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Volumn 4, Issue 1, 2013, Pages 13-27

The emerging roles for histone demethylases in the modulation of signaling pathways

Author keywords

Chromatin; Histone demethylation; Signaling pathways; Transcription

Indexed keywords

ANIMALIA;

EID: 84876587025     PISSN: 18685021     EISSN: 1868503X     Source Type: Journal    
DOI: 10.1515/bmc-2012-0031     Document Type: Review
Times cited : (6)

References (143)
  • 1
    • 34249337761 scopus 로고    scopus 로고
    • Perceptions of epigenetics
    • Bird A. Perceptions of epigenetics. Nature 2007; 447: 396-8.
    • (2007) Nature , vol.447 , pp. 396-398
    • Bird, A.1
  • 2
    • 79955134157 scopus 로고    scopus 로고
    • Epigenetic mechanisms in memory and synaptic function
    • Sultan FA, Day JJ. Epigenetic mechanisms in memory and synaptic function. Epigenomics 2011; 3: 157-81.
    • (2011) Epigenomics , vol.3 , pp. 157-181
    • Sultan, F.A.1    Day, J.J.2
  • 3
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister AJ, Kouzarides T. Regulation of chromatin by histone modifications. Cell Res 2011; 21: 381-95.
    • (2011) Cell Res , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 6
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: Biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast N, Shi Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu Rev Biochem 2010; 79: 155-79.
    • (2010) Annu Rev Biochem , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 9
    • 78049286684 scopus 로고    scopus 로고
    • Histone demethylases in development and disease
    • Pedersen MT, Helin K. Histone demethylases in development and disease. Trends Cell Biol 2010; 20: 662-71.
    • (2010) Trends Cell Biol , vol.20 , pp. 662-671
    • Pedersen, M.T.1    Helin, K.2
  • 11
    • 84860215207 scopus 로고    scopus 로고
    • Molecular mechanisms and potential functions of histone demethylases
    • Kooistra SM, Helin K. Molecular mechanisms and potential functions of histone demethylases. Nat Rev Mol Cell Biol 2012; 13: 297-311.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 297-311
    • Kooistra, S.M.1    Helin, K.2
  • 12
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose RJ, Kallin EM, Zhang Y. JmjC-domain-containing proteins and histone demethylation. Nat Rev Genet 2006; 7: 715-27.
    • (2006) Nat Rev Genet , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 14
    • 36049022778 scopus 로고    scopus 로고
    • JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
    • Frescas D, Guardavaccaro D, Bassermann F, Koyama-Nasu R, Pagano M. JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes. Nature 2007; 450: 309-13.
    • (2007) Nature , vol.450 , pp. 309-313
    • Frescas, D.1    Guardavaccaro, D.2    Bassermann, F.3    Koyama-Nasu, R.4    Pagano, M.5
  • 17
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K, Toumazou C, Tsukada Y, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 2006; 125: 483-95.
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 21
    • 77449121100 scopus 로고    scopus 로고
    • Jmjd1a demethylase-regulated histone modification is essential for cAMP-response element modulator-regulated gene expression and spermatogenesis
    • Liu Z, Zhou S, Liao L, Chen X, Meistrich M, Xu J. Jmjd1a demethylase-regulated histone modification is essential for cAMP-response element modulator-regulated gene expression and spermatogenesis. J Biol Chem 2010; 285: 2758-70.
    • (2010) J Biol Chem , vol.285 , pp. 2758-2770
    • Liu, Z.1    Zhou, S.2    Liao, L.3    Chen, X.4    Meistrich, M.5    Xu, J.6
  • 22
    • 77749330238 scopus 로고    scopus 로고
    • Histone demethylase JHDM2A is involved in male infertility and obesity
    • Okada Y, Tateishi K, Zhang Y. Histone demethylase JHDM2A is involved in male infertility and obesity. J Androl 2010; 31: 75-8.
