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Volumn 9, Issue 1, 2014, Pages

An high-throughput in vivo screening system to select H3K4-specific histone demethylase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

COMPOUND 3195; HISTONE DEMETHYLASE INHIBITOR; HISTONE H3; OXYGENASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84900435770     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0086002     Document Type: Article
Times cited : (16)

References (52)
  • 1
    • 84857427738 scopus 로고    scopus 로고
    • Chromatin and transcription in yeast
    • Rando OJ, Winston F (2012) Chromatin and transcription in yeast. Genetics 190: 351-387.
    • (2012) Genetics , vol.190 , pp. 351-387
    • Rando, O.J.1    Winston, F.2
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin Modifications and Their Function
    • Kouzarides T (2007) Chromatin Modifications and Their Function. Cell 128: 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • DOI 10.1038/nrm1761, PII N1761
    • Martin C, Zhang Y (2005) The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 6: 838-849. (Pubitemid 41568733)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 5
    • 69949085947 scopus 로고    scopus 로고
    • Histone H3 Lysine 4 di-methylation
    • Pinskaya M, Morillon A (2009) Histone H3 Lysine 4 di-methylation. Epigenetics 4: 302-306.
    • (2009) Epigenetics , vol.4 , pp. 302-306
    • Pinskaya, M.1    Morillon, A.2
  • 7
    • 33750698262 scopus 로고    scopus 로고
    • The multiple faces of Set1
    • Dehe PM, Geli V (2006) The multiple faces of Set1. Biochem Cell Biol 84: 536-548.
    • (2006) Biochem Cell Biol , vol.84 , pp. 536-548
    • Dehe, P.M.1    Geli, V.2
  • 8
    • 84866887452 scopus 로고    scopus 로고
    • Two distinct repressive mechanisms for histone 3 lysine 4 methylation through promoting 39-end antisense transcription
    • Margaritis T, Oreal V, Brabers N, Maestroni L, Vitaliano-Prunier A, et al. (2012) Two distinct repressive mechanisms for histone 3 lysine 4 methylation through promoting 39-end antisense transcription. PLoS Genet 8: e1002952.
    • (2012) PLoS Genet , vol.8
    • Margaritis, T.1    Oreal, V.2    Brabers, N.3    Maestroni, L.4    Vitaliano-Prunier, A.5
  • 9
    • 80053411336 scopus 로고    scopus 로고
    • Recent transcription-induced histone H3 Lysine 4 (H3K4) methylation inhibits gene reactivation
    • Zhou BO, Zhou J (2011) Recent transcription-induced histone H3 Lysine 4 (H3K4) methylation inhibits gene reactivation. J Biol Chem 286: 34770-34776.
    • (2011) J Biol Chem , vol.286 , pp. 34770-34776
    • Zhou, B.O.1    Zhou, J.2
  • 10
    • 84874763341 scopus 로고    scopus 로고
    • H3K4me3 interactions with TAF3 regulate preinitiation complex assembly and selective gene activation
    • Lauberth SM, Nakayama T, Wu X, Ferris AL, Tang Z, et al. (2013) H3K4me3 interactions with TAF3 regulate preinitiation complex assembly and selective gene activation. Cell 152: 1021-1036.
    • (2013) Cell , vol.152 , pp. 1021-1036
    • Lauberth, S.M.1    Nakayama, T.2    Wu, X.3    Ferris, A.L.4    Tang, Z.5
  • 11
    • 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 PA, Christensen J, Agger K, Helin K (2008) Erasing the methyl mark: Histone demethylase at the center of cellular differentiation and disease. Genes & Dev 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
  • 13
    • 16344368814 scopus 로고    scopus 로고
    • Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
    • DOI 10.1016/j.febslet.2005.03.015
    • Forneris E, Binda C, Vanoni MA, Mattevi A, Battaglioli E (2005) Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. FEBS Lett 579: 2203-2207. (Pubitemid 40469693)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2203-2207
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Mattevi, A.4    Battaglioli, E.5
  • 14
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Shi Y, Lan F, Matson P, Mulligan P, Whetstine JR, et al. (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119: 941-953. (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 19
    • 70349780606 scopus 로고    scopus 로고
    • The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors
    • Spannhoff A, Hauser AT, Heinke R, Sippl W, Jung M (2009) The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. Chem Med Chem 4: 1568-1582.
