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Volumn 16, Issue 10, 2011, Pages 1137-1152

Screening for compounds that modulate epigenetic regulation of the transcriptome: An overview

Author keywords

acetylation; CpG islands; methylation; posttranslational modification

Indexed keywords

5 AZA 2' DEOXYCYTIDINE; 8 QUINOLINOL; AMINE OXIDASE (FLAVIN CONTAINING); AZACITIDINE; CARBOPLATIN; CISPLATIN; DEPSIPEPTIDE; DNA METHYLTRANSFERASE 1; DNA METHYLTRANSFERASE 3A; DOXORUBICIN; ENTINOSTAT; ETOPOSIDE; GEMCITABINE; GEMTUZUMAB; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEMETHYLASE; HISTONE METHYLTRANSFERASE; IMATINIB; LENALIDOMIDE; MG 98; MOCETINOSTAT; N PHTHALOYLTRYPTOPHAN; PACLITAXEL; ROMIDEPSIN; TRANSCRIPTOME; TRANYLCYPROMINE; TRICHOSTATIN A; UNINDEXED DRUG; VORINOSTAT; ZEBULARINE;

EID: 83455178102     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057111417871     Document Type: Review
Times cited : (21)

References (97)
  • 1
    • 77957970301 scopus 로고    scopus 로고
    • Epigenetic Modifications and Human Disease
    • Portela A., Esteller M.. Epigenetic Modifications and Human Disease. Nat. Biotechnol. 2010 ; 28: 1057-1068
    • (2010) Nat. Biotechnol , vol.28 , pp. 1057-1068
    • Portela, A.1    Esteller, M.2
  • 2
    • 77957937450 scopus 로고    scopus 로고
    • Epigenetic Modifications as Therapeutic Targets
    • Kelly T. K., De Carvalho D., Jones P.. Epigenetic Modifications as Therapeutic Targets. Nat. Biotechnol. 2010 ; 28: 1069-1078
    • (2010) Nat. Biotechnol , vol.28 , pp. 1069-1078
    • Kelly, T.K.1    De Carvalho, D.2    Jones, P.3
  • 3
    • 77958150580 scopus 로고    scopus 로고
    • Targeting DNA Methylation for Epigenetic Therapy
    • Yang X., Lay F., Han H., Jones P.. Targeting DNA Methylation for Epigenetic Therapy. Trends Pharmacol. Sci. 2010 ; 31: 536-546
    • (2010) Trends Pharmacol. Sci , vol.31 , pp. 536-546
    • Yang, X.1    Lay, F.2    Han, H.3    Jones, P.4
  • 4
    • 34250316675 scopus 로고    scopus 로고
    • The therapeutic uses of chromatin-modifying agents
    • DOI 10.1517/14728222.11.6.835
    • Mai A.. The Therapeutic Uses of Chromatin-Modifying Agents. Expert Opin. Ther. Targets. 2007 ; 11: 835-851 (Pubitemid 46908272)
    • (2007) Expert Opinion on Therapeutic Targets , vol.11 , Issue.6 , pp. 835-851
    • Mai, A.1
  • 5
    • 77957970301 scopus 로고    scopus 로고
    • Epigenetic Modifications in Pluripotent and Differentiated Cells
    • Meissner A.. Epigenetic Modifications in Pluripotent and Differentiated Cells. Nat. Biotechnol. 2010 ; 28: 1057-1068
    • (2010) Nat. Biotechnol , vol.28 , pp. 1057-1068
    • Meissner, A.1
  • 6
    • 17744391429 scopus 로고    scopus 로고
    • Co-evolution of X-chromosome inactivation and imprinting in mammals
    • DOI 10.1038/nrg1602
    • Reik W., Lewis A.. Co-evolution of X-Chromosome Inactivation and Imprinting in Mammals. Nat. Rev. Genet. 2005 ; 6: 403-410 (Pubitemid 40577183)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.5 , pp. 403-410
    • Reik, W.1    Lewis, A.2
  • 7
    • 39749152283 scopus 로고    scopus 로고
    • DNA methyltransferase 3B (DNMT3B) mutations in ICF syndrome lead to altered epigenetic modifications and aberrant expression of genes regulating development, neurogenesis and immune function
    • DOI 10.1093/hmg/ddm341
    • Jin B., Tao Q., Peng J., Soo H. M., Wu W., Ying J., Fields C. R., Delmas A. L., Liu X., Qiu J., et al. DNA Methyltransferase 3B (DNMT3B) Mutations in ICF Syndrome Lead to Altered Epigenetic Modifications and Aberrant Expression of Genes Regulating Development, Neurogenesis and Immune Function. Hum. Mol. Genet. 2008 ; 17: 690-709 (Pubitemid 351292258)
    • (2008) Human Molecular Genetics , vol.17 , Issue.5 , pp. 690-709
    • Jin, B.1    Tao, Q.2    Peng, J.3    Soo, H.M.4    Wu, W.5    Ying, J.6    Fields, C.R.7    Delmas, A.I.8    Liu, X.9    Qiu, J.10    Robertson, K.D.11
  • 8
    • 56249113842 scopus 로고    scopus 로고
    • Epigenetic Connections between Autoimmune Disorders and Hematological Malignancies
