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Volumn 83, Issue 7, 2015, Pages 1316-1326

Structural diversity of the epigenetics pocketome

Author keywords

Binding pocket; Chromatin factors; Drug design; Epigenetics; Inhibitor; Pocketome; Selectivity; Structure

Indexed keywords

ACYLTRANSFERASE; DNA; HISTONE; LYSINE ACETYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE; RNA; SIRTUIN; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; CHROMATIN; LIGAND; MOLECULAR LIBRARY; PROTEIN BINDING; TUMOR PROTEIN;

EID: 84931010257     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24830     Document Type: Article
Times cited : (9)

References (32)
  • 1
    • 84863986133 scopus 로고    scopus 로고
    • Functions of DNA methylation: islands, start sites, gene bodies and beyond
    • Jones PA. Functions of DNA methylation: islands, start sites, gene bodies and beyond. Nat Rev Genet 2012;13:484-492.
    • (2012) Nat Rev Genet , vol.13 , pp. 484-492
    • Jones, P.A.1
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007;128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 84867553154 scopus 로고    scopus 로고
    • Human RNA methyltransferase BCDIN3D regulates microRNA processing
    • Xhemalce B, Robson SC, Kouzarides T. Human RNA methyltransferase BCDIN3D regulates microRNA processing. Cell 2012;151:278-288.
    • (2012) Cell , vol.151 , pp. 278-288
    • Xhemalce, B.1    Robson, S.C.2    Kouzarides, T.3
  • 4
    • 84896034247 scopus 로고    scopus 로고
    • Molecular biology. Internal mRNA methylation finally finds functions
    • Nilsen TW. Molecular biology. Internal mRNA methylation finally finds functions. Science 2014;343:1207-1208.
    • (2014) Science , vol.343 , pp. 1207-1208
    • Nilsen, T.W.1
  • 6
    • 43949136445 scopus 로고    scopus 로고
    • Modes of action of the DNA methyltransferase inhibitors azacytidine and decitabine
    • Stresemann C, Lyko F. Modes of action of the DNA methyltransferase inhibitors azacytidine and decitabine. Int J Cancer 2008;123:8-13.
    • (2008) Int J Cancer , vol.123 , pp. 8-13
    • Stresemann, C.1    Lyko, F.2
  • 7
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug
    • Marks PA, Breslow R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat Biotechnol 2007;25:84-90.
    • (2007) Nat Biotechnol , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 8
    • 84890284556 scopus 로고    scopus 로고
    • Molecular pathways: protein methyltransferases in cancer
    • Copeland RA. Molecular pathways: protein methyltransferases in cancer. Clin Cancer Res 2013;19:6344-6350.
    • (2013) Clin Cancer Res , vol.19 , pp. 6344-6350
    • Copeland, R.A.1
  • 9
    • 84865066583 scopus 로고    scopus 로고
    • ChromoHub: a data hub for navigators of chromatin-mediated signalling
    • Liu L, Zhen XT, Denton E, Marsden BD, Schapira M. ChromoHub: a data hub for navigators of chromatin-mediated signalling. Bioinformatics 2012;28:2205-2206.
    • (2012) Bioinformatics , vol.28 , pp. 2205-2206
    • Liu, L.1    Zhen, X.T.2    Denton, E.3    Marsden, B.D.4    Schapira, M.5
  • 10
    • 79951526605 scopus 로고    scopus 로고
    • Ligand binding site superposition and comparison based on atomic property fields: identification of distant homologues, convergent evolution and PDB-wide clustering of binding sites
    • Totrov M. Ligand binding site superposition and comparison based on atomic property fields: identification of distant homologues, convergent evolution and PDB-wide clustering of binding sites. BMC Bioinform 2011;12: S35
    • (2011) BMC Bioinform , vol.12 , pp. S35
    • Totrov, M.1
  • 12
    • 80054765573 scopus 로고    scopus 로고
    • Structural biology of human metal-dependent histone deacetylases
    • Schapira M. Structural biology of human metal-dependent histone deacetylases. Handb Exp Pharmacol 2011;206:225-240.
    • (2011) Handb Exp Pharmacol , vol.206 , pp. 225-240
    • Schapira, M.1
  • 15
    • 69949148388 scopus 로고    scopus 로고
    • Protein methyltransferases as a target class for drug discovery
    • Copeland RA, Solomon ME, Richon VM. Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov 2009;8:724-732.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 16
    • 84899973908 scopus 로고    scopus 로고
    • Targeting bromodomains: epigenetic readers of lysine acetylation
    • Filippakopoulos P, Knapp S. Targeting bromodomains: epigenetic readers of lysine acetylation. Nat Rev Drug Discov 2014;13:337-356.
    • (2014) Nat Rev Drug Discov , vol.13 , pp. 337-356
    • Filippakopoulos, P.1    Knapp, S.2
  • 25
    • 84911927586 scopus 로고    scopus 로고
    • Structural biology and chemistry of protein arginine methyltransferases
    • Schapira M, Ferreira de Freitas R. Structural biology and chemistry of protein arginine methyltransferases. Med Chem Commun 2014;5:1779-1788.
    • (2014) Med Chem Commun , vol.5 , pp. 1779-1788
    • Schapira, M.1    Ferreira de Freitas, R.2
  • 26
    • 80455125845 scopus 로고    scopus 로고
    • Structural chemistry of human SET domain protein methyltransferases
    • Schapira M. Structural chemistry of human SET domain protein methyltransferases. Curr Chem Genomics 2012;5:85-94.
    • (2012) Curr Chem Genomics , vol.5 , pp. 85-94
    • Schapira, M.1
  • 27
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W, Wang Y, Allis CD. Binary switches and modification cassettes in histone biology and beyond. Nature 2003;425:475-479.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 28
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
    • Taverna SD, Li H, Ruthenburg AJ, Allis CD, Patel DJ. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat Struct Mol Biol 2007;14:1025-1040.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 30
    • 79953694494 scopus 로고    scopus 로고
    • Biophysical probes reveal a "compromise" nature of the methyl-lysine binding pocket in l3mbtl1
    • Gao C, Herold JM, Kireev D, Wigle T, Norris JL, Frye S. Biophysical probes reveal a "compromise" nature of the methyl-lysine binding pocket in l3mbtl1. J Am Chem Soc 2011;133:5357-5362.
    • (2011) J Am Chem Soc , vol.133 , pp. 5357-5362
    • Gao, C.1    Herold, J.M.2    Kireev, D.3    Wigle, T.4    Norris, J.L.5    Frye, S.6
  • 31
    • 84885848767 scopus 로고    scopus 로고
    • Tudor: a versatile family of histone methylation 'readers'
    • Lu R, Wang GG. Tudor: a versatile family of histone methylation 'readers'. Trends Biochem Sci 2013;38:546-555.
    • (2013) Trends Biochem Sci , vol.38 , pp. 546-555
    • Lu, R.1    Wang, G.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.