    • (2009) Chem Med Chem , vol.4 , pp. 1568-1582
    • Spannhoff, A.1    Hauser, A.T.2    Heinke, R.3    Sippl, W.4    Jung, M.5
  • 21
    • 77449088946 scopus 로고    scopus 로고
    • The histone demethylase RBP2 is overexpressed in gastric cancer and its inhibition triggers senescence of cancer cells
    • Zeng J, Ge Z, Wang L, Li Q, Wang N, et al. (2010) The histone demethylase RBP2 is overexpressed in gastric cancer and its inhibition triggers senescence of cancer cells. Gastroenterology 138: 981-992.
    • (2010) Gastroenterology , vol.138 , pp. 981-992
    • Zeng, J.1    Ge, Z.2    Wang, L.3    Li, Q.4    Wang, N.5
  • 22
    • 80051998696 scopus 로고    scopus 로고
    • Loss of the retinoblastoma binding protein 2 (RBP2) histone demethylase suppresses tumorigenesis in mice lacking Rb1 or Men1
    • Lin W, Cao J, Liu J, Beshiri ML, Fujiwara Y, et al. (2011) Loss of the retinoblastoma binding protein 2 (RBP2) histone demethylase suppresses tumorigenesis in mice lacking Rb1 or Men1. Proc Natl Acad Sci USA 108: 13379-13386.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13379-13386
    • Lin, W.1    Cao, J.2    Liu, J.3    Beshiri, M.L.4    Fujiwara, Y.5
  • 23
    • 77950809059 scopus 로고    scopus 로고
    • A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations
    • Sharma SV, Lee DY, Li B, Quinlan MP, Takahashi F, et al. (2010) A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations. Cell 141: 69-80.
    • (2010) Cell , vol.141 , pp. 69-80
    • Sharma, S.V.1    Lee, D.Y.2    Li, B.3    Quinlan, M.P.4    Takahashi, F.5
  • 24
    • 84865017108 scopus 로고    scopus 로고
    • Genomic amplification and a role in drug-resistance for the KDM5A histone demethylase in breast cancer
    • Hou J, Wu J, Dombkowski A, Zhang K, Holowatyj A, et al. (2012) Genomic amplification and a role in drug-resistance for the KDM5A histone demethylase in breast cancer. Am J Transl Res 4: 247-256.
    • (2012) Am J Transl Res , vol.4 , pp. 247-256
    • Hou, J.1    Wu, J.2    Dombkowski, A.3    Zhang, K.4    Holowatyj, A.5
  • 25
    • 81755186916 scopus 로고    scopus 로고
    • Jumonji/ARID1 B (JARID1B) Protein Promotes Breast Tumor Cell Cycle Progression through Epigenetic Repression of MicroRNA let-7e
    • Mitra D, Das PM, Huynh FC, Jones FE (2012) Jumonji/ARID1 B (JARID1B) Protein Promotes Breast Tumor Cell Cycle Progression through Epigenetic Repression of MicroRNA let-7e. J Biol Chem 286: 40531-40535.
    • (2012) J Biol Chem , vol.286 , pp. 40531-40535
    • Mitra, D.1    Das, P.M.2    Huynh, F.C.3    Jones, F.E.4
  • 26
    • 84861868041 scopus 로고    scopus 로고
    • H3K4 demethylation by Jarid1a and Jarid1b contributes to retinoblastoma-mediated gene silencing during cellular senescence
    • Chicas A, Kapoor A, Wang X, Aksoy O, Evertts AG, et al. (2012) H3K4 demethylation by Jarid1a and Jarid1b contributes to retinoblastoma-mediated gene silencing during cellular senescence. Proc Natl Acad Sci USA 109: 8971-8976.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 8971-8976
    • Chicas, A.1    Kapoor, A.2    Wang, X.3    Aksoy, O.4    Evertts, A.G.5
  • 27
    • 84875987260 scopus 로고    scopus 로고
    • Identification of small molecules inhibitors of Jumonji AT-Rich Interactive Domain 1B (JARID1B) Histone Demethylase by a sensitive High-throughput Screen
    • Sayegh J, Ran Zou M, Morales A, Blair LP, Norcia M, et al. (2013) Identification of small molecules inhibitors of Jumonji AT-Rich Interactive Domain 1B (JARID1B) Histone Demethylase by a sensitive High-throughput Screen. J Biol Chem 288:9408-9417.
    • (2013) J Biol Chem , vol.288 , pp. 9408-9417
    • Sayegh, J.1    Ran Zou, M.2    Morales, A.3    Blair, L.P.4    Norcia, M.5
  • 29
    • 79959204866 scopus 로고    scopus 로고
    • A Selective Inhibitor and Probe of the Cellular Functions of Jumonji C Domain-Containing Histone Demethylases
    • Luo X, Liu Y, Kubicek S, Myllyharju J, Tumber A, et al. (2011) A Selective Inhibitor and Probe of the Cellular Functions of Jumonji C Domain-Containing Histone Demethylases. J Am Chem Soc 133: 9451-9456.
