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Volumn 17, Issue 1, 2012, Pages 71-84

Fluorescence-Based Methods for Screening Writers and Readers of Histone Methyl Marks

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSYLHOMOCYSTEINASE; EED PROTEIN, HUMAN; EHMT1 PROTEIN, HUMAN; EHMT2 PROTEIN, HUMAN; ENZYME INHIBITOR; HISTOCOMPATIBILITY ANTIGEN; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; PEPTIDE; PRMT3 PROTEIN, HUMAN; PROTEIN ARGININE METHYLTRANSFERASE; REPRESSOR PROTEIN; SETD7 PROTEIN, HUMAN; SETD8 PROTEIN, HUMAN; SUV39H2 PROTEIN, HUMAN; WDR5 PROTEIN, HUMAN;

EID: 84861808843     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057111422256     Document Type: Article
Times cited : (41)

References (74)
  • 1
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin Modifications and Their Function
    • Kouzarides T. Chromatin Modifications and Their Function. Cell 2007, 128(4), 693–705.
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 4
    • 79251590753 scopus 로고    scopus 로고
    • Specificity Analysis-Based Identification of New Methylation Targets of the SET7/9 Protein Lysine Methyltransferase
    • Dhayalan A. Kudithipudi S. Rathert P. Jeltsch A. Specificity Analysis-Based Identification of New Methylation Targets of the SET7/9 Protein Lysine Methyltransferase. Chem. Biol. 2011, 18(1), 111–120.
    • (2011) Chem. Biol. , vol.18 , Issue.1 , pp. 111-120
    • Dhayalan, A.1    Kudithipudi, S.2    Rathert, P.3    Jeltsch, A.4
  • 8
    • 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. Miranda T. B. Jiang W. Frankel A. Roemer M. E. Robb V. A. Gutmann D. H. Herschman H. R. Clarke S. Newsham I. F. 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 2004, 23(47), 7761–7771.
    • (2004) Oncogene , vol.23 , Issue.47 , pp. 7761-7771
    • Singh, V.1    Miranda, T.B.2    Jiang, W.3    Frankel, A.4    Roemer, M.E.5    Robb, V.A.6    Gutmann, D.H.7    Herschman, H.R.8    Clarke, S.9    Newsham, I.F.10
  • 10
    • 20844450998 scopus 로고    scopus 로고
    • Arginine Methylation an Emerging Regulator of Protein Function
    • Bedford M. T. Richard S. Arginine Methylation an Emerging Regulator of Protein Function. Mol. Cell 2005, 18(3), 263–72.
    • (2005) Mol. Cell , vol.18 , Issue.3 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 11
    • 0032479171 scopus 로고    scopus 로고
    • PRMT 3, a Type I Protein Arginine N-Methyltransferase That Differs from PRMT1 in Its Oligomerization, Subcellular Localization, Substrate Specificity, and Regulation
    • Tang J. Gary J. D. Clarke S. Herschman H. R. PRMT 3, a Type I Protein Arginine N-Methyltransferase That Differs from PRMT1 in Its Oligomerization, Subcellular Localization, Substrate Specificity, and Regulation. J. Biol. Chem. 1998, 273(27), 16935–16945.
    • (1998) J. Biol. Chem. , vol.273 , Issue.27 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 12
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 Is a Ribosomal Protein Methyltransferase That Affects the Cellular Levels of Ribosomal Subunits
    • Bachand F. Silver P. A. PRMT3 Is a Ribosomal Protein Methyltransferase That Affects the Cellular Levels of Ribosomal Subunits. Embo. J. 2004, 23(13), 2641–2650.
    • (2004) Embo. J. , vol.23 , Issue.13 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 13
    • 77956176969 scopus 로고    scopus 로고
    • PRMT3 Is Essential for Dendritic Spine Maturation in Rat Hippocampal Neurons
    • Miyata S. Mori Y. Tohyama M. PRMT3 Is Essential for Dendritic Spine Maturation in Rat Hippocampal Neurons. Brain Res. 2010, 1352, 11–20.