    • (2010) J Androl , vol.31 , pp. 75-78
    • Okada, Y.1    Tateishi, K.2    Zhang, Y.3
  • 26
    • 67649800263 scopus 로고    scopus 로고
    • Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the Jumonji domain-containing JMJD2/KDM4 proteins
    • Trojer P, Zhang J, Yonezawa M, Schmidt A, Zheng H, Jenuwein T, Reinberg D. Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the Jumonji domain-containing JMJD2/KDM4 proteins. J Biol Chem 2009; 284: 8395-405.
    • (2009) J Biol Chem , vol.284 , pp. 8395-8405
    • Trojer, P.1    Zhang, J.2    Yonezawa, M.3    Schmidt, A.4    Zheng, H.5    Jenuwein, T.6    Reinberg, D.7
  • 27
    • 79959835076 scopus 로고    scopus 로고
    • A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation
    • Verrier L, Escaffit F, Chailleux C, Trouche D, Vandromme M. A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation. PLoS Genet 2011; 7: e1001390.
    • (2011) PLoS Genet , vol.7
    • Verrier, L.1    Escaffit, F.2    Chailleux, C.3    Trouche, D.4    Vandromme, M.5
  • 29
    • 34250168304 scopus 로고    scopus 로고
    • Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D
    • Shin S, Janknecht R. Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D. Biochem Biophys Res Commun 2007; 359: 742-6.
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 742-746
    • Shin, S.1    Janknecht, R.2
  • 30
    • 35348982301 scopus 로고    scopus 로고
    • Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells
    • Loh YH, Zhang W, Chen X, George J, Ng HH. Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells. Genes Dev 2007; 21: 2545-57.
    • (2007) Genes Dev , vol.21 , pp. 2545-2557
    • Loh, Y.H.1    Zhang, W.2    Chen, X.3    George, J.4    Ng, H.H.5
  • 31
    • 22544465244 scopus 로고    scopus 로고
    • JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2)
    • Zhang D, Yoon HG, Wong J. JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2). Mol Cell Biol 2005; 25: 6404-14.
    • (2005) Mol Cell Biol , vol.25 , pp. 6404-6414
    • Zhang, D.1    Yoon, H.G.2    Wong, J.3
  • 45
    • 55349106954 scopus 로고    scopus 로고
    • Evolutionary history of histone demethylase families: Distinct evolutionary patterns suggest functional divergence
    • Zhou X, Ma H. Evolutionary history of histone demethylase families: distinct evolutionary patterns suggest functional divergence. BMC Evol Biol 2008; 8: 294.
    • (2008) BMC Evol Biol , vol.8 , pp. 294
    • Zhou, X.1    Ma, H.2
  • 46
    • 33947152396 scopus 로고    scopus 로고
    • The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth
    • Secombe J, Li L, Carlos L, Eisenman RN. The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth. Genes Dev 2007; 21: 537-51.
    • (2007) Genes Dev , vol.21 , pp. 537-551
    • Secombe, J.1    Li, L.2    Carlos, L.3    Eisenman, R.N.4
  • 51
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa F, Totaro MG, Prosperini E, Notarbartolo S, Testa G, Natoli G. The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 2007; 130: 1083-94.
    • (2007) Cell , vol.130 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 53
    • 66149138053 scopus 로고    scopus 로고
    • The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence
    • Agger K, Cloos PA, Rudkjaer L, Williams K, Andersen G, Christensen J, Helin K. The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence. Genes Dev 2009; 23: 1171-6.
    • (2009) Genes Dev , vol.23 , pp. 1171-1176
    • Agger, K.1    Cloos, P.A.2    Rudkjaer, L.3    Williams, K.4    Andersen, G.5    Christensen, J.6    Helin, K.7
  • 54
    • 66249109644 scopus 로고    scopus 로고
    • Polycomb mediated epigenetic silencing and replication timing at the INK4a/ARF locus during senescence
    • Agherbi H, Gaussmann-Wenger A, Verthuy C, Chasson L, Serrano M, Djabali M. Polycomb mediated epigenetic silencing and replication timing at the INK4a/ARF locus during senescence. PLoS One 2009; 4: e5622.