    • Javierre B. M., Esteller M., Ballestar E.. Epigenetic Connections between Autoimmune Disorders and Hematological Malignancies. Trends Immunol. 2008 ; 29: 616-623
    • (2008) Trends Immunol , vol.29 , pp. 616-623
    • Javierre, B.M.1    Esteller, M.2    Ballestar, E.3
  • 9
    • 67650360177 scopus 로고    scopus 로고
    • Epigenetic Control in Rheumatoid Arthritis Synovial Fibroblasts
    • Karouzakis E., Gay R. E., Gay S., Neidhart M.. Epigenetic Control in Rheumatoid Arthritis Synovial Fibroblasts. Nat. Rev. Rheumatol. 2009 ; 5: 266-272
    • (2009) Nat. Rev. Rheumatol , vol.5 , pp. 266-272
    • Karouzakis, E.1    Gay, R.E.2    Gay, S.3    Neidhart, M.4
  • 16
    • 62849104641 scopus 로고    scopus 로고
    • Efficacy of Azacitidine Compared with That of Conventional Care Regimens in the Treatment of Higher-Risk Myelodysplastic Syndromes: A Randomised, Open-Label, Phase III Study
    • Fenaux P., Mufti G. J., Hellstrom-Lindberg E., Santini V., Finelli C., Giagounidis A., Schoch R., Gattermann N., Sanz G., List A., et al. Efficacy of Azacitidine Compared with That of Conventional Care Regimens in the Treatment of Higher-Risk Myelodysplastic Syndromes: A Randomised, Open-Label, Phase III Study. Lancet Oncol. 2009 ; 10: 223-232
    • (2009) Lancet Oncol , vol.10 , pp. 223-232
    • Fenaux, P.1    Mufti, G.J.2    Hellstrom-Lindberg, E.3    Santini, V.4    Finelli, C.5    Giagounidis, A.6    Schoch, R.7    Gattermann, N.8    Sanz, G.9    List, A.10
  • 17
    • 10644256532 scopus 로고    scopus 로고
    • Zebularine: A new drug for epigenetic therapy
    • DOI 10.1042/BST0320910
    • Yoo C. B., Cheng J. C., Jones P. A.. Zebularine: A New Drug for Epigenetic Therapy. Biochem. Soc. Trans. 2004 ; 32: 910-912 (Pubitemid 39655501)
    • (2004) Biochemical Society Transactions , vol.32 , Issue.6 , pp. 910-912
    • Yoo, C.B.1    Cheng, J.C.2    Jones, P.A.3
  • 18
    • 78649327715 scopus 로고    scopus 로고
    • Biological Rationale for the Use of DNA Methyltransferase Inhibitors as New Strategy for Modulation of Tumor Response to Chemotherapy and Radiation
    • Gravina G., Festuccia C., Marampon F., Popov V., Pestell R., Zani B. M., Tombolini V.. Biological Rationale for the Use of DNA Methyltransferase Inhibitors as New Strategy for Modulation of Tumor Response to Chemotherapy and Radiation. Mol. Cancer. 2010 ; 9: 305
    • (2010) Mol. Cancer , vol.9 , pp. 305
    • Gravina, G.1    Festuccia, C.2    Marampon, F.3    Popov, V.4    Pestell, R.5    Zani, B.M.6    Tombolini, V.7
  • 19
    • 0031941434 scopus 로고    scopus 로고
    • Direct real time observation of base flipping by the EcoRI DNA methyltransferase
    • DOI 10.1074/jbc.273.4.2368
    • Allan B., Beechem J., Lindstrom W., Reich N. O.. Direct Real Time Observation of Base Flipping by the EcoRI DNA Methyltransferase. J. Biol. Chem. 1998 ; 273: 2368-2373 (Pubitemid 28069292)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 2368-2373
    • Allan, B.W.1    Beechem, J.M.2    Lindstrom, W.M.3    Reich, N.O.4
  • 20
    • 18844448011 scopus 로고    scopus 로고
    • Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of Dam methyltransferase
    • DOI 10.1016/j.cell.2005.02.021, PII S009286740500187X
    • Horton J., Liebert K., Hattman S., Jeltsch A., Cheng X.. Transition from Nonspecific to Specific DNA Interactions along the Substrate-Recognition Pathway of Dam Methyltransferase. Cell. 2005 ; 121: 349-361 (Pubitemid 40692296)
    • (2005) Cell , vol.121 , Issue.3 , pp. 349-361
    • Horton, J.R.1    Liebert, K.2    Hattman, S.3    Jeltsch, A.4    Cheng, X.5
  • 21
    • 18044393242 scopus 로고    scopus 로고
    • Profound flanking sequence preference of Dnmt3a and Dnmt3b mammalian DNA methyltransferases shape the human epigenome
    • DOI 10.1016/j.jmb.2005.02.044
    • Handa V., Jeltsch A.. Profound Flanking Sequence Preference of Dnmt3a and Dnmt3b Mammalian DNA Methyltransferases Shape the Human Epigenome. J. Mol. Biol. 2005 ; 348: 1103-1112 (Pubitemid 40602369)
    • (2005) Journal of Molecular Biology , vol.348 , Issue.5 , pp. 1103-1112
    • Handa, V.1    Jeltsch, A.2