    • (2010) Brain Res. , vol.1352 , pp. 11-20
    • Miyata, S.1    Mori, Y.2    Tohyama, M.3
  • 14
    • 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(5849), 444–447.
    • (2007) Science , vol.318 , Issue.5849 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 15
    • 34848885467 scopus 로고    scopus 로고
    • Interplay between Chromatin Remodelers and Protein Arginine Methyltransferases
    • Pal S. Sif S. Interplay between Chromatin Remodelers and Protein Arginine Methyltransferases. J. Cell Physiol. 2007, 213(2), 306–315.
    • (2007) J. Cell Physiol. , vol.213 , Issue.2 , pp. 306-315
    • Pal, S.1    Sif, S.2
  • 16
    • 78149423004 scopus 로고    scopus 로고
    • Regulation of the Histone H4 Monomethylase PR-Set7 by CRL4(Cdt2)-Mediated PCNA-Dependent Degradation during DNA Damage
    • Oda H. Hubner M. R. Beck D. B. Vermeulen M. Hurwitz J. Spector D. L. Reinberg D. Regulation of the Histone H4 Monomethylase PR-Set7 by CRL4(Cdt2)-Mediated PCNA-Dependent Degradation during DNA Damage. Mol. Cell 2010, 40(3), 364–376.
    • (2010) Mol. Cell , vol.40 , Issue.3 , pp. 364-376
    • Oda, H.1    Hubner, M.R.2    Beck, D.B.3    Vermeulen, M.4    Hurwitz, J.5    Spector, D.L.6    Reinberg, D.7
  • 17
    • 64749106929 scopus 로고    scopus 로고
    • Monomethylation of Histone H4-Lysine 20 Is Involved in Chromosome Structure and Stability and Is Essential for Mouse Development
    • Oda H. Okamoto I. Murphy N. Chu J. Price S. M. Shen M. M. Torres-Padilla M. E. Heard E. Reinberg D. Monomethylation of Histone H4-Lysine 20 Is Involved in Chromosome Structure and Stability and Is Essential for Mouse Development. Mol. Cell Biol. 2009, 29(8), 2278–2295.
    • (2009) Mol. Cell Biol. , vol.29 , Issue.8 , pp. 2278-2295
    • Oda, H.1    Okamoto, I.2    Murphy, N.3    Chu, J.4    Price, S.M.5    Shen, M.M.6    Torres-Padilla, M.E.7    Heard, E.8    Reinberg, D.9
  • 19
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a Novel Histone H3 Methyltransferase That Facilitates Transcription by Precluding Histone Tail Modifications Required for Heterochromatin Formation
    • Nishioka K. Chuikov S. Sarma K. Erdjument-Bromage H. Allis C. D. Tempst P. Reinberg D. Set9, a Novel Histone H3 Methyltransferase That Facilitates Transcription by Precluding Histone Tail Modifications Required for Heterochromatin Formation. Genes Dev. 2002, 16(4), 479–489.
    • (2002) Genes Dev. , vol.16 , Issue.4 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 23
    • 77951623834 scopus 로고    scopus 로고
    • Lysine Methylation Regulates the PRB Tumour Suppressor Protein
    • Munro S. Khaire N. Inche A. Carr S. La Thangue N. B. Lysine Methylation Regulates the PRB Tumour Suppressor Protein. Oncogene 2010, 29(16), 2357–2367.