    • (2009) PLoS One , vol.4
    • Agherbi, H.1    Gaussmann-Wenger, A.2    Verthuy, C.3    Chasson, L.4    Serrano, M.5    Djabali, M.6
  • 58
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y, Cheng X. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat Struct Mol Biol 2010; 17: 38-43.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 62
    • 77649152293 scopus 로고    scopus 로고
    • KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
    • Tsukada Y, Ishitani T, Nakayama KI. KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development. Genes Dev 2010; 24: 432-7.
    • (2010) Genes Dev , vol.24 , pp. 432-437
    • Tsukada, Y.1    Ishitani, T.2    Nakayama, K.I.3
  • 66
    • 77955280094 scopus 로고    scopus 로고
    • The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation
    • Qiu J, Shi G, Jia Y, Li J, Wu M, Dong S, Wong J. The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Res 2010; 20: 908-18.
    • (2010) Cell Res , vol.20 , pp. 908-918
    • Qiu, J.1    Shi, G.2    Jia, Y.3    Li, J.4    Wu, M.5    Dong, S.6    Wong, J.7
  • 67
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen H, Li J, Song T, Lu M, Kan PY, Lee MG, Sha B, Shi X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J Biol Chem 2010; 285: 9322-6.
    • (2010) J Biol Chem , vol.285 , pp. 9322-9326
    • Wen, H.1    Li, J.2    Song, T.3    Lu, M.4    Kan, P.Y.5    Lee, M.G.6    Sha, B.7    Shi, X.8
  • 70
    • 84862909294 scopus 로고    scopus 로고
    • Jmjd5, an H3K36me2 histone demethylase, modulates embryonic cell proliferation through the regulation of Cdkn1a expression
    • Ishimura A, Minehata K, Terashima M, Kondoh G, Hara T, Suzuki T. Jmjd5, an H3K36me2 histone demethylase, modulates embryonic cell proliferation through the regulation of Cdkn1a expression. Development 2012; 139: 749-59.
    • (2012) Development , vol.139 , pp. 749-759
    • Ishimura, A.1    Minehata, K.2    Terashima, M.3    Kondoh, G.4    Hara, T.5    Suzuki, T.6
  • 72
    • 84859746191 scopus 로고    scopus 로고
    • JMJD5, a Jumonji C (JmjC) domain-containing protein, negatively regulates osteoclastogenesis by facilitating NFATc1 protein degradation
    • Youn MY, Yokoyama A, Fujiyama-Nakamura S, Ohtake F, Minehata K, Yasuda H, Suzuki T, Kato S, Imai Y. JMJD5, a Jumonji C (JmjC) domain-containing protein, negatively regulates osteoclastogenesis by facilitating NFATc1 protein degradation. J Biol Chem 2012; 287: 12994-3004.
    • (2012) J Biol Chem , vol.287 , pp. 12994-13004
    • Youn, M.Y.1    Yokoyama, A.2    Fujiyama-Nakamura, S.3    Ohtake, F.4    Minehata, K.5    Yasuda, H.6    Suzuki, T.7    Kato, S.8    Imai, Y.9
  • 73
    • 84868706322 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of JMJD5 indicate an alternate specificity and function
    • Del Rizzo PA, Krishnan S, Trievel R. Crystal structure and functional analysis of JMJD5 indicate an alternate specificity and function. Mol Cell Biol 2012; 32: 4044-52.
    • (2012) Mol Cell Biol , vol.32 , pp. 4044-4052
    • Del Rizzo, P.A.1    Krishnan, S.2    Trievel, R.3
  • 75
  • 78
    • 34247394225 scopus 로고    scopus 로고
    • Mutation of Drosophila Lsd1 disrupts H3-K4 methylation, resulting in tissuespecific defects during development
    • Di Stefano L, Ji JY, Moon NS, Herr A, Dyson N. Mutation of Drosophila Lsd1 disrupts H3-K4 methylation, resulting in tissuespecific defects during development. Curr Biol 2007; 17: 808-12.
