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Volumn 1839, Issue 8, 2014, Pages 702-710

Readers of histone methylarginine marks

Author keywords

Arginine methylation; CARM1; Histone code; PRMT1; Tudor domain

Indexed keywords

ARGININE; HISTONE; LONG UNTRANSLATED RNA; METHYLARGININE; SMALL NUCLEAR RNA; UNCLASSIFIED DRUG;

EID: 84904048466     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2014.02.015     Document Type: Review
Times cited : (126)

References (130)
  • 1
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford M.T., Clarke S.G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 2009, 33:1-13.
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 2
    • 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., Richard S. Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J. Biol. Chem. 2000, 275:16030-16036.
    • (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
  • 3
    • 33749535702 scopus 로고    scopus 로고
    • Arginine methylation in a beta-hairpin peptide: implications for Arg-pi interactions, DeltaCp(o), and the cold denatured state
    • Hughes R.M., Waters M.L. Arginine methylation in a beta-hairpin peptide: implications for Arg-pi interactions, DeltaCp(o), and the cold denatured state. J. Am. Chem. Soc. 2006, 128:12735-12742.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12735-12742
    • Hughes, R.M.1    Waters, M.L.2
  • 5
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang B., Chen Y., Zhao Y., Bruick R.K. JMJD6 is a histone arginine demethylase. Science 2007, 318:444-447.
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 6
    • 84894579192 scopus 로고    scopus 로고
    • Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release
    • Liu W., Ma Q., Wong K., Li W., Ohgi K., Zhang J., Aggarwal A.K., Rosenfeld M.G. Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release. Cell 2013, 155:1581-1595.
    • (2013) Cell , vol.155 , pp. 1581-1595
    • Liu, W.1    Ma, Q.2    Wong, K.3    Li, W.4    Ohgi, K.5    Zhang, J.6    Aggarwal, A.K.7    Rosenfeld, M.G.8
  • 11
    • 35348916034 scopus 로고    scopus 로고
    • Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains
    • Troffer-Charlier N., Cura V., Hassenboehler P., Moras D., Cavarelli J. Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains. EMBO J. 2007, 26:4391-4401.
    • (2007) EMBO J. , vol.26 , pp. 4391-4401
    • Troffer-Charlier, N.1    Cura, V.2    Hassenboehler, P.3    Moras, D.4    Cavarelli, J.5
  • 12
    • 35348861410 scopus 로고    scopus 로고
    • Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase
    • Yue W.W., Hassler M., Roe S.M., Thompson-Vale V., Pearl L.H. Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase. EMBO J. 2007, 26:4402-4412.
    • (2007) EMBO J. , vol.26 , pp. 4402-4412
    • Yue, W.W.1    Hassler, M.2    Roe, S.M.3    Thompson-Vale, V.4    Pearl, L.H.5
  • 13
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • Zhang X., Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 2003, 11:509-520.
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 14
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang X., Zhou L., Cheng X. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J. 2000, 19:3509-3519.
    • (2000) EMBO J. , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 15
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary J.D., Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 1998, 61:65-131.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 16
    • 0015376995 scopus 로고
    • Epsilon-N-methylated lysine and guanidine-N-methylated arginine of proteins. 3. Presence and distribution in nature and mammals
    • Matsuoka M. Epsilon-N-methylated lysine and guanidine-N-methylated arginine of proteins. 3. Presence and distribution in nature and mammals. Seikagaku 1972, 44:364-370.
    • (1972) Seikagaku , vol.44 , pp. 364-370
    • Matsuoka, M.1
  • 18
    • 84881113123 scopus 로고    scopus 로고
    • Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome
    • Bremang M., Cuomo A., Agresta A.M., Stugiewicz M., Spadotto V., Bonaldi T. Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome. Mol. Biosyst. 2013, 9:2231-2247.
    • (2013) Mol. Biosyst. , vol.9 , pp. 2231-2247
    • Bremang, M.1    Cuomo, A.2    Agresta, A.M.3    Stugiewicz, M.4    Spadotto, V.5    Bonaldi, T.6
  • 21
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • Di Lorenzo A., Bedford M.T. Histone arginine methylation. FEBS Lett. 2011, 585:2024-2031.