    • (2011) J Am Chem Soc , vol.133 , pp. 9451-9456
    • Luo, X.1    Liu, Y.2    Kubicek, S.3    Myllyharju, J.4    Tumber, A.5
  • 30
    • 77955345001 scopus 로고    scopus 로고
    • Design, Synthesis, Enzyme-Inhibitory Activity, and Effect on Human Cancer Cells of a Novel Series of Jumonji Domain-Containing Protein 2 Histone Demethylase Inhibitors
    • Hamada S, Suzuki T, Mino K, Koseki K, Oehme F, Flamme I (2010) Design, Synthesis, Enzyme-Inhibitory Activity, and Effect on Human Cancer Cells of a Novel Series of Jumonji Domain-Containing Protein 2 Histone Demethylase Inhibitors. J Med Chem 53: 5629-5638.
    • (2010) J Med Chem , vol.53 , pp. 5629-5638
    • Hamada, S.1    Suzuki, T.2    Mino, K.3    Koseki, K.4    Oehme, F.5    Flamme, I.6
  • 31
    • 77649224314 scopus 로고    scopus 로고
    • Selective Inhibitors of the JMJD2 Histone Demethylases: Combined Nondenaturing Mass Spectrometric Screening and Crystallographic Approaches
    • Rose NR, Woon ECY, Kingham GL, King ONF, Mecinović J, et al. (2010) Selective Inhibitors of the JMJD2 Histone Demethylases: Combined Nondenaturing Mass Spectrometric Screening and Crystallographic Approaches. J Med Chem 53: 1810-1818.
    • (2010) J Med Chem , vol.53 , pp. 1810-1818
    • Rose, N.R.1    Woon, E.C.Y.2    Kingham, G.L.3    King, O.N.F.4    Mecinović, J.5
  • 34
    • 34250782684 scopus 로고    scopus 로고
    • Extraction, purification and analysis of histones
    • DOI 10.1038/nprot.2007.202, PII NPROT.2007.202
    • Shechter D, Dormann HL, Allis CD, Hakel SB (2007) Extraction, purification and analysis of histones. Nat Protoc 2: 1445-1457. (Pubitemid 46952324)
    • (2007) Nature Protocols , vol.2 , Issue.6 , pp. 1445-1457
    • Shechter, D.1    Dormann, H.L.2    Allis, C.D.3    Hake, S.B.4
  • 36
    • 65249123408 scopus 로고    scopus 로고
    • Poliubiquitination of the demetylase Jhd2 controls histone methylation and genes expression
    • Mersman DP, Du H, Fingerman IM, South PF, Briggs SD (2009) Poliubiquitination of the demetylase Jhd2 controls histone methylation and genes expression. Genes Dev 23: 951-962.
    • (2009) Genes Dev , vol.23 , pp. 951-962
    • Mersman, D.P.1    Du, H.2    Fingerman, I.M.3    South, P.F.4    Briggs, S.D.5
  • 37
    • 60849094787 scopus 로고    scopus 로고
    • Specific roles for the Ccr4-Not complex subunits in expression of the genome
    • Azzouz N, Panasenko OO, Deluen C, Hsieh J, Theiler G, et al. (2010) Specific roles for the Ccr4-Not complex subunits in expression of the genome. RNA 15: 277-383.
    • (2010) RNA , vol.15 , pp. 277-383
    • Azzouz, N.1    Panasenko, O.O.2    Deluen, C.3    Hsieh, J.4    Theiler, G.5
  • 38
    • 33646505724 scopus 로고    scopus 로고
    • Structural insights into histone demethylation by JMJD2 family members
    • Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, et al. (2006) Structural insights into histone demethylation by JMJD2 family members. Cell 125: 691-702.
    • (2006) Cell , vol.125 , pp. 691-702
    • Chen, Z.1    Zang, J.2    Whetstine, J.3    Hong, X.4    Davrazou, F.5
  • 39
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • DOI 10.1038/nrg1945, PII NRG1945
    • Klose JR, Kallin EM, Khang Y (2006) JmjC-domain-containing proteins and histone demethylation. Nat Rev Gen 7: 715-727. (Pubitemid 44260007)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.9 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 42
    • 84861182365 scopus 로고    scopus 로고
    • Studies of H3K4me3 demethylation by KDM5B/Jarid1B/PLU1 reveals strong substrate recognition in vitro and identifies 2,4-pyridine-dicarboxylic acid as an in vitro and in cell inhibitor
    • Kristensen LH, Nielsen AL, Helgstrand C, Lees M, Cloos P, et al. (2012) Studies of H3K4me3 demethylation by KDM5B/Jarid1B/PLU1 reveals strong substrate recognition in vitro and identifies 2,4-pyridine-dicarboxylic acid as an in vitro and in cell inhibitor. FEBS J 279: 1905-1914.
