner. J. Biol. Chem. 280: 28927-28935.
    • (2005) J. Biol. Chem , vol.280 , pp. 28927-28935
    • Ohkura, N.1    Takahashi, M.2    Yaguchi, H.3    Nagamura, Y.4    Tsukada, T.5
  • 101
    • 36248991292 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1: Positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis
    • Osborne, T. C., O. Obianyo, X. Zhang, X. Cheng, and P. R. Thompson. 2007. Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis. Biochemistry 46:13370-13381.
    • (2007) Biochemistry , vol.46 , pp. 13370-13381
    • Osborne, T.C.1    Obianyo, O.2    Zhang, X.3    Cheng, X.4    Thompson, P.R.5
  • 102
    • 33845418030 scopus 로고    scopus 로고
    • Protein arginine methylation: Cellular functions and methods of analysis
    • Pahlich, S., R. P. Zakaryan, and H. Gehring. 2006. Protein arginine methylation: cellular functions and methods of analysis. Biochim. Biophys. Acta 1764:1890-1903.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1890-1903
    • Pahlich, S.1    Zakaryan, R.P.2    Gehring, H.3
  • 103
    • 0014600365 scopus 로고
    • Enzymatic methylation of histones
    • Paik, W. K., and S. Kim. 1969. Enzymatic methylation of histones. Arch. Biochem. Biophys. 134:632-637.
    • (1969) Arch. Biochem. Biophys , vol.134 , pp. 632-637
    • Paik, W.K.1    Kim, S.2
  • 104
    • 0014409081 scopus 로고
    • Protein methylase I. Purification and properties of the enzyme
    • Paik, W. K., and S. Kim. 1968. Protein methylase I. Purification and properties of the enzyme. J. Biol. Chem. 243:2108-2114.
    • (1968) J. Biol. Chem , vol.243 , pp. 2108-2114
    • Paik, W.K.1    Kim, S.2
  • 105
    • 0014559733 scopus 로고
    • Protein methylation in rat brain in vitro
    • Paik, W. K., and S. Kim. 1969. Protein methylation in rat brain in vitro. J. Neurochem. 16:1257-1261.
    • (1969) J. Neurochem , vol.16 , pp. 1257-1261
    • Paik, W.K.1    Kim, S.2
  • 106
    • 33847678615 scopus 로고    scopus 로고
    • Historical review: The field of protein methylation
    • Paik, W. K., D. C. Paik, and S. Kim. 2007. Historical review: the field of protein methylation. Trends Biochem. Sci. 32:146-152.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 146-152
    • Paik, W.K.1    Paik, D.C.2    Kim, S.3
  • 107
    • 77649090565 scopus 로고    scopus 로고
    • Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications
    • Pang, C. N., E. Gasteiger, and M. R. Wilkins. 2010. Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications. BMC Genomics 11:92.
    • (2010) BMC Genomics , vol.11 , pp. 92
    • Pang, C.N.1    Gasteiger, E.2    Wilkins, M.R.3
  • 108
    • 34748853038 scopus 로고    scopus 로고
    • Evolutionarily divergent type II protein arginine methyltransferase in Trypanosoma brucei
    • Pasternack, D. A., J. Sayegh, S. Clarke, and L. K. Read. 2007. Evolutionarily divergent type II protein arginine methyltransferase in Trypanosoma brucei. Eukaryot. Cell 6:1665-1681.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1665-1681
    • Pasternack, D.A.1    Sayegh, J.2    Clarke, S.3    Read, L.K.4
  • 109
    • 27644531658 scopus 로고    scopus 로고
    • In vitro and in vivo analysis of the major type I protein arginine methyltransferase from Trypanosoma brucei
    • Pelletier, M., D. A. Pasternack, and L. K. Read. 2005. In vitro and in vivo analysis of the major type I protein arginine methyltransferase from Trypanosoma brucei. Mol. Biochem. Parasitol. 144:206-217.
    • (2005) Mol. Biochem. Parasitol , vol.144 , pp. 206-217
    • Pelletier, M.1    Pasternack, D.A.2    Read, L.K.3
  • 110
    • 0034762135 scopus 로고    scopus 로고
    • Arginine methylation of a mitochondrial guide RNA binding protein from Trypanosoma brucei
    • Pelletier, M., et al. 2001. Arginine methylation of a mitochondrial guide RNA binding protein from Trypanosoma brucei. Mol. Biochem. Parasitol. 118:49-59.