    • (2011) FEBS Lett. , vol.585 , pp. 2024-2031
    • Di Lorenzo, A.1    Bedford, M.T.2
  • 23
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T. Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science 1990, 250:979-982.
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4    Moran, M.F.5    Pawson, T.6
  • 24
    • 77953292595 scopus 로고    scopus 로고
    • Post-translational modifications in signal integration
    • Deribe Y.L., Pawson T., Dikic I. Post-translational modifications in signal integration. Nat. Struct. Mol. Biol. 2010, 17:666-672.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 666-672
    • Deribe, Y.L.1    Pawson, T.2    Dikic, I.3
  • 25
    • 0031081575 scopus 로고    scopus 로고
    • Tudor domains in proteins that interact with RNA
    • Ponting C.P. Tudor domains in proteins that interact with RNA. Trends Biochem. Sci. 1997, 22:51-52.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 51-52
    • Ponting, C.P.1
  • 26
    • 0031027360 scopus 로고    scopus 로고
    • The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the Tudor protein involved in Drosophila melanogaster development
    • Callebaut I., Mornon J.P. The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the Tudor protein involved in Drosophila melanogaster development. Biochem. J. 1997, 321(Pt 1):125-132.
    • (1997) Biochem. J. , vol.321 , Issue.PART 1 , pp. 125-132
    • Callebaut, I.1    Mornon, J.P.2
  • 27
    • 0022400587 scopus 로고
    • Tudor, a gene required for assembly of the germ plasm in Drosophila melanogaster
    • Boswell R.E., Mahowald A.P. Tudor, a gene required for assembly of the germ plasm in Drosophila melanogaster. Cell 1985, 43:97-104.
    • (1985) Cell , vol.43 , pp. 97-104
    • Boswell, R.E.1    Mahowald, A.P.2
  • 29
    • 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., Dreyfuss G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell 2001, 7:1111-1117.
    • (2001) Mol. Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 31
    • 80051554264 scopus 로고    scopus 로고
    • Spinal muscular atrophy: a timely review
    • Kolb S.J., Kissel J.T. Spinal muscular atrophy: a timely review. Arch. Neurol. 2011, 68:979-984.
    • (2011) Arch. Neurol. , vol.68 , pp. 979-984
    • Kolb, S.J.1    Kissel, J.T.2
  • 32
    • 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., Meheus L., de Brabandere V., Fischer U., Luhrmann R. 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 2001, 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
  • 34
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001, 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 35
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan M.V., Lee J., Ward I.M., Kim J.E., Thompson J.R., Chen J., Mer G. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 2006, 127:1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 39
    • 77956271553 scopus 로고    scopus 로고
    • Structural basis for methylarginine-dependent recognition of Aubergine by Tudor
    • Liu H., Wang J.Y., Huang Y., Li Z., Gong W., Lehmann R., Xu R.M. Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. Genes Dev. 2010, 24:1876-1881.
    • (2010) Genes Dev. , vol.24 , pp. 1876-1881
    • Liu, H.1    Wang, J.Y.2    Huang, Y.3    Li, Z.4    Gong, W.5    Lehmann, R.6    Xu, R.M.7
  • 45
    • 3242669648 scopus 로고    scopus 로고
    • Detection of novel mutations in the SMN Tudor domain in type I SMA patients
    • Cusco I., Barcelo M.J., del Rio E., Baiget M., Tizzano E.F. Detection of novel mutations in the SMN Tudor domain in type I SMA patients. Neurology 2004, 63:146-149.
    • (2004) Neurology , vol.63 , pp. 146-149
    • Cusco, I.1    Barcelo, M.J.2    del Rio, E.3    Baiget, M.4    Tizzano, E.F.5
  • 46
    • 33846001366 scopus 로고    scopus 로고
    • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
    • Cheng D., Cote J., Shaaban S., Bedford M.T. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol. Cell 2007, 25:71-83.