    • (2010) Oncogene , vol.29 , Issue.16 , pp. 2357-2367
    • Munro, S.1    Khaire, N.2    Inche, A.3    Carr, S.4    La Thangue, N.B.5
  • 25
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-kappaB Activity through Lysine Monomethylation of p65
    • Ea C. K. Baltimore D. Regulation of NF-kappaB Activity through Lysine Monomethylation of p65. Proc. Natl. Acad. Sci. U. S. A. 2009, 106(45), 18972–18977.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.45 , pp. 18972-18977
    • Ea, C.K.1    Baltimore, D.2
  • 27
    • 44349108499 scopus 로고    scopus 로고
    • The Emerging Field of Dynamic Lysine Methylation of Non-Histone Proteins
    • Huang J. Berger S. L. The Emerging Field of Dynamic Lysine Methylation of Non-Histone Proteins. Curr. Opin. Genet. Dev. 2008, 18(2), 152–158.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , Issue.2 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 31
    • 0037099413 scopus 로고    scopus 로고
    • G9a Histone Methyltransferase Plays a Dominant Role in Euchromatic Histone H3 Lysine 9 Methylation and Is Essential for Early Embryogenesis
    • Tachibana M. Sugimoto K. Nozaki M. Ueda J. Ohta T. Ohki M. Fukuda M. Takeda N. Niida H. Kato H. G9a Histone Methyltransferase Plays a Dominant Role in Euchromatic Histone H3 Lysine 9 Methylation and Is Essential for Early Embryogenesis. Genes Dev. 2002, 16(14), 1779–1791.
    • (2002) Genes Dev. , vol.16 , Issue.14 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6    Fukuda, M.7    Takeda, N.8    Niida, H.9    Kato, H.10
  • 33
    • 33846038833 scopus 로고    scopus 로고
    • 5-Aza-2′-Deoxycytidine-Mediated Reductions in G9a Histone Methyltransferase and Histone H3 K9 Di-Methylation Levels Are Linked to Tumor Suppressor Gene Reactivation
    • Wozniak R. J. Klimecki W. T. Lau S. S. Feinstein Y. Futscher B. W. 5-Aza-2′-Deoxycytidine-Mediated Reductions in G9a Histone Methyltransferase and Histone H3 K9 Di-Methylation Levels Are Linked to Tumor Suppressor Gene Reactivation. Oncogene 2007, 26(1), 77–90.
    • (2007) Oncogene , vol.26 , Issue.1 , pp. 77-90
    • Wozniak, R.J.1    Klimecki, W.T.2    Lau, S.S.3    Feinstein, Y.4    Futscher, B.W.5
  • 34
    • 78049307486 scopus 로고    scopus 로고
    • H3K9 Histone Methyltransferase G9a Promotes Lung Cancer Invasion and Metastasis by Silencing the Cell Adhesion Molecule Ep-CAM
    • Chen M. W. Hua K. T. Kao H. J. Chi C. C. Wei L. H. Johansson G. Shiah S. G. Chen P. S. Jeng Y. M. Cheng T. Y. H3K9 Histone Methyltransferase G9a Promotes Lung Cancer Invasion and Metastasis by Silencing the Cell Adhesion Molecule Ep-CAM. Cancer Res. 2010, 70(20), 7830–7840.
    • (2010) Cancer Res. , vol.70 , Issue.20 , pp. 7830-7840
    • Chen, M.W.1    Hua, K.T.2    Kao, H.J.3    Chi, C.C.4    Wei, L.H.5    Johansson, G.6    Shiah, S.G.7    Chen, P.S.8    Jeng, Y.M.9    Cheng, T.Y.10
  • 38
    • 58649110597 scopus 로고    scopus 로고
    • Structural Basis for the Requirement of Additional Factors for MLL1 Set Domain Activity and Recognition of Epigenetic Marks
    • Southall S. M. Wong P. S. Odho Z. Roe S. M. Wilson J. R. Structural Basis for the Requirement of Additional Factors for MLL1 Set Domain Activity and Recognition of Epigenetic Marks. Mol. Cell 2009, 33(2), 181–191.
    • (2009) Mol. Cell , vol.33 , Issue.2 , pp. 181-191
    • Southall, S.M.1    Wong, P.S.2    Odho, Z.3    Roe, S.M.4    Wilson, J.R.5
  • 39
    • 77958477957 scopus 로고    scopus 로고
    • Characterization of a Novel WDR5-Binding Site That Recruits RbBP5 through a Conserved Motif to Enhance Methylation of Histone H3 Lysine 4 by Mixed Lineage Leukemia Protein-1
    • Odho Z. Southall S. M. Wilson J. R. Characterization of a Novel WDR5-Binding Site That Recruits RbBP5 through a Conserved Motif to Enhance Methylation of Histone H3 Lysine 4 by Mixed Lineage Leukemia Protein-1. J. Biol. Chem. 2010, 285(43), 32967–76.