  • 23
    • 22244435605 scopus 로고    scopus 로고
    • Epigenetic reactivation of tumor suppressor genes by a novel small-molecule inhibitor of human DNA methyltransferases
    • DOI 10.1158/0008-5472.CAN-04-2957
    • Brueckner B., Boy R., Siedlecki P., Musch T., Kliem C., Zielenkiewicz P., Suhai S., Wiessler M., Lyko F.. Reactivation of Tumor Suppressor Genes by a Novel Small-Molecule Inhibitor of Human DNA Methyltransferases. Cancer Res. 2005 ; 65: 6305-6311 (Pubitemid 40994416)
    • (2005) Cancer Research , vol.65 , Issue.14 , pp. 6305-6311
    • Brueckner, B.1    Boy, R.G.2    Siedlecki, P.3    Musch, T.4    Kliem, H.C.5    Zielenkiewicz, P.6    Suhai, S.7    Wiessler, M.8    Lyko, F.9
  • 24
    • 76449100936 scopus 로고    scopus 로고
    • Novel and Selective DNA Methyltransferase Inhibitors: Docking-Based Virtual Screening and Experimental Evaluation
    • Kuck D., Singh N., Lyko F., Medina-Franco J.. Novel and Selective DNA Methyltransferase Inhibitors: Docking-Based Virtual Screening and Experimental Evaluation. Bioorg. Med. Chem. 2010 ; 18: 822-829
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 822-829
    • Kuck, D.1    Singh, N.2    Lyko, F.3    Medina-Franco, J.4
  • 25
    • 84855359225 scopus 로고    scopus 로고
    • In Development of a Non-Radioactive, No-Wash Biochemical Assay for High-Throughput Screening of Small Molecule Modulators of DNA Methyltransferases
    • Orlando, FL, Apr 27-31 abstract WP512
    • RouleauN.SilvaL.RyabovI.RobyP.MarciA. In Development of a Non-Radioactive, No-Wash Biochemical Assay for High-Throughput Screening of Small Molecule Modulators of DNA Methyltransferases, Proceedings of the SBS Conference, Orlando, FL, Apr 27-31, 2011; abstract WP512. http:// perkinelmerreagents.onconfluence.com/download/attachments/328664/ DNMT+2011+SBS+Poster.pdf?version=1&modificationDate=1303753984593
    • (2011) Proceedings of the SBS Conference
    • Rouleau, N.1    Silva, L.2    Ryabov, I.3    Roby, P.4    Marci, A.5
  • 26
    • 40549138467 scopus 로고    scopus 로고
    • Detection and Quantitation of the Activity of DNA Methyltransferases Using a Biotin/Avidin Microplate Assay
    • Liebert K., Jeltsch A.. Detection and Quantitation of the Activity of DNA Methyltransferases Using a Biotin/Avidin Microplate Assay. Methods Mol Biol. 2008 ; 418: 149-156
    • (2008) Methods Mol Biol , vol.418 , pp. 149-156
    • Liebert, K.1    Jeltsch, A.2
  • 27
    • 0037331049 scopus 로고    scopus 로고
    • Detection and analysis of enzymatic DNA methylation of oligonucleotide substrates by matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • DOI 10.1016/S0003-2697(02)00568-7, PII S0003269702005687
    • Humeny A., Beck C., Becker C. M., Jeltsch A.. Detection and Analysis of Enzymatic DNA Methylation of Oligonucleotide Substrates by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry. Anal. Biochem. 2003 ; 313: 160-166 (Pubitemid 36268831)
    • (2003) Analytical Biochemistry , vol.313 , Issue.1 , pp. 160-166
    • Humeny, A.1    Beck, C.2    Becker, C.-M.3    Jeltsch, A.4
  • 28
    • 0032519379 scopus 로고    scopus 로고
    • 2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases
    • DOI 10.1093/nar/26.4.1076
    • Holz B., Klimasauskas S., Serva S., Weinhold E.. 2-Aminopurine as a Fluorescent Probe for DNA Base Flipping by Methyltransferases. Nucleic Acids Res. 1998 ; 26: 1076-1083 (Pubitemid 28291665)
    • (1998) Nucleic Acids Research , vol.26 , Issue.4 , pp. 1076-1083
    • Holz, B.1    Klimasauskas, S.2    Serva, S.3    Weinhold, E.4
  • 30
    • 33646088737 scopus 로고    scopus 로고
    • Structure and Substrate Recognition of the Escherichia coli DNA Adenine Methyltransferase
    • Horton J. R., Liebert K., Bekes M., Jeltsch A., Cheng X.. Structure and Substrate Recognition of the Escherichia coli DNA Adenine Methyltransferase. J. Mol. Biol. 2006 ; 358: 559-570
    • (2006) J. Mol. Biol , vol.358 , pp. 559-570
    • Horton, J.R.1    Liebert, K.2    Bekes, M.3    Jeltsch, A.4    Cheng, X.5
  • 31
    • 37549014569 scopus 로고    scopus 로고