    • (2007) Mol. Cell , vol.25 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 47
    • 38849088603 scopus 로고    scopus 로고
    • KH-type splicing regulatory protein interacts with survival motor neuron protein and is misregulated in spinal muscular atrophy
    • Tadesse H., Deschenes-Furry J., Boisvenue S., Cote J. KH-type splicing regulatory protein interacts with survival motor neuron protein and is misregulated in spinal muscular atrophy. Hum. Mol. Genet. 2008, 17:506-524.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 506-524
    • Tadesse, H.1    Deschenes-Furry, J.2    Boisvenue, S.3    Cote, J.4
  • 48
    • 84883385816 scopus 로고    scopus 로고
    • The Tudor protein survival motor neuron (SMN) is a chromatin-binding protein that interacts with methylated lysine 79 of histone H3
    • Sabra M., Texier P., El Maalouf J., Lomonte P. The Tudor protein survival motor neuron (SMN) is a chromatin-binding protein that interacts with methylated lysine 79 of histone H3. J. Cell Sci. 2013, 126:3664-3677.
    • (2013) J. Cell Sci. , vol.126 , pp. 3664-3677
    • Sabra, M.1    Texier, P.2    El Maalouf, J.3    Lomonte, P.4
  • 49
    • 0031759799 scopus 로고    scopus 로고
    • Characterization of a gene encoding survival motor neuron (SMN)-related protein, a constituent of the spliceosome complex
    • Talbot K., Miguel-Aliaga I., Mohaghegh P., Ponting C.P., Davies K.E. Characterization of a gene encoding survival motor neuron (SMN)-related protein, a constituent of the spliceosome complex. Hum. Mol. Genet. 1998, 7:2149-2156.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 2149-2156
    • Talbot, K.1    Miguel-Aliaga, I.2    Mohaghegh, P.3    Ponting, C.P.4    Davies, K.E.5
  • 51
    • 0035903086 scopus 로고    scopus 로고
    • SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome
    • Rappsilber J., Ajuh P., Lamond A.I., Mann M. SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. J. Biol. Chem. 2001, 276:31142-31150.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31142-31150
    • Rappsilber, J.1    Ajuh, P.2    Lamond, A.I.3    Mann, M.4
  • 53
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Cote J., Richard S. Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 2005, 280:28476-28483.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 55
    • 84871712509 scopus 로고    scopus 로고
    • Protein arginine methyltransferases and cancer
    • Yang Y., Bedford M.T. Protein arginine methyltransferases and cancer. Nat. Rev. Cancer 2013, 13:37-50.
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 37-50
    • Yang, Y.1    Bedford, M.T.2
  • 56
    • 78650233514 scopus 로고    scopus 로고
    • TDRD3 is an effector molecule for arginine-methylated histone marks
    • Yang Y., Lu Y., Espejo A., Wu J., Xu W., Liang S., Bedford M.T. TDRD3 is an effector molecule for arginine-methylated histone marks. Mol. Cell 2010, 40:1016-1023.
    • (2010) Mol. Cell , vol.40 , pp. 1016-1023
    • Yang, Y.1    Lu, Y.2    Espejo, A.3    Wu, J.4    Xu, W.5    Liang, S.6    Bedford, M.T.7
  • 58
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: a molecular perspective
    • Wang J.C. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell Biol. 2002, 3:430-440.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 59
    • 0037062474 scopus 로고    scopus 로고
    • Preferential cleavage of plasmid-based R-loops and D-loops by Drosophila topoisomerase IIIbeta
    • Wilson-Sali T., Hsieh T.S. Preferential cleavage of plasmid-based R-loops and D-loops by Drosophila topoisomerase IIIbeta. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:7974-7979.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7974-7979
    • Wilson-Sali, T.1    Hsieh, T.S.2
  • 60
    • 84893466770 scopus 로고    scopus 로고
    • Arginine methylation facilitates the recruitment of TOP3B to chromatin to prevent R loop accumulation
    • Yang Y., McBride K.M., Hensley S., Lu Y., Chedin F., Bedford M.T. Arginine methylation facilitates the recruitment of TOP3B to chromatin to prevent R loop accumulation. Mol. Cell. 2014, 53:484-497.