    • (2010) J. Biol. Chem. , vol.285 , Issue.43 , pp. 32967-32976
    • Odho, Z.1    Southall, S.M.2    Wilson, J.R.3
  • 40
    • 57749108294 scopus 로고    scopus 로고
    • A Conserved Arginine-Containing Motif Crucial for the Assembly and Enzymatic Activity of the Mixed Lineage Leukemia Protein-1 Core Complex
    • Patel A. Vought V. E. Dharmarajan V. Cosgrove M. S. A Conserved Arginine-Containing Motif Crucial for the Assembly and Enzymatic Activity of the Mixed Lineage Leukemia Protein-1 Core Complex. J. Biol. Chem. 2008, 283(47), 32162–32175.
    • (2008) J. Biol. Chem. , vol.283 , Issue.47 , pp. 32162-32175
    • Patel, A.1    Vought, V.E.2    Dharmarajan, V.3    Cosgrove, M.S.4
  • 42
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 Associates with Histone H3 Methylated at K4 and Is Essential for H3 K4 Methylation and Vertebrate Development
    • Wysocka J. Swigut T. Milne T. A. Dou Y. Zhang X. Burlingame A. L. Roeder R. G. Brivanlou A. H. Allis C. D. WDR5 Associates with Histone H3 Methylated at K4 and Is Essential for H3 K4 Methylation and Vertebrate Development. Cell 2005, 121(6), 859–872.
    • (2005) Cell , vol.121 , Issue.6 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.4    Zhang, X.5    Burlingame, A.L.6    Roeder, R.G.7    Brivanlou, A.H.8    Allis, C.D.9
  • 44
    • 77957937450 scopus 로고    scopus 로고
    • Epigenetic Modifications as Therapeutic Targets
    • Kelly T. K. De Carvalho D. D. Jones P. A. Epigenetic Modifications as Therapeutic Targets. Nat. Biotechnol. 2010, 28(10), 1069–1078.
    • (2010) Nat. Biotechnol. , vol.28 , Issue.10 , pp. 1069-1078
    • Kelly, T.K.1    De Carvalho, D.D.2    Jones, P.A.3
  • 45
    • 77956191215 scopus 로고    scopus 로고
    • Biophysical Characterization of Recombinant Proteins: A Key to Higher Structural Genomics Success
    • Vedadi M. Arrowsmith C. H. Allali-Hassani A. Senisterra G. Wasney G. A. Biophysical Characterization of Recombinant Proteins: A Key to Higher Structural Genomics Success. J. Struct. Biol. 2010, 172(1), 107–119.
    • (2010) J. Struct. Biol. , vol.172 , Issue.1 , pp. 107-119
    • Vedadi, M.1    Arrowsmith, C.H.2    Allali-Hassani, A.3    Senisterra, G.4    Wasney, G.A.5
  • 47
    • 70350067813 scopus 로고    scopus 로고
    • Analysis of the Interaction of BCL9 with Beta-Catenin and Development of Fluorescence Polarization and Surface Plasmon Resonance Binding Assays for This Interaction
    • Kawamoto S. A. Thompson A. D. Coleska A. Nikolovska-Coleska Z. Yi H. Wang S. Analysis of the Interaction of BCL9 with Beta-Catenin and Development of Fluorescence Polarization and Surface Plasmon Resonance Binding Assays for This Interaction. Biochemistry 2009, 48(40), 9534–9541.
    • (2009) Biochemistry , vol.48 , Issue.40 , pp. 9534-9541
    • Kawamoto, S.A.1    Thompson, A.D.2    Coleska, A.3    Nikolovska-Coleska, Z.4    Yi, H.5    Wang, S.6
  • 48
    • 70349785135 scopus 로고    scopus 로고
    • Development of High-Throughput Assays Based on Fluorescence Polarization for Inhibitors of the Polo-Box Domains of Polo-Like Kinases 2 and 3
    • Reindl W. Graber M. Strebhardt K. Berg T. Development of High-Throughput Assays Based on Fluorescence Polarization for Inhibitors of the Polo-Box Domains of Polo-Like Kinases 2 and 3. Anal. Biochem. 2009, 395(2), 189–194.