    • (2001) Mol. Biochem. Parasitol , vol.118 , pp. 49-59
    • Pelletier, M.1
  • 111
    • 67649359948 scopus 로고    scopus 로고
    • A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis
    • Perreault, A., S. Gascon, A. D'Amours, J. M. Aletta, and F. Bachand. 2009. A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis. J. Biol. Chem. 284:15026-15037.
    • (2009) J. Biol. Chem , vol.284 , pp. 15026-15037
    • Perreault, A.1    Gascon, S.2    D'amours, A.3    Aletta, J.M.4    Bachand, F.5
  • 112
    • 0035104190 scopus 로고    scopus 로고
    • Low-complexity regions in Plasmodium falciparum proteins
    • Pizzi, E., and C. Frontali. 2001. Low-complexity regions in Plasmodium falciparum proteins. Genome Res. 11:218-229.
    • (2001) Genome Res , vol.11 , pp. 218-229
    • Pizzi, E.1    Frontali, C.2
  • 113
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • Pollack, B. P., et al. 1999. The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J. Biol. Chem. 274:31531-31542.
    • (1999) J. Biol. Chem , vol.274 , pp. 31531-31542
    • Pollack, B.P.1
  • 114
    • 70549084861 scopus 로고    scopus 로고
    • Transcriptome analysis of differentiating trypanosomes reveals the existence of multiple post-transcriptional regulons
    • Queiroz, R., C. Benz, K. Fellenberg, J. D. Hoheisel, and C. Clayton. 2009. Transcriptome analysis of differentiating trypanosomes reveals the existence of multiple post-transcriptional regulons. BMC Genomics 10:495.
    • (2009) BMC Genomics , vol.10 , pp. 495
    • Queiroz, R.1    Benz, C.2    Fellenberg, K.3    Hoheisel, J.D.4    Clayton, C.5
  • 115
    • 33847759102 scopus 로고    scopus 로고
    • Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro
    • Raijmakers, R., et al. 2007. Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro. J. Mol. Biol. 367: 1118-1129.
    • (2007) J. Mol. Biol , vol.367 , pp. 1118-1129
    • Raijmakers, R.1
  • 116
    • 77951217870 scopus 로고    scopus 로고
    • Methylation of ribosomal protein S10 by proteinarginine methyltransferase 5 regulates ribosome biogenesis
    • Ren, J., et al. 2010. Methylation of ribosomal protein S10 by proteinarginine methyltransferase 5 regulates ribosome biogenesis. J. Biol. Chem. 285:12695-12705.
    • (2010) J. Biol. Chem , vol.285 , pp. 12695-12705
    • Ren, J.1
  • 117
    • 34548636476 scopus 로고    scopus 로고
    • Arginine methylation of Sam68 and SLM proteins negatively regulates their poly(U) RNA binding activity
    • Rho, J., S. Choi, C.-R. Jung, and D.-S. Im. 2007. Arginine methylation of Sam68 and SLM proteins negatively regulates their poly(U) RNA binding activity. Arch. Biochem. Biophys. 466:49-57.
    • (2007) Arch. Biochem. Biophys , vol.466 , pp. 49-57
    • Rho, J.1    Choi, S.2    Jung, C.-R.3    Im, D.-S.4
  • 118
    • 33947327864 scopus 로고    scopus 로고
    • hCAF1, a new regulator of PRMT1- dependent arginine methylation
    • Robin-Lespinasse, Y., et al. 2007. hCAF1, a new regulator of PRMT1- dependent arginine methylation. J. Cell Sci. 120:638-647.
    • (2007) J. Cell Sci , vol.120 , pp. 638-647
    • Robin-Lespinasse, Y.1
  • 119
    • 43549096649 scopus 로고    scopus 로고
    • Post-translational modification of cellular proteins during Leishmania donovani differentiation
    • Rosenzweig, D., D. Smith, P. J. Myler, R. W. Olafson, and D. Zilberstein. 2008. Post-translational modification of cellular proteins during Leishmania donovani differentiation. Proteomics 8:1843-1850.