    • (2014) Mol. Cell. , vol.53 , pp. 484-497
    • Yang, Y.1    McBride, K.M.2    Hensley, S.3    Lu, Y.4    Chedin, F.5    Bedford, M.T.6
  • 64
    • 0029131021 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE
    • Tong X., Drapkin R., Yalamanchili R., Mosialos G., Kieff E. The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol. Cell. Biol. 1995, 15:4735-4744.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4735-4744
    • Tong, X.1    Drapkin, R.2    Yalamanchili, R.3    Mosialos, G.4    Kieff, E.5
  • 67
    • 17644374227 scopus 로고    scopus 로고
    • The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6
    • Valineva T., Yang J., Palovuori R., Silvennoinen O. The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6. J. Biol. Chem. 2005, 280:14989-14996.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14989-14996
    • Valineva, T.1    Yang, J.2    Palovuori, R.3    Silvennoinen, O.4
  • 69
    • 79958013243 scopus 로고    scopus 로고
    • Histone H4 acetylation differentially modulates arginine methylation by an in Cis mechanism
    • Feng Y., Wang J., Asher S., Hoang L., Guardiani C., Ivanov I., Zheng Y.G. Histone H4 acetylation differentially modulates arginine methylation by an in Cis mechanism. J. Biol. Chem. 2011, 286:20323-20334.
    • (2011) J. Biol. Chem. , vol.286 , pp. 20323-20334
    • Feng, Y.1    Wang, J.2    Asher, S.3    Hoang, L.4    Guardiani, C.5    Ivanov, I.6    Zheng, Y.G.7
  • 70
    • 46349107531 scopus 로고    scopus 로고
    • Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing
    • Li C.L., Yang W.Z., Chen Y.P., Yuan H.S. Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing. Nucleic Acids Res. 2008, 36:3579-3589.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3579-3589
    • Li, C.L.1    Yang, W.Z.2    Chen, Y.P.3    Yuan, H.S.4
  • 72
    • 84861561394 scopus 로고    scopus 로고
    • Tudor staphylococcal nuclease (Tudor-SN) participates in small ribonucleoprotein (snRNP) assembly via interacting with symmetrically dimethylated Sm proteins
    • Gao X., Zhao X., Zhu Y., He J., Shao J., Su C., Zhang Y., Zhang W., Saarikettu J., Silvennoinen O., Yao Z., Yang J. Tudor staphylococcal nuclease (Tudor-SN) participates in small ribonucleoprotein (snRNP) assembly via interacting with symmetrically dimethylated Sm proteins. J. Biol. Chem. 2012, 287:18130-18141.
    • (2012) J. Biol. Chem. , vol.287 , pp. 18130-18141
    • Gao, X.1    Zhao, X.2    Zhu, Y.3    He, J.4    Shao, J.5    Su, C.6    Zhang, Y.7    Zhang, W.8    Saarikettu, J.9    Silvennoinen, O.10    Yao, Z.11    Yang, J.12
  • 73
    • 34547829272 scopus 로고    scopus 로고
    • Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome
    • Yang J., Valineva T., Hong J., Bu T., Yao Z., Jensen O.N., Frilander M.J., Silvennoinen O. Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome. Nucleic Acids Res. 2007, 35:4485-4494.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4485-4494
    • Yang, J.1    Valineva, T.2    Hong, J.3    Bu, T.4    Yao, Z.5    Jensen, O.N.6    Frilander, M.J.7    Silvennoinen, O.8
  • 75
    • 79957591404 scopus 로고    scopus 로고
    • Identification of staphylococcal nuclease domain-containing 1 (SND1) as a Metadherin-interacting protein with metastasis-promoting functions
    • Blanco M.A., Aleckovic M., Hua Y., Li T., Wei Y., Xu Z., Cristea I.M., Kang Y. Identification of staphylococcal nuclease domain-containing 1 (SND1) as a Metadherin-interacting protein with metastasis-promoting functions. J. Biol. Chem. 2011, 286:19982-19992.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19982-19992
    • Blanco, M.A.1    Aleckovic, M.2    Hua, Y.3    Li, T.4    Wei, Y.5    Xu, Z.6    Cristea, I.M.7    Kang, Y.8
  • 76
    • 35148895851 scopus 로고    scopus 로고
    • SND1, a component of RNA-induced silencing complex, is up-regulated in human colon cancers and implicated in early stage colon carcinogenesis
    • Tsuchiya N., Ochiai M., Nakashima K., Ubagai T., Sugimura T., Nakagama H. SND1, a component of RNA-induced silencing complex, is up-regulated in human colon cancers and implicated in early stage colon carcinogenesis. Cancer Res. 2007, 67:9568-9576.