    • (2009) Anal. Biochem. , vol.395 , Issue.2 , pp. 189-194
    • Reindl, W.1    Graber, M.2    Strebhardt, K.3    Berg, T.4
  • 49
    • 20444414511 scopus 로고    scopus 로고
    • A Coupled Fluorescent Assay for Histone Methyltransferases
    • Collazo E. Couture J. F. Bulfer S. Trievel R. C. A Coupled Fluorescent Assay for Histone Methyltransferases. Anal. Biochem. 2005, 342(1), 86–92.
    • (2005) Anal. Biochem. , vol.342 , Issue.1 , pp. 86-92
    • Collazo, E.1    Couture, J.F.2    Bulfer, S.3    Trievel, R.C.4
  • 52
    • 77955363182 scopus 로고    scopus 로고
    • Protein Lysine Methyltransferase G9a Inhibitors: Design, Synthesis, and Structure Activity Relationships of 2,4-Diamino-7-Aminoalkoxy-Quinazolines
    • Liu F. Chen X. Allali-Hassani A. Quinn A. M. Wigle T. J. Wasney G. A. Dong A. Senisterra G. Chau I. Siarheyeva A. Protein Lysine Methyltransferase G9a Inhibitors: Design, Synthesis, and Structure Activity Relationships of 2,4-Diamino-7-Aminoalkoxy-Quinazolines. J. Med. Chem. 2010, 53(15), 5844–5857.
    • (2010) J. Med. Chem. , vol.53 , Issue.15 , pp. 5844-5857
    • Liu, F.1    Chen, X.2    Allali-Hassani, A.3    Quinn, A.M.4    Wigle, T.J.5    Wasney, G.A.6    Dong, A.7    Senisterra, G.8    Chau, I.9    Siarheyeva, A.10
  • 53
    • 77952113727 scopus 로고    scopus 로고
    • A Continuous, Quantitative Fluorescent Assay for Plant Caffeic Acid O-Methyltransferases
    • Palmer N. A. Sattler S. E. Saathoff A. J. Sarath G. A Continuous, Quantitative Fluorescent Assay for Plant Caffeic Acid O-Methyltransferases. J. Agric. Food Chem. 2010, 58(9), 5220–5226.
    • (2010) J. Agric. Food Chem. , vol.58 , Issue.9 , pp. 5220-5226
    • Palmer, N.A.1    Sattler, S.E.2    Saathoff, A.J.3    Sarath, G.4
  • 55
    • 0842303035 scopus 로고    scopus 로고
    • An Enzyme-Coupled Colorimetric Assay for S-Adenosylmethionine-Dependent Methyltransferases
    • Hendricks C. L. Ross J. R. Pichersky E. Noel J. P. Zhou Z. S. An Enzyme-Coupled Colorimetric Assay for S-Adenosylmethionine-Dependent Methyltransferases. Anal. Biochem. 2004, 326(1), 100–105.
    • (2004) Anal. Biochem. , vol.326 , Issue.1 , pp. 100-105
    • Hendricks, C.L.1    Ross, J.R.2    Pichersky, E.3    Noel, J.P.4    Zhou, Z.S.5
  • 57
    • 77952361615 scopus 로고    scopus 로고
    • A Chemiluminescence-Based Method for Identification of Histone Lysine Methyltransferase Inhibitors
    • Quinn A. M. Allali-Hassani A. Vedadi M. Simeonov A. A Chemiluminescence-Based Method for Identification of Histone Lysine Methyltransferase Inhibitors. Mol. Biosyst. 2010, 6(5), 782–788.