    • The M.EcoRV DNA-(Adenine N6)-Methyltransferase Uses DNA Bending for Recognition of an Expanded EcoDam Recognition Site
    • Jurkowski T. P., Anspach N., Kulishova L., Nellen W., Jeltsch A. The M.EcoRV DNA-(Adenine N6)-Methyltransferase Uses DNA Bending for Recognition of an Expanded EcoDam Recognition Site. J. Biol. Chem. 2007 ; 282: 36942-36952
    • (2007) J. Biol. Chem , vol.282 , pp. 36942-36952
    • Jurkowski, T.P.1    Anspach, N.2    Kulishova, L.3    Nellen, W.4    Jeltsch, A.5
  • 32
    • 33748754248 scopus 로고    scopus 로고
    • Conformational transitions as determinants of specificity for the DNA methyltransferase EcoRI
    • DOI 10.1074/jbc.M603388200
    • Youngblood B., Reich N. O.. Conformational Transitions as Determinants of Specificity for the DNA Methyltransferase EcoRI. J. Biol. Chem. 2006 ; 281: 26821-26831 (Pubitemid 44401711)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 26821-26831
    • Youngblood, B.1    Reich, N.O.2
  • 33
    • 63649131837 scopus 로고    scopus 로고
    • Reagentless, Electrochemical Approach for the Specific Detection of Double- and Single-Stranded DNA Binding Proteins
    • Ricci F., Bonham A., Mason A., Reich N. O., Plaxco K.. Reagentless, Electrochemical Approach for the Specific Detection of Double- and Single-Stranded DNA Binding Proteins. Anal. Chem. 2009 ; 81: 1608-1614
    • (2009) Anal. Chem , vol.81 , pp. 1608-1614
    • Ricci, F.1    Bonham, A.2    Mason, A.3    Reich, N.O.4    Plaxco, K.5
  • 34
    • 67949120337 scopus 로고    scopus 로고
    • Tracking Transcription Factor Complexes on DNA Using Total Internal Reflectance Fluorescence Protein Binding Microarrays
    • Bonham A., Neumann T., Tirrell M., Reich N. O.. Tracking Transcription Factor Complexes on DNA Using Total Internal Reflectance Fluorescence Protein Binding Microarrays. Nucleic Acids Res. 2009 ; 37 (13). e94
    • (2009) Nucleic Acids Res , vol.37 , Issue.13 , pp. 94
    • Bonham, A.1    Neumann, T.2    Tirrell, M.3    Reich, N.O.4
  • 36
    • 51949111451 scopus 로고    scopus 로고
    • Chemical Probes for Histone-Modifying Enzymes
    • Cole P.. Chemical Probes for Histone-Modifying Enzymes. Nat. Chem. Biol. 2008 ; 4: 590-597
    • (2008) Nat. Chem. Biol , vol.4 , pp. 590-597
    • Cole, P.1
  • 37
    • 58049198236 scopus 로고    scopus 로고
    • Talk Is Cheap-Cross-Talk in Establishment, Maintenance, and Readout of Chromatin Modifications
    • Fischle W.. Talk Is Cheap-Cross-Talk in Establishment, Maintenance, and Readout of Chromatin Modifications. Genes Dev. 2008 ; 22: 3375-3382
    • (2008) Genes Dev , vol.22 , pp. 3375-3382
    • Fischle, W.1
  • 38
    • 44649163849 scopus 로고    scopus 로고
    • Mechanisms Involved in the Regulation of Histone Lysine Demethylases
    • Lan F., Nottke A., Yang Shi Y.. Mechanisms Involved in the Regulation of Histone Lysine Demethylases. Curr. Opin. Cell Biol. 2008 ; 20: 316-325
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 316-325
    • Lan, F.1    Nottke, A.2    Yang Shi, Y.3
  • 39
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: Histone demethylases at the center of cellular differentiation and disease
    • DOI 10.1101/gad.1652908
    • Cloos P., Christensen J., Agger K., Helin K.. Erasing the Methyl Mark: Histone Demethylases at the Center of Cellular Differentiation and Disease. Genes Dev. 2008 ; 22: 1115-1140 (Pubitemid 351656572)
    • (2008) Genes and Development , vol.22 , Issue.9 , pp. 1115-1140
    • Cloos, P.A.C.1    Christensen, J.2    Agger, K.3    Helin, K.4
  • 40
    • 33745632390 scopus 로고    scopus 로고
    • The Epigenetic Magic of Histone Lysine Methylation
    • Jenuwein T.. The Epigenetic Magic of Histone Lysine Methylation. FEBS J. 2006 ; 273: 3121-3135
    • (2006) FEBS J , vol.273 , pp. 3121-3135
    • Jenuwein, T.1
  • 41
    • 33845755946 scopus 로고    scopus 로고
    • Heterochromatin revisited
    • DOI 10.1038/nrg2008, PII NRG2008
    • Grewal S. I., Jia S.. Heterochromatin Revisited. Nat. Rev. Genet. 2007 ; 8: 35-46 (Pubitemid 46006048)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.1 , pp. 35-46