    • (2007) Cancer Res. , vol.67 , pp. 9568-9576
    • Tsuchiya, N.1    Ochiai, M.2    Nakashima, K.3    Ubagai, T.4    Sugimura, T.5    Nakagama, H.6
  • 77
    • 67349141725 scopus 로고    scopus 로고
    • Loss of the Mili-interacting Tudor domain-containing protein-1 activates transposons and alters the Mili-associated small RNA profile
    • Reuter M., Chuma S., Tanaka T., Franz T., Stark A., Pillai R.S. Loss of the Mili-interacting Tudor domain-containing protein-1 activates transposons and alters the Mili-associated small RNA profile. Nat. Struct. Mol. Biol. 2009, 16:639-646.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 639-646
    • Reuter, M.1    Chuma, S.2    Tanaka, T.3    Franz, T.4    Stark, A.5    Pillai, R.S.6
  • 81
    • 84892599690 scopus 로고    scopus 로고
    • PIWI proteins and PIWI-interacting RNAs in the soma
    • Ross R.J., Weiner M.M., Lin H. PIWI proteins and PIWI-interacting RNAs in the soma. Nature 2014, 505:353-359.
    • (2014) Nature , vol.505 , pp. 353-359
    • Ross, R.J.1    Weiner, M.M.2    Lin, H.3
  • 82
    • 0034603692 scopus 로고    scopus 로고
    • Complex RNA processing of TDRKH, a novel gene encoding the putative RNA-binding Tudor and KH domains
    • Lamb F.S., Barna T.J., Goud C., Marenholz I., Mischke D., Schutte B.C. Complex RNA processing of TDRKH, a novel gene encoding the putative RNA-binding Tudor and KH domains. Gene 2000, 246:209-218.
    • (2000) Gene , vol.246 , pp. 209-218
    • Lamb, F.S.1    Barna, T.J.2    Goud, C.3    Marenholz, I.4    Mischke, D.5    Schutte, B.C.6
  • 83
    • 84880220867 scopus 로고    scopus 로고
    • TDRKH is essential for spermatogenesis and participates in primary piRNA biogenesis in the germline
    • Saxe J.P., Chen M., Zhao H., Lin H. TDRKH is essential for spermatogenesis and participates in primary piRNA biogenesis in the germline. EMBO J. 2013, 32:1869-1885.
    • (2013) EMBO J. , vol.32 , pp. 1869-1885
    • Saxe, J.P.1    Chen, M.2    Zhao, H.3    Lin, H.4
  • 85
    • 65049090424 scopus 로고    scopus 로고
    • TDRD6 is required for spermiogenesis, chromatoid body architecture, and regulation of miRNA expression
    • Vasileva A., Tiedau D., Firooznia A., Muller-Reichert T., Jessberger R. TDRD6 is required for spermiogenesis, chromatoid body architecture, and regulation of miRNA expression. Curr. Biol. 2009, 19:630-639.
    • (2009) Curr. Biol. , vol.19 , pp. 630-639
    • Vasileva, A.1    Tiedau, D.2    Firooznia, A.3    Muller-Reichert, T.4    Jessberger, R.5
  • 89
    • 69249149620 scopus 로고    scopus 로고
    • Thrombospondin-1 is a transcriptional repression target of PRMT6
    • Michaud-Levesque J., Richard S. Thrombospondin-1 is a transcriptional repression target of PRMT6. J. Biol. Chem. 2009, 284:21338-21346.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21338-21346
    • Michaud-Levesque, J.1    Richard, S.2
  • 90
    • 84862612318 scopus 로고    scopus 로고
    • Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription
    • Qiu Y., Liu L., Zhao C., Han C., Li F., Zhang J., Wang Y., Li G., Mei Y., Wu M., Wu J., Shi Y. Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription. Genes Dev. 2012, 26:1376-1391.