    • (2010) Mol. Biosyst. , vol.6 , Issue.5 , pp. 782-788
    • Quinn, A.M.1    Allali-Hassani, A.2    Vedadi, M.3    Simeonov, A.4
  • 59
    • 77955399089 scopus 로고    scopus 로고
    • Accessing Protein Methyltransferase and Demethylase Enzymology Using Microfluidic Capillary Electrophoresis
    • Wigle T. J. Provencher L. M. Norris J. L. Jin J. Brown P. J. Frye S. V. Janzen W. P. Accessing Protein Methyltransferase and Demethylase Enzymology Using Microfluidic Capillary Electrophoresis. Chem. Biol. 2010, 17(7), 695–704.
    • (2010) Chem. Biol. , vol.17 , Issue.7 , pp. 695-704
    • Wigle, T.J.1    Provencher, L.M.2    Norris, J.L.3    Jin, J.4    Brown, P.J.5    Frye, S.V.6    Janzen, W.P.7
  • 60
    • 21244475895 scopus 로고    scopus 로고
    • Avidin Plate Assay System for Enzymatic Characterization of a Histone Lysine Methyltransferase
    • Gowher H. Zhang X. Cheng X. Jeltsch A. Avidin Plate Assay System for Enzymatic Characterization of a Histone Lysine Methyltransferase. Anal. Biochem. 2005, 342(2), 287–291.
    • (2005) Anal. Biochem. , vol.342 , Issue.2 , pp. 287-291
    • Gowher, H.1    Zhang, X.2    Cheng, X.3    Jeltsch, A.4
  • 61
    • 74049085886 scopus 로고    scopus 로고
    • A Continuous Protein Methyltransferase (G9a) Assay for Enzyme Activity Measurement and Inhibitor Screening
    • Dhayalan A. Dimitrova E. Rathert P. Jeltsch A. A Continuous Protein Methyltransferase (G9a) Assay for Enzyme Activity Measurement and Inhibitor Screening. J. Biomol. Screen. 2009, 14(9), 1129–1133.
    • (2009) J. Biomol. Screen. , vol.14 , Issue.9 , pp. 1129-1133
    • Dhayalan, A.1    Dimitrova, E.2    Rathert, P.3    Jeltsch, A.4
  • 63
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • Zhang J. H. Chung T. D. Oldenburg K. R. A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J. Biomol. Screen. 1999, 4(2), 67–73.
    • (1999) J. Biomol. Screen. , vol.4 , Issue.2 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 64
    • 78651268931 scopus 로고    scopus 로고
    • Histone Methyltransferases: Regulation of Transcription and Contribution to Human Disease
    • Nimura K. Ura K. Kaneda Y. Histone Methyltransferases: Regulation of Transcription and Contribution to Human Disease. J. Mol. Med. 2010, 88(12), 1213–1220.
    • (2010) J. Mol. Med. , vol.88 , Issue.12 , pp. 1213-1220
    • Nimura, K.1    Ura, K.2    Kaneda, Y.3
  • 66
    • 79955119487 scopus 로고    scopus 로고
    • Pharmacologic Disruption of Polycomb Repressive Complex 2 Inhibits Tumorigenicity and Tumor Progression in Prostate Cancer
    • Crea F. Hurt E. M. Mathews L. A. Cabarcas S. M. Sun L. Marquez V. E. Danesi R. Farrar W. L. Pharmacologic Disruption of Polycomb Repressive Complex 2 Inhibits Tumorigenicity and Tumor Progression in Prostate Cancer. Mol. Cancer 2011, 10(1), 40.