    • (2008) Proteomics , vol.8 , pp. 1843-1850
    • Rosenzweig, D.1    Smith, D.2    Myler, P.J.3    Olafson, R.W.4    Zilberstein, D.5
  • 120
    • 27944481176 scopus 로고    scopus 로고
    • Histone-modifying complexes regulate gene expression pertinent to the differentiation of the protozoan parasite Toxoplasma gondii
    • Saksouk, N., et al. 2005. Histone-modifying complexes regulate gene expression pertinent to the differentiation of the protozoan parasite Toxoplasma gondii. Mol. Cell. Biol. 25:10301-10314.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 10301-10314
    • Saksouk, N.1
  • 121
    • 45449112755 scopus 로고    scopus 로고
    • Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast
    • Sayegh, J., and S. G. Clarke. 2008. Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast. Biochem. Biophys. Res. Comm. 372:811-815.
    • (2008) Biochem. Biophys. Res. Comm , vol.372 , pp. 811-815
    • Sayegh, J.1    Clarke, S.G.2
  • 122
    • 37549043199 scopus 로고    scopus 로고
    • Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain
    • Sayegh, J., K. Webb, D. Cheng, M. T. Bedford, and S. G. Clarke. 2007. Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain. J. Biol. Chem. 282:36444-36453.
    • (2007) J. Biol. Chem , vol.282 , pp. 36444-36453
    • Sayegh, J.1    Webb, K.2    Cheng, D.3    Bedford, M.T.4    Clarke, S.G.5
  • 123
    • 70449723338 scopus 로고    scopus 로고
    • The role of deadenylation in the degradation of unstable mRNAs in trypanosomes
    • Schwede, A., et al. 2009. The role of deadenylation in the degradation of unstable mRNAs in trypanosomes. Nucleic Acids Res. 37:5511-5528.
    • (2009) Nucleic Acids Res , vol.37 , pp. 5511-5528
    • Schwede, A.1
  • 124
    • 0032030939 scopus 로고    scopus 로고
    • Arginine methylation facilitates the nuclear export of hnRNP proteins
    • Shen, E. C., et al. 1998. Arginine methylation facilitates the nuclear export of hnRNP proteins. Genes Dev. 12:679-691.
    • (1998) Genes Dev , vol.12 , pp. 679-691
    • Shen, E.C.1
  • 125
    • 67349234069 scopus 로고    scopus 로고
    • Arginine methylation of ribosomal protein S3 affects ribosome assembly
    • Shin, H. S., et al. 2009. Arginine methylation of ribosomal protein S3 affects ribosome assembly. Biochem. Biophys. Res. Comm. 385:273-278.
    • (2009) Biochem. Biophys. Res. Comm , vol.385 , pp. 273-278
    • Shin, H.S.1
  • 126
    • 0037108318 scopus 로고    scopus 로고
    • Eukaryotic evolution: Getting to the root of the problem
    • Simpson, A. G., and A. J. Roger. 2002. Eukaryotic evolution: getting to the root of the problem. Curr. Biol. 12:R691-R693.
    • (2002) Curr. Biol , vol.12
    • Simpson, A.G.1    Roger, A.J.2
  • 127
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • Sims, R. J., III, K. Nishioka, and D. Reinberg. 2003. Histone lysine methylation: a signature for chromatin function. Trends Genet. 19:629-639.
    • (2003) Trends Genet , vol.19 , pp. 629-639
    • Sims III, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 128
    • 7644222810 scopus 로고    scopus 로고
    • DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo
    • Singh, V., et al. 2004. DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Oncogene 23:7761-7771.
    • (2004) Oncogene , vol.23 , pp. 7761-7771
    • Singh, V.1
  • 129
    • 0039374447 scopus 로고    scopus 로고
    • Unusual sites of arginine methylation in poly(A)- binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3
    • Smith, J. J., et al. 1999. Unusual sites of arginine methylation in poly(A)- binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J. Biol. Chem. 274:13229-13234.