    • Grewal, S.I.S.1    Jia, S.2
  • 42
    • 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
    • DOI 10.1101/gad.989402
    • Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., Fukuda M., Takeda N., Niida H., Kato H., et al. G9a Histone Methyltransferase Plays a Dominant Role in Euchromatic Histone H3 Lysine 9 Methylation and Is Essential for Early Embryogenesis. Genes Dev. 2002 ; 16: 1779-1791 (Pubitemid 34803894)
    • (2002) Genes and Development , 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    Shinkai, Y.11
  • 43
    • 20144388930 scopus 로고    scopus 로고
    • Histone Methyltransferases G9a and GLP Form Heteromeric Complexes and Are Both Crucial for Methylation of Euchromatin at H3-K9
    • Tachibana M., Ueda J., Fukuda M., Ohta T., Iwanari H., Sakihama T., Kodama T., Hamakubo T., Shinkai Y.. Histone Methyltransferases G9a and GLP Form Heteromeric Complexes and Are Both Crucial for Methylation of Euchromatin at H3-K9. Genes Dev. 2005 ; 19: 815-826
    • (2005) Genes Dev , vol.19 , pp. 815-826
    • Tachibana, M.1    Ueda, J.2    Fukuda, M.3    Ohta, T.4    Iwanari, H.5    Sakihama, T.6    Kodama, T.7    Hamakubo, T.8    Shinkai, Y.9
  • 44
    • 77955291294 scopus 로고    scopus 로고
    • Structural Basis for H3K4 Trimethylation by Yeast Set1/COMPASS
    • Takahashi Y., Shilatifard A.. Structural Basis for H3K4 Trimethylation by Yeast Set1/COMPASS. Adv. Enzyme Regul. 2010 ; 50 (1). 104-110
    • (2010) Adv. Enzyme Regul , vol.50 , Issue.1 , pp. 104-110
    • Takahashi, Y.1    Shilatifard, A.2
  • 45
    • 79953741829 scopus 로고    scopus 로고
    • A Role for Set1/MLL-Related Components in Epigenetic Regulation of the Caenorhabditis elegans Germ Line
    • Li T., Kelly W. G.. A Role for Set1/MLL-Related Components in Epigenetic Regulation of the Caenorhabditis elegans Germ Line. PLoS Genet. 2011 ; 7 ( 3 ):
    • (2011) PLoS Genet , vol.7 , Issue.3
    • Li, T.1    Kelly, W.G.2
  • 46
    • 77950501203 scopus 로고    scopus 로고
    • Mixed Lineage Leukemia: A Structure-Function Perspective of the MLL1 Protein
    • Cosgrove M., Patel A.. Mixed Lineage Leukemia: A Structure-Function Perspective of the MLL1 Protein. FEBS J. 2010 ; 277 (8). 1832-1842
    • (2010) FEBS J , vol.277 , Issue.8 , pp. 1832-1842
    • Cosgrove, M.1    Patel, A.2
  • 48
    • 37249024572 scopus 로고    scopus 로고
    • Structure and mechanism of lysine-specific demethylase enzymes
    • DOI 10.1074/jbc.R700027200
    • Anand R., Marmorstein R.. Structure and Mechanism of Lysine-Specific Demethylase Enzymes. J. Biol. Chem. 2007 ; 282: 35425-35429 (Pubitemid 350277089)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35425-35429
    • Anand, R.1    Marmorstein, R.2
  • 49
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • DOI 10.1074/jbc.C700100200
    • Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A.. Structural Basis of LSD1-CoREST Selectivity in Histone H3 Recognition. J. Biol Chem. 2007 ; 282: 20070-20074 (Pubitemid 47099979)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 51
    • 78649528262 scopus 로고    scopus 로고
    • Quantitative High-Throughput Screening Identifies 8-Hydroxyquinolines as Cell-Active Histone Demethylase Inhibitors
    • King O. N. F., Li X. S., Sakurai M., Kawamura A., Rose N. R., Ng S. S., Quinn A. M., Rai G., Mott B. T., Beswick P., et al. Quantitative High-Throughput Screening Identifies 8-Hydroxyquinolines as Cell-Active Histone Demethylase Inhibitors. PLoS ONE. 2010 ; 5 (11). e15535
    • (2010) PLoS ONE , vol.5 , Issue.11 , pp. 15535
    • King, O.N.F.1    Li, X.S.2    Sakurai, M.3    Kawamura, A.4    Rose, N.R.5    Ng, S.S.6    Quinn, A.M.7    Rai, G.8    Mott, B.T.9    Beswick, P.10
  • 52
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • DOI 10.1038/nature04802, PII NATURE04802
    • Li H., Ilin S., Wang W., Duncan E. M., Wysocka J., Allis C. D., Patel D. J.. Molecular Basis for Site-Specific Read-Out of Histone H3K4me3 by the BPTF PHD Finger of NURF. Nature. 2006 ; 442: 91-95 (Pubitemid 44064215)