    • (2012) Genes Dev. , vol.26 , pp. 1376-1391
    • Qiu, Y.1    Liu, L.2    Zhao, C.3    Han, C.4    Li, F.5    Zhang, J.6    Wang, Y.7    Li, G.8    Mei, Y.9    Wu, M.10    Wu, J.11    Shi, Y.12
  • 97
    • 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., 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. 2004, 24:9630-9645.
    • (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
  • 98
    • 43049084803 scopus 로고    scopus 로고
    • The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5
    • Lacroix M., Messaoudi S.E., Rodier G., Le Cam A., Sardet C., Fabbrizio E. The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 2008, 9:452-458.
    • (2008) EMBO Rep. , vol.9 , pp. 452-458
    • Lacroix, M.1    Messaoudi, S.E.2    Rodier, G.3    Le Cam, A.4    Sardet, C.5    Fabbrizio, E.6
  • 101
    • 70449099301 scopus 로고    scopus 로고
    • Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain
    • Otani J., Nankumo T., Arita K., Inamoto S., Ariyoshi M., Shirakawa M. Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain. EMBO Rep. 2009, 10:1235-1241.
    • (2009) EMBO Rep. , vol.10 , pp. 1235-1241
    • Otani, J.1    Nankumo, T.2    Arita, K.3    Inamoto, S.4    Ariyoshi, M.5    Shirakawa, M.6
  • 103
    • 84871568905 scopus 로고    scopus 로고
    • Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4
    • Dhar S.S., Lee S.H., Kan P.Y., Voigt P., Ma L., Shi X., Reinberg D., Lee M.G. Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4. Gene Dev. 2012, 26:2749-2762.
    • (2012) Gene Dev. , vol.26 , pp. 2749-2762
    • Dhar, S.S.1    Lee, S.H.2    Kan, P.Y.3    Voigt, P.4    Ma, L.5    Shi, X.6    Reinberg, D.7    Lee, M.G.8
  • 104
    • 84859585596 scopus 로고    scopus 로고
    • Histone H3R17me2a mark recruits human RNA polymerase-associated factor 1 complex to activate transcription
    • Wu J., Xu W. Histone H3R17me2a mark recruits human RNA polymerase-associated factor 1 complex to activate transcription. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:5675-5680.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5675-5680
    • Wu, J.1    Xu, W.2
  • 105
    • 84862496145 scopus 로고    scopus 로고
    • A role for CARM1-mediated histone H3 arginine methylation in protecting histone acetylation by releasing corepressors from chromatin
    • Wu J., Cui N., Wang R., Li J., Wong J. A role for CARM1-mediated histone H3 arginine methylation in protecting histone acetylation by releasing corepressors from chromatin. PLoS One 2012, 7:e34692.
    • (2012) PLoS One , vol.7
    • Wu, J.1    Cui, N.2    Wang, R.3    Li, J.4    Wong, J.5
  • 106
    • 78651515331 scopus 로고    scopus 로고
    • Regulated recruitment of tumor suppressor BRCA1 to the p21 gene by coactivator methylation
    • Lee Y.H., Bedford M.T., Stallcup M.R. Regulated recruitment of tumor suppressor BRCA1 to the p21 gene by coactivator methylation. Genes Dev. 2011, 25:176-188.
    • (2011) Genes Dev. , vol.25 , pp. 176-188
    • Lee, Y.H.1    Bedford, M.T.2    Stallcup, M.R.3
  • 107
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke I.A., Lowery D.M., Nguyen A., Yaffe M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 2003, 302:636-639.
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 108
    • 84879987789 scopus 로고    scopus 로고
    • LincRNAs: genomics, evolution, and mechanisms
    • Ulitsky I., Bartel D.P. lincRNAs: genomics, evolution, and mechanisms. Cell 2013, 154:26-46.