    • (1999) J. Biol. Chem , vol.274 , pp. 13229-13234
    • Smith, J.J.1
  • 130
    • 2542476990 scopus 로고    scopus 로고
    • Arginine methylation of RNA helicase A determines its subcellular localization
    • Smith, W. A., B. T. Schurter, F. Wong-Staal, and M. David. 2004. Arginine methylation of RNA helicase A determines its subcellular localization. J. Biol. Chem. 279:22795-22798.
    • (2004) J. Biol. Chem , vol.279 , pp. 22795-22798
    • Smith, W.A.1    Schurter, B.T.2    Wong-Staal, F.3    David, M.4
  • 131
    • 77950283716 scopus 로고    scopus 로고
    • Epigenetic mechanisms regulate stage differentiation in the minimized protozoan Giardia lamblia
    • Sonda, S., et al. 2010. Epigenetic mechanisms regulate stage differentiation in the minimized protozoan Giardia lamblia. Mol. Microbiol. 76:48-67.
    • (2010) Mol. Microbiol , vol.76 , pp. 48-67
    • Sonda, S.1
  • 132
    • 0035962649 scopus 로고    scopus 로고
    • Role of protein methylation in chromatin remodeling and transcriptional regulation
    • Stallcup, M. R. 2001. Role of protein methylation in chromatin remodeling and transcriptional regulation. Oncogene 20:3014-3020.
    • (2001) Oncogene , vol.20 , pp. 3014-3020
    • Stallcup, M.R.1
  • 133
    • 33748856576 scopus 로고    scopus 로고
    • Chromosome-wide analysis of gene function by RNA interference in the African trypanosome
    • Subramaniam, C., et al. 2006. Chromosome-wide analysis of gene function by RNA interference in the African trypanosome. Eukaryot. Cell 5:1539-1549.
    • (2006) Eukaryot. Cell , vol.5 , pp. 1539-1549
    • Subramaniam, C.1
  • 134
    • 34447119527 scopus 로고    scopus 로고
    • Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice
    • Swiercz, R., D. Cheng, D. Kim, and M. T. Bedford. 2007. Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice. J. Biol. Chem. 282: 16917-16923.
    • (2007) J. Biol. Chem , vol.282 , pp. 16917-16923
    • Swiercz, R.1    Cheng, D.2    Kim, D.3    Bedford, M.T.4
  • 135
    • 14244255860 scopus 로고    scopus 로고
    • Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3
    • Swiercz, R., M. D. Person, and M. T. Bedford. 2005. Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Biochem. J. 386:85-91.
    • (2005) Biochem. J , vol.386 , pp. 85-91
    • Swiercz, R.1    Person, M.D.2    Bedford, M.T.3
  • 136
    • 79952578531 scopus 로고    scopus 로고
    • The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity
    • Takahashi, Y., et al. 2011. The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity. J. Recept. Signal Transduct. Res. 31:168-172.
    • (2011) J. Recept. Signal Transduct. Res , vol.31 , pp. 168-172
    • Takahashi, Y.1
  • 137
    • 0034677814 scopus 로고    scopus 로고
    • PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells
    • Tang, J., et al. 2000. PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. J. Biol. Chem. 275:7723-7730.
    • (2000) J. Biol. Chem , vol.275 , pp. 7723-7730
    • Tang, J.1
  • 138
    • 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., J. D. Gary, S. Clarke, and H. R. Herschman. 1998. 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. 273:16935-16945.
    • (1998) J. Biol. Chem , vol.273 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 139
    • 67650403817 scopus 로고    scopus 로고
    • Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum
    • Trelle, M. B., A. M. Salcedo-Amaya, A. M. Cohen, H. G. Stunnenberg, and O. N. Jensen. 2009. Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum. J. Proteome Res. 8:3439-3450.
    • (2009) J. Proteome Res , vol.8 , pp. 3439-3450
    • Trelle, M.B.1    Salcedo-Amaya, A.M.2    Cohen, A.M.3    Stunnenberg, H.G.4    Jensen, O.N.5
  • 140
    • 4143111261 scopus 로고    scopus 로고
    • Histone methyltransferases in Aspergillus nidulans: Evidence for a novel enzyme with a unique substrate specificity
    • Trojer, P., et al. 2004. Histone methyltransferases in Aspergillus nidulans: evidence for a novel enzyme with a unique substrate specificity. Biochemistry 43:10834-10843.