    • (2006) Nature , vol.442 , Issue.7098 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 53
    • 78649718101 scopus 로고    scopus 로고
    • Essential Functions of the Histone Demethylase Lid
    • Li L., Greer C., Eisenman R. N., Secombe J.. Essential Functions of the Histone Demethylase Lid. PLoS Genet. 2010 ; 6 ( 11 ):
    • (2010) PLoS Genet , vol.6 , Issue.11
    • Li, L.1    Greer, C.2    Eisenman, R.N.3    Secombe, J.4
  • 55
    • 30644474460 scopus 로고    scopus 로고
    • Identification of a Specific Inhibitor of the Histone Methyltransferase SU(VAR)3-9
    • Greiner D., Bonaldi T., Eskeland R., Roemer E., Imhof A.. Identification of a Specific Inhibitor of the Histone Methyltransferase SU(VAR)3-9. Nat. Chem. Biol. 2005 ; 1: 143-145
    • (2005) Nat. Chem. Biol , vol.1 , pp. 143-145
    • Greiner, D.1    Bonaldi, T.2    Eskeland, R.3    Roemer, E.4    Imhof, A.5
  • 58
    • 77952355653 scopus 로고    scopus 로고
    • Biochemical, Structural, and Biological Evaluation of Tranylcypromine Derivatives as Inhibitors of Histone Demethylases LSD1 and LSD2
    • Binda C., Valente S., Romanenghi M., Pilotto S., Cirilli R., Karytinos A., Ciossani G., Botrugno O. A.. Biochemical, Structural, and Biological Evaluation of Tranylcypromine Derivatives as Inhibitors of Histone Demethylases LSD1 and LSD2. J. Am. Chem. Soc. 2010 ; 132: 6827-6833
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 6827-6833
    • Binda, C.1    Valente, S.2    Romanenghi, M.3    Pilotto, S.4    Cirilli, R.5    Karytinos, A.6    Ciossani, G.7    Botrugno, O.A.8
  • 62
    • 69449102464 scopus 로고    scopus 로고
    • Genome-Wide Mapping of HATs and HDACs Reveals Distinct Functions in Active and Inactive Genes
    • Wang Z., Zang C., Cui K., Schones D. E., Barski A., Peng W., Zhao K.. Genome-Wide Mapping of HATs and HDACs Reveals Distinct Functions in Active and Inactive Genes. Cell. 2009 ; 138: 1019-1031
    • (2009) Cell , vol.138 , pp. 1019-1031
    • Wang, Z.1    Zang, C.2    Cui, K.3    Schones, D.E.4    Barski, A.5    Peng, W.6    Zhao, K.7
  • 63
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • DOI 10.1016/S1074-5521(02)00092-3, PII S1074552102000923
    • Grozinger C. M., Schreiber S. L.. Deacetylase Enzymes: Biological Functions and the Use of Small-Molecule Inhibitors. Chem. Biol. 2002 ; 9: 3-16 (Pubitemid 34155860)
    • (2002) Chemistry and Biology , vol.9 , Issue.1 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 64
    • 43249121693 scopus 로고    scopus 로고
    • Histone deacetylase 5 acquires calcium/calmodulin-dependent kinase II responsiveness by oligomerization with histone deacetylase 4
    • DOI 10.1128/MCB.01611-07
    • Backs J., Backs T., Bezprozvannaya S., McKinsey T., Olson E.. Histone Deacetylase 5 Acquires Calcium/Calmodulin-Dependent Kinase II Responsiveness by Oligomerization with Histone Deacetylase 4. Mol. Cell. Biol. 2008 ; 28: 3437-3445 (Pubitemid 351657105)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.10 , pp. 3437-3445
    • Backs, J.1    Backs, T.2    Bezprozvannaya, S.3    McKinsey, T.A.4    Olson, E.N.5
  • 65
    • 26844518082 scopus 로고    scopus 로고
    • Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death
    • DOI 10.1523/JNEUROSCI.1826-05.2005
    • Bolger T., Yao T.. Intracellular Trafficking of Histone Deacetylase 4 Regulates Neuronal Cell Death. J. Neurosci. 2005 ; 25: 9544-9553 (Pubitemid 41464769)
    • (2005) Journal of Neuroscience , vol.25 , Issue.41 , pp. 9544-9553
    • Bolger, T.A.1    Yao, T.-P.2
  • 66
    • 77958524817 scopus 로고    scopus 로고
    • Dynamic Epigenetic Regulation in Neurons: Enzymes, Stimuli and Signaling Pathways
    • Riccio A.. Dynamic Epigenetic Regulation in Neurons: Enzymes, Stimuli and Signaling Pathways. Nat. Neurosci. 2010 ; 13: 1330-1337
    • (2010) Nat. Neurosci , vol.13 , pp. 1330-1337
    • Riccio, A.1
  • 67
    • 77958526499 scopus 로고    scopus 로고
    • Epigenetic Regulation of the Neural Transcriptome: The Meaning of the Marks