    • (2007) Curr Biol , vol.17 , pp. 808-812
    • Di Stefano, L.1    Ji, J.Y.2    Moon, N.S.3    Herr, A.4    Dyson, N.5
  • 83
    • 53549088904 scopus 로고    scopus 로고
    • Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin
    • Li F, Huarte M, Zaratiegui M, Vaughn MW, Shi Y, Martienssen R, Cande WZ. Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Cell 2008; 135: 272-83.
    • (2008) Cell , vol.135 , pp. 272-283
    • Li, F.1    Huarte, M.2    Zaratiegui, M.3    Vaughn, M.W.4    Shi, Y.5    Martienssen, R.6    Cande, W.Z.7
  • 85
    • 66449097375 scopus 로고    scopus 로고
    • LSD1 demethylates histone and non-histone proteins
    • Nicholson TB, Chen T. LSD1 demethylates histone and non-histone proteins. Epigenetics 2009; 4: 129-32.
    • (2009) Epigenetics , vol.4 , pp. 129-132
    • Nicholson, T.B.1    Chen, T.2
  • 87
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • Ciccone DN, Su H, Hevi S, Gay F, Lei H, Bajko J, Xu G, Li E, Chen T. KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. Nature 2009; 461: 415-8.
    • (2009) Nature , vol.461 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3    Gay, F.4    Lei, H.5    Bajko, J.6    Xu, G.7    Li, E.8    Chen, T.9
  • 88
    • 64249166375 scopus 로고    scopus 로고
    • A C. elegans LSD1 demethylase contributes to germline immortality by reprogramming epigenetic memory
    • Katz DJ, Edwards TM, Reinke V, Kelly WG. A C. elegans LSD1 demethylase contributes to germline immortality by reprogramming epigenetic memory. Cell 2009; 137: 308-20.
    • (2009) Cell , vol.137 , pp. 308-320
    • Katz, D.J.1    Edwards, T.M.2    Reinke, V.3    Kelly, W.G.4
  • 90
    • 79951855952 scopus 로고    scopus 로고
    • Fbxl10/Kdm2b deficiency accelerates neural progenitor cell death and leads to exencephaly
    • Fukuda T, Tokunaga A, Sakamoto R, Yoshida N. Fbxl10/Kdm2b deficiency accelerates neural progenitor cell death and leads to exencephaly. Mol Cell Neurosci 2011; 46: 614-24.
    • (2011) Mol Cell Neurosci , vol.46 , pp. 614-624
    • Fukuda, T.1    Tokunaga, A.2    Sakamoto, R.3    Yoshida, N.4
  • 91
    • 64749111074 scopus 로고    scopus 로고
    • Role of Jhdm2a in regulating metabolic gene expression and obesity resistance
    • Tateishi K, Okada Y, Kallin EM, Zhang Y. Role of Jhdm2a in regulating metabolic gene expression and obesity resistance. Nature 2009; 458: 757-61.
    • (2009) Nature , vol.458 , pp. 757-761
    • Tateishi, K.1    Okada, Y.2    Kallin, E.M.3    Zhang, Y.4
  • 92
    • 35948993829 scopus 로고    scopus 로고
    • Histone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and spermatogenesis
    • Okada Y, Scott G, Ray MK, Mishina Y, Zhang Y. Histone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and spermatogenesis. Nature 2007; 450: 119-23.
    • (2007) Nature , vol.450 , pp. 119-123
    • Okada, Y.1    Scott, G.2    Ray, M.K.3    Mishina, Y.4    Zhang, Y.5
  • 94
    • 79958217709 scopus 로고    scopus 로고
    • The testisenriched histone demethylase, KDM4D, regulates methylation of histone H3 lysine 9 during spermatogenesis in the mouse but is dispensable for fertility
    • Iwamori N, Zhao M, Meistrich ML, Matzuk MM. The testisenriched histone demethylase, KDM4D, regulates methylation of histone H3 lysine 9 during spermatogenesis in the mouse but is dispensable for fertility. Biol Reprod 2011; 84: 1225-34.