    • (2004) Biochemistry , vol.43 , pp. 10834-10843
    • Trojer, P.1
  • 141
    • 74849115776 scopus 로고    scopus 로고
    • Arginine methylation as a molecular signature of the Piwi small RNA pathway
    • Vagin, V. V., G. J. Hannon, and A. A. Aravin. 2009. Arginine methylation as a molecular signature of the Piwi small RNA pathway. Cell Cycle 8:4003-4004.
    • (2009) Cell Cycle , vol.8 , pp. 4003-4004
    • Vagin, V.V.1    Hannon, G.J.2    Aravin, A.A.3
  • 142
    • 68149164399 scopus 로고    scopus 로고
    • Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members
    • Vagin, V. V., et al. 2009. Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members. Genes Dev. 23:1749-1762.
    • (2009) Genes Dev , vol.23 , pp. 1749-1762
    • Vagin, V.V.1
  • 143
    • 60649099160 scopus 로고    scopus 로고
    • Accurate localization and relative quantification of arginine methylation using Nanoflow liquid chromatography coupled to electron transfer dissociation and Orbitrap mass spectrometry
    • Wang, H., et al. 2009. Accurate localization and relative quantification of arginine methylation using Nanoflow liquid chromatography coupled to electron transfer dissociation and Orbitrap mass spectrometry. J. Am. Soc. Mass Spectrom. 20:507-519.
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , pp. 507-519
    • Wang, H.1
  • 144
    • 5044228483 scopus 로고    scopus 로고
    • Human PAD4 regulates histone arginine methylation levels via demethylimination
    • Wang, Y., et al. 2004. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 306:279-283.
    • (2004) Science , vol.306 , pp. 279-283
    • Wang, Y.1
  • 145
    • 67650072604 scopus 로고    scopus 로고
    • Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
    • Webby, C. J., et al. 2009. Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 325:90-93.
    • (2009) Science , vol.325 , pp. 90-93
    • Webby, C.J.1
  • 146
    • 0037148758 scopus 로고    scopus 로고
    • The genome sequence of Schizosaccharomyces pombe
    • Wood, V., et al. 2002. The genome sequence of Schizosaccharomyces pombe. Nature 415:871-880.
    • (2002) Nature , vol.415 , pp. 871-880
    • Wood, V.1
  • 147
    • 2542485409 scopus 로고    scopus 로고
    • Organellar proteomics reveals Golgi arginine dimethylation
    • Wu, C. C., et al. 2004. Organellar proteomics reveals Golgi arginine dimethylation. Mol. Biol. Cell 15:2907-2919.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2907-2919
    • Wu, C.C.1
  • 148
    • 32844468049 scopus 로고    scopus 로고
    • Histone arginine methylation and its dynamic regulation
    • Wysocka, J., C. D. Allis, and S. Coonrod. 2006. Histone arginine methylation and its dynamic regulation. Front. Biosci. 11:344-355.
    • (2006) Front. Biosci , vol.11 , pp. 344-355
    • Wysocka, J.1    Allis, C.D.2    Coonrod, S.3
  • 149
    • 0038313055 scopus 로고    scopus 로고
    • Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
    • Yadav, N., et al. 2003. Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 100:6464-6468.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 6464-6468
    • Yadav, N.1
  • 150
    • 33744908297 scopus 로고    scopus 로고
    • The arginine methyltransferase PRMT2 binds RB and regulates E2F function
    • Yoshimoto, T., et al. 2006. The arginine methyltransferase PRMT2 binds RB and regulates E2F function. Exp. Cell Res. 312:2040-2053.
    • (2006) Exp. Cell Res , vol.312 , pp. 2040-2053
    • Yoshimoto, T.1
  • 151
    • 40349113414 scopus 로고    scopus 로고
    • Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity
    • Zhao, X., et al. 2008. Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity. Genes Dev. 22:640-653.
    • (2008) Genes Dev , vol.22 , pp. 640-653
    • Zhao, X.1
  • 152
    • 77956341763 scopus 로고    scopus 로고
    • PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130
    • Zhou, Z., et al. 2010. PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130. Cell Res. 20:1023-1033.
    • (2010) Cell Res , vol.20 , pp. 1023-1033
    • Zhou, Z.1


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