    • (2013) Cell , vol.154 , pp. 26-46
    • Ulitsky, I.1    Bartel, D.P.2
  • 109
    • 33645231102 scopus 로고    scopus 로고
    • Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin
    • Bernstein E., Duncan E.M., Masui O., Gil J., Heard E., Allis C.D. Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin. Mol. Cell. Biol. 2006, 26:2560-2569.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2560-2569
    • Bernstein, E.1    Duncan, E.M.2    Masui, O.3    Gil, J.4    Heard, E.5    Allis, C.D.6
  • 110
    • 81055140863 scopus 로고    scopus 로고
    • NcRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs
    • Yang L., Lin C., Liu W., Zhang J., Ohgi K.A., Grinstein J.D., Dorrestein P.C., Rosenfeld M.G. ncRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs. Cell 2011, 147:773-788.
    • (2011) Cell , vol.147 , pp. 773-788
    • Yang, L.1    Lin, C.2    Liu, W.3    Zhang, J.4    Ohgi, K.A.5    Grinstein, J.D.6    Dorrestein, P.C.7    Rosenfeld, M.G.8
  • 111
    • 77953121401 scopus 로고    scopus 로고
    • PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity
    • Nair S.S., Nair B.C., Cortez V., Chakravarty D., Metzger E., Schule R., Brann D.W., Tekmal R.R., Vadlamudi R.K. PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity. EMBO Rep. 2010, 11:438-444.
    • (2010) EMBO Rep. , vol.11 , pp. 438-444
    • Nair, S.S.1    Nair, B.C.2    Cortez, V.3    Chakravarty, D.4    Metzger, E.5    Schule, R.6    Brann, D.W.7    Tekmal, R.R.8    Vadlamudi, R.K.9
  • 112
    • 84880317205 scopus 로고    scopus 로고
    • PELP1 oncogenic functions involve CARM1 regulation
    • Mann M., Cortez V., Vadlamudi R. PELP1 oncogenic functions involve CARM1 regulation. Carcinogenesis 2013, 34:1468-1475.
    • (2013) Carcinogenesis , vol.34 , pp. 1468-1475
    • Mann, M.1    Cortez, V.2    Vadlamudi, R.3
  • 117
    • 78149244916 scopus 로고    scopus 로고
    • Identification of non-peptide malignant brain tumor (MBT) repeat antagonists by virtual screening of commercially available compounds
    • Kireev D., Wigle T.J., Norris-Drouin J., Herold J.M., Janzen W.P., Frye S.V. Identification of non-peptide malignant brain tumor (MBT) repeat antagonists by virtual screening of commercially available compounds. J. Med. Chem. 2010, 53:7625-7631.
    • (2010) J. Med. Chem. , vol.53 , pp. 7625-7631
    • Kireev, D.1    Wigle, T.J.2    Norris-Drouin, J.3    Herold, J.M.4    Janzen, W.P.5    Frye, S.V.6
  • 119
    • 84874619010 scopus 로고    scopus 로고
    • Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding
    • Le D.D., Cortesi A.T., Myers S.A., Burlingame A.L., Fujimori D.G. Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding. J. Am. Chem. Soc. 2013, 135:2879-2882.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2879-2882
    • Le, D.D.1    Cortesi, A.T.2    Myers, S.A.3    Burlingame, A.L.4    Fujimori, D.G.5
  • 121
    • 77955587632 scopus 로고    scopus 로고
    • Beta-catenin primes organizer gene expression by recruiting a histone H3 arginine 8 methyltransferase, Prmt2
    • Blythe S.A., Cha S.W., Tadjuidje E., Heasman J., Klein P.S. Beta-catenin primes organizer gene expression by recruiting a histone H3 arginine 8 methyltransferase, Prmt2. Dev Cell 2010, 19:220-231.
    • (2010) Dev Cell , vol.19 , pp. 220-231
    • Blythe, S.A.1    Cha, S.W.2    Tadjuidje, E.3    Heasman, J.4    Klein, P.S.5
  • 122
    • 84865526587 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1
    • Karkhanis V., Wang L., Tae S., Hu Y.J., Imbalzano A.N., Sif S. Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1. J. Biol. Chem. 2012, 287:29801-29814.
    • (2012) J. Biol. Chem. , vol.287 , pp. 29801-29814
    • Karkhanis, V.1    Wang, L.2    Tae, S.3    Hu, Y.J.4    Imbalzano, A.N.5    Sif, S.6
  • 128
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • Zhang L., Eugeni E.E., Parthun M.R., Freitas M.A. Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 2003, 112:77-86.
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4


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