    • Meaney M., Ferguson-Smith A.. Epigenetic Regulation of the Neural Transcriptome: The Meaning of the Marks. Nat. Neurosci. 2010 ; 13: 1313-1318
    • (2010) Nat. Neurosci , vol.13 , pp. 1313-1318
    • Meaney, M.1    Ferguson-Smith, A.2
  • 68
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • DOI 10.1038/nrd2133, PII NRD2133
    • Bolden J. E., Peart M. J., Johnstone R. W.. Anticancer Activities of Histone Deacetylase Inhibitors. Nat. Rev. Drug Discov. 2006 ; 5: 769-784 (Pubitemid 44348499)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 69
    • 70349100446 scopus 로고    scopus 로고
    • Histone Deacetylase Inhibitors: Current Status and Overview of Recent Clinical Trials
    • Ma X., Ezzeldin H. H., Diasio R. B.. Histone Deacetylase Inhibitors: Current Status and Overview of Recent Clinical Trials. Drugs. 2009 ; 69: 1911-1934
    • (2009) Drugs , vol.69 , pp. 1911-1934
    • Ma, X.1    Ezzeldin, H.H.2    Diasio, R.B.3
  • 70
    • 0035839892 scopus 로고    scopus 로고
    • In vivo analysis of the molecular genetics of acute promyelocytic leukemia
    • DOI 10.1038/sj.onc.1204600
    • Pandolfi P. P.. In Vivo Analysis of the Molecular Genetics of Acute Promyelocytic Leukemia. Oncogene. 2001 ; 20: 5726-5735 (Pubitemid 32928110)
    • (2001) Oncogene , vol.20 , Issue.40 REV. ISS. 4 , pp. 5726-5735
    • Pandolfi, P.P.1
  • 72
    • 33748928786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
    • DOI 10.1038/nrn1989, PII NRN1989
    • Butler R., Bates G.. Histone Deacetylase Inhibitors as Therapeutics for Polyglutamine Disorders. Nat. Rev. 2006 ; 7: 784-796 (Pubitemid 44435261)
    • (2006) Nature Reviews Neuroscience , vol.7 , Issue.10 , pp. 784-796
    • Butler, R.1    Bates, G.P.2
  • 73
    • 41549136422 scopus 로고    scopus 로고
    • Paths of Convergence: Sirtuins in Aging and Neurodegeneration
    • DOI 10.1016/j.neuron.2008.03.015, PII S0896627308002614
    • Gan L., Mucke L.. Paths of Convergence: Sirtuins in Aging and Neurodegeneration. Neuron. 2008 ; 58: 10-14 (Pubitemid 351467036)
    • (2008) Neuron , vol.58 , Issue.1 , pp. 10-14
    • Gan, L.1    Mucke, L.2
  • 76
    • 77954204335 scopus 로고    scopus 로고
    • Virtual Ligand Screening of the p300/CBP Histone Acetyltransferase: Identification of a Selective Small Molecule Inhibitor
    • Bowers E. M., Yan G., Mukherjee C., Orry A., Wang L., Holbert M. A., Crump N. T., Hazzalin C. A., Liszczak G., Yuan H., et al. Virtual Ligand Screening of the p300/CBP Histone Acetyltransferase: Identification of a Selective Small Molecule Inhibitor. Chem. Biol. 2010 ; 17 (5). 471-482
    • (2010) Chem. Biol , vol.17 , Issue.5 , pp. 471-482
    • Bowers, E.M.1    Yan, G.2    Mukherjee, C.3    Orry, A.4    Wang, L.5    Holbert, M.A.6    Crump, N.T.7    Hazzalin, C.A.8    Liszczak, G.9    Yuan, H.10
  • 77
    • 0034730127 scopus 로고    scopus 로고
    • Histone Deacetylase Inhibitor Selectively Induces p21WAF1 Expression and Gene-Associated Histone Acetylation
    • Richon V. M., Sandhoff T. W., Rifkind R. A., Marks P. A.. Histone Deacetylase Inhibitor Selectively Induces p21WAF1 Expression and Gene-Associated Histone Acetylation. Proc. Natl. Acad. Sci. 2000 ; 97: 10014-10019
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 81
    • 43749109171 scopus 로고    scopus 로고
    • A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas
    • DOI 10.1038/leu.2008.9, PII LEU20089
    • Balasubramanian S., Ramos J., Luo W., Sirisawad M., Verner E., Buggy J. J.. A Novel Histone Deacetylase 8 (HDAC8)-Specific Inhibitor PCI-34051 Induces Apoptosis in T-Cell Lymphomas. Leukemia. 2008 ; 22: 1026-1034 (Pubitemid 351689885)
    • (2008) Leukemia , vol.22 , Issue.5 , pp. 1026-1034
    • Balasubramanian, S.1    Ramos, J.2    Luo, W.3    Sirisawad, M.4    Verner, E.5    Buggy, J.J.6
  • 82
    • 78650575875 scopus 로고    scopus 로고
    • Selective Inhibition of Histone Deacetylase 6 (HDAC6) Induces DNA Damage and Sensitizes Transformed Cells to Anticancer Agents
    • Namdar M., Perez G., Ngo L., Marks P.. Selective Inhibition of Histone Deacetylase 6 (HDAC6) Induces DNA Damage and Sensitizes Transformed Cells to Anticancer Agents. Proc. Natl. Acad. Sci. U. S. A. 2010 ; 107: 20003-20008