    • (2012) FEBS J , vol.279 , pp. 1905-1914
    • Kristensen, L.H.1    Nielsen, A.L.2    Helgstrand, C.3    Lees, M.4    Cloos, P.5
  • 44
    • 33751169387 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1)
    • Ke Q, Costa M (2006) Hypoxia-inducible factor-1 (HIF-1). Mol Pharmacol 70: 1469-1480.
    • (2006) Mol Pharmacol , vol.70 , pp. 1469-1480
    • Ke, Q.1    Costa, M.2
  • 45
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • DOI 10.1038/nchembio0308-152, PII NCHEMBIO0308152
    • Loenarz C, Schofield CJ (2008) Expanding chemical biology of 2-oxoglutarate oxygenase. Nat Chem Biol 4: 152-156. (Pubitemid 351264133)
    • (2008) Nature Chemical Biology , vol.4 , Issue.3 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 46
    • 78049396647 scopus 로고    scopus 로고
    • Expanding role of the Jumonji C Domain as an RNA hydroxylase
    • Noma A, Ishitani R, Kato M, Nagao A, Nureki O, et al. (2010) Expanding role of the Jumonji C Domain as an RNA hydroxylase. J Biol Chem 285: 34503-34507.
    • (2010) J Biol Chem , vol.285 , pp. 34503-34507
    • Noma, A.1    Ishitani, R.2    Kato, M.3    Nagao, A.4    Nureki, O.5
  • 47
    • 84889595831 scopus 로고    scopus 로고
    • A small molecule modulates Jumonji histone demethylase activity and selectively inhibits cancer growth
    • Wang L, Chang J, Varghese D, Dellinger M, Kumar S, et al. (2013) A small molecule modulates Jumonji histone demethylase activity and selectively inhibits cancer growth Nat Comm 4: 2035.
    • (2013) Nat Comm , vol.4 , pp. 2035
    • Wang, L.1    Chang, J.2    Varghese, D.3    Dellinger, M.4    Kumar, S.5
  • 48
    • 84869238311 scopus 로고    scopus 로고
    • Maintenance of gene silencing by the coordinate action of the H3K9 methyltransferase G9a/KMT1C and the H3K4 demethylase Jarid1a/KDM5A
    • Chaturvedi CP, Somasundaram B, Singh K, Carpenedo R, Stanford WL, et al. (2012) Maintenance of gene silencing by the coordinate action of the H3K9 methyltransferase G9a/KMT1C and the H3K4 demethylase Jarid1a/KDM5A. Proc Natl Acad Sci USA 46: 18845-18850.
    • (2012) Proc Natl Acad Sci USA , vol.46 , pp. 18845-18850
    • Chaturvedi, C.P.1    Somasundaram, B.2    Singh, K.3    Carpenedo, R.4    Stanford, W.L.5
  • 49
    • 61349113967 scopus 로고    scopus 로고
    • Dynamic association of MLL1, H3K4 trimethylation with chromatin and Hox gene expression during the cell cycle
    • Mishra BP, Ansari KI, Mandal SS (2009) Dynamic association of MLL1, H3K4 trimethylation with chromatin and Hox gene expression during the cell cycle. FEBS J 276: 1629-1640.
    • (2009) FEBS J , vol.276 , pp. 1629-1640
    • Mishra, B.P.1    Ansari, K.I.2    Mandal, S.S.3
  • 50
    • 84864013839 scopus 로고    scopus 로고
    • Origin and formation of histone methylation across the human cell cycle
    • Zee BM, Britton LP, Wolle D, Haberman DM, Garcia BA (2012) Origin and formation of histone methylation across the human cell cycle. Mol Cell Biol 32: 2503-2514.
    • (2012) Mol Cell Biol , vol.32 , pp. 2503-2514
    • Zee, B.M.1    Britton, L.P.2    Wolle, D.3    Haberman, D.M.4    Garcia, B.A.5
  • 51
    • 78649807567 scopus 로고    scopus 로고
    • Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA
    • Kaneco S, Li G, Son J, Xu C-F, Margueron R, et al. (2010) Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA Genes & Dev 24: 2615-2620.
    • (2010) Genes & Dev , vol.24 , pp. 2615-2620
    • Kaneco, S.1    Li, G.2    Son, J.3    Xu, C.-F.4    Margueron, R.5


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