    • (2011) Mol. Cancer , vol.10 , Issue.1 , pp. 40
    • Crea, F.1    Hurt, E.M.2    Mathews, L.A.3    Cabarcas, S.M.4    Sun, L.5    Marquez, V.E.6    Danesi, R.7    Farrar, W.L.8
  • 67
    • 78650613168 scopus 로고    scopus 로고
    • Binding of Different Histone Marks Differentially Regulates the Activity and Specificity of Polycomb Repressive Complex 2 (PRC2)
    • Xu C. Bian C. Yang W. Galka M. Ouyang H. Chen C. Qiu W. Liu H. Jones A. E. MacKenzie F. Binding of Different Histone Marks Differentially Regulates the Activity and Specificity of Polycomb Repressive Complex 2 (PRC2). Proc. Natl. Acad. Sci. U. S. A. 2010, 107(45), 19266–19271.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.45 , pp. 19266-19271
    • Xu, C.1    Bian, C.2    Yang, W.3    Galka, M.4    Ouyang, H.5    Chen, C.6    Qiu, W.7    Liu, H.8    Jones, A.E.9    MacKenzie, F.10
  • 68
    • 11144241618 scopus 로고    scopus 로고
    • Substrate Specificity and Kinetic Mechanism of Mammalian G9a Histone H3 Methyltransferase
    • Patnaik D. Chin H. G. Esteve P. O. Benner J. Jacobsen S. E. Pradhan S. Substrate Specificity and Kinetic Mechanism of Mammalian G9a Histone H3 Methyltransferase. J. Biol. Chem. 2004, 279(51), 53248–53258.
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 53248-53258
    • Patnaik, D.1    Chin, H.G.2    Esteve, P.O.3    Benner, J.4    Jacobsen, S.E.5    Pradhan, S.6
  • 70
    • 32244444118 scopus 로고    scopus 로고
    • Structural Basis for the Methylation Site Specificity of SET7/9
    • Couture J. F. Collazo E. Hauk G. Trievel R. C. Structural Basis for the Methylation Site Specificity of SET7/9. Nat. Struct. Mol. Biol. 2006, 13(2), 140–146.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , Issue.2 , pp. 140-146
    • Couture, J.F.1    Collazo, E.2    Hauk, G.3    Trievel, R.C.4
  • 71
    • 0037020199 scopus 로고    scopus 로고
    • Structure and Catalytic Mechanism of a Set Domain Protein Methyltransferase
    • Trievel R. C. Beach B. M. Dirk L. M. Houtz R. L. Hurley JH. Structure and Catalytic Mechanism of a Set Domain Protein Methyltransferase. Cell 2002, 111(1), 91–103.
    • (2002) Cell , vol.111 , Issue.1 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Dirk, L.M.3    Houtz, R.L.4    Hurley, J.H.5
  • 72
    • 33947615716 scopus 로고    scopus 로고
    • Kinetic Manifestation of Processivity during Multiple Methylations Catalyzed by Set Domain Protein Methyltransferases
    • Dirk L. M. Flynn E. M. Dietzel K. Couture J. F. Trievel R. C. Houtz R. L. Kinetic Manifestation of Processivity during Multiple Methylations Catalyzed by Set Domain Protein Methyltransferases. Biochemistry 2007, 46(12), 3905–3915.
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3905-3915
    • Dirk, L.M.1    Flynn, E.M.2    Dietzel, K.3    Couture, J.F.4    Trievel, R.C.5    Houtz, R.L.6
  • 73
    • 22344454519 scopus 로고    scopus 로고
    • Structural and Functional Analysis of SET8, a Histone H4 Lys-20 Methyltransferase
    • Couture J. F. Collazo E. Brunzelle J. S. Trievel R. C. Structural and Functional Analysis of SET8, a Histone H4 Lys-20 Methyltransferase. Genes Dev. 2005, 19(12), 1455–1465.
    • (2005) Genes Dev. , vol.19 , Issue.12 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 74
    • 24344468254 scopus 로고    scopus 로고
    • Different Methylation Characteristics of Protein Arginine Methyltransferase 1 and 3 toward the Ewing Sarcoma Protein and a Peptide
    • Pahlich S. Bschir K. Chiavi C. Belyanskaya L. Gehring H. Different Methylation Characteristics of Protein Arginine Methyltransferase 1 and 3 toward the Ewing Sarcoma Protein and a Peptide. Proteins 2005, 61(1), 164–175.
    • (2005) Proteins , vol.61 , Issue.1 , pp. 164-175
    • Pahlich, S.1    Bschir, K.2    Chiavi, C.3    Belyanskaya, L.4    Gehring, H.5


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