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 20003-20008
    • Namdar, M.1    Perez, G.2    Ngo, L.3    Marks, P.4
  • 87
    • 49849106385 scopus 로고    scopus 로고
    • KD5170, a Novel Mercaptoketone-Based Histone Deacetylase Inhibitor That Exhibits Broad Spectrum Antitumor Activity in Vitro and in Vivo
    • Hassig C., Symons K. T., Guo X., Nguyen P. M., Annable T., Wash P. L., Payne J. E., Jenkins D. A., Bonnefous C., Trotter C., et al. KD5170, a Novel Mercaptoketone-Based Histone Deacetylase Inhibitor That Exhibits Broad Spectrum Antitumor Activity In Vitro and In Vivo. Mol. Cancer Ther. 2008 ; 7 (5). 1054-1065
    • (2008) Mol. Cancer Ther , vol.7 , Issue.5 , pp. 1054-1065
    • Hassig, C.1    Symons, K.T.2    Guo, X.3    Nguyen, P.M.4    Annable, T.5    Wash, P.L.6    Payne, J.E.7    Jenkins, D.A.8    Bonnefous, C.9    Trotter, C.10
  • 90
    • 33845741562 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of γ-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer
    • DOI 10.1158/0008-5472.CAN-06-0049
    • Geng L., Cuneo K., Fu A., Tu T., Atadja P., Hallahan D.. Histone Deacetylase (HDAC) Inhibitor LBH589 Increases Duration of H2AX Foci and Confines HDAC4 to the Cytoplasm in Irradiated Non-Small Cell Lung Cancer. Cancer Res. 2006 ; 66: 11298-11304 (Pubitemid 46009960)
    • (2006) Cancer Research , vol.66 , Issue.23 , pp. 11298-11304
    • Geng, L.1    Cuneo, K.C.2    Fu, A.3    Tu, T.4    Atadja, P.W.5    Hallahan, D.E.6
  • 91
    • 33947315736 scopus 로고    scopus 로고
    • Cancer epigenomics: DNA methylomes and histone-modification maps
    • DOI 10.1038/nrg2005, PII NRG2005
    • Esteller M.. Cancer Epigenomics: DNA Methylomes and Histone-Modification Maps. Nat. Rev. 2007 ; 8: 286-298 (Pubitemid 46439286)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.4 , pp. 286-298
    • Esteller, M.1
  • 92
    • 26844499947 scopus 로고    scopus 로고
    • Probing lysine acetylation in proteins: Strategies, limitations, and pitfalls of in vitro acetyltransferase assays
    • DOI 10.1074/mcp.M500047-MCP200
    • Dormeyer W., Ott M., Schnolzer M.. Probing Lysine Acetylation in Proteins Strategies, Limitations, and Pitfall of In Vitro Acetyltransferase Assays. Mol. Cell. Proteomics. 2005 ; 4: 1226-1239 (Pubitemid 41448711)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1226-1239
    • Dormeyer, W.1    Ott, M.2    Schnolzer, M.3
  • 93
    • 77956916411 scopus 로고    scopus 로고
    • Peptide Arrays Identify Isoform-Selective Substrates for Profiling Endogenous Lysine Deacetylase Activity
    • Gurard-Levin Z., Kilian K., Kim J., Bahr K., Mrksich M.. Peptide Arrays Identify Isoform-Selective Substrates for Profiling Endogenous Lysine Deacetylase Activity. JACS Chem. Biol. 2010 ; 5: 863-873
    • (2010) JACS Chem. Biol , vol.5 , pp. 863-873
    • Gurard-Levin, Z.1    Kilian, K.2    Kim, J.3    Bahr, K.4    Mrksich, M.5
  • 96
    • 79955121416 scopus 로고    scopus 로고
    • Epigenetic Screening Trends
    • Spring
    • Comley J.. Epigenetic Screening Trends. Drug Discov. World. 2011 ; (Spring). 40-55
    • (2011) Drug Discov. World , pp. 40-55
    • Comley, J.1
  • 97
    • 65649152375 scopus 로고    scopus 로고
    • Phase i Study of MG98, an Oligonucleotide Antisense Inhibitor of Human DNA Methyltransferase 1, Given as a 7-Day Infusion in Patients with Advanced Solid Tumors
    • Plummer R., Vidal L., Griffin M., Lesley M., de Bono J., Coulthard S., Sludden J., Siu L. L., Chen E. X., Oza A. M., et al. Phase I Study of MG98, an Oligonucleotide Antisense Inhibitor of Human DNA Methyltransferase 1, Given as a 7-Day Infusion in Patients with Advanced Solid Tumors. Clin. Cancer Res. 2009 ; 15 (9). 3177-3183
    • (2009) Clin. Cancer Res , vol.15 , Issue.9 , pp. 3177-3183
    • Plummer, R.1    Vidal, L.2    Griffin, M.3    Lesley, M.4    De Bono, J.5    Coulthard, S.6    Sludden, J.7    Siu, L.L.8    Chen, E.X.9    Oza, A.M.10


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