    • (2011) Biol Reprod , vol.84 , pp. 1225-1234
    • Iwamori, N.1    Zhao, M.2    Meistrich, M.L.3    Matzuk, M.M.4
  • 95
    • 79957892087 scopus 로고    scopus 로고
    • The histone trimethyllysine demethylase JMJD2A promotes cardiac hypertrophy in response to hypertrophic stimuli in mice
    • Zhang QJ, Chen HZ, Wang L, Liu DP, Hill JA, Liu ZP. The histone trimethyllysine demethylase JMJD2A promotes cardiac hypertrophy in response to hypertrophic stimuli in mice. J Clin Invest 2011; 121: 2447-56.
    • (2011) J Clin Invest , vol.121 , pp. 2447-2456
    • Zhang, Q.J.1    Chen, H.Z.2    Wang, L.3    Liu, D.P.4    Hill, J.A.5    Liu, Z.P.6
  • 97
    • 72449133771 scopus 로고    scopus 로고
    • The histone demethylase Dmel\Kdm4A controls genes required for life span and male-specific sex determination in Drosophila
    • Lorbeck MT, Singh N, Zervos A, Dhatta M, Lapchenko M, Yang C, Elefant F. The histone demethylase Dmel\Kdm4A controls genes required for life span and male-specific sex determination in Drosophila . Gene 2010; 450: 8-17.
    • (2010) Gene , vol.450 , pp. 8-17
    • Lorbeck, M.T.1    Singh, N.2    Zervos, A.3    Dhatta, M.4    Lapchenko, M.5    Yang, C.6    Elefant, F.7
  • 99
    • 0032772975 scopus 로고    scopus 로고
    • Jumonji gene is essential for the neurulation and cardiac development of mouse embryos with a C3H/He background
    • Takeuchi T, Kojima M, Nakajima K, Kondo S. Jumonji gene is essential for the neurulation and cardiac development of mouse embryos with a C3H/He background. Mech Dev 1999; 86: 29-38.
    • (1999) Mech Dev , vol.86 , pp. 29-38
    • Takeuchi, T.1    Kojima, M.2    Nakajima, K.3    Kondo, S.4
  • 101
    • 0033786540 scopus 로고    scopus 로고
    • A screen for new trithorax group genes identified little imaginal discs, the Drosophila melanogaster homologue of human retinoblastoma binding protein 2
    • Gildea JJ, Lopez R, Shearn A. A screen for new trithorax group genes identified little imaginal discs, the Drosophila melanogaster homologue of human retinoblastoma binding protein 2. Genetics 2000; 156: 645-63.
    • (2000) Genetics , vol.156 , pp. 645-663
    • Gildea, J.J.1    Lopez, R.2    Shearn, A.3
  • 104
    • 84855957128 scopus 로고    scopus 로고
    • UTX, a histone H3-lysine 27 demethylase, acts as a critical switch to activate the cardiac developmental program
    • Lee S, Lee JW, Lee SK. UTX, a histone H3-lysine 27 demethylase, acts as a critical switch to activate the cardiac developmental program. Dev Cell 2012; 22: 25-37.
    • (2012) Dev Cell , vol.22 , pp. 25-37
    • Lee, S.1    Lee, J.W.2    Lee, S.K.3
  • 106
    • 34347341762 scopus 로고    scopus 로고
    • A novel mutation in the PHF8 gene is associated with X-linked mental retardation with cleft lip/cleft palate
    • Abidi FE, Miano MG, Murray JC, Schwartz CE. A novel mutation in the PHF8 gene is associated with X-linked mental retardation with cleft lip/cleft palate. Clin Genet 2007; 72: 19-22.
    • (2007) Clin Genet , vol.72 , pp. 19-22
    • Abidi, F.E.1    Miano, M.G.2    Murray, J.C.3    Schwartz, C.E.4
  • 107
    • 34547862845 scopus 로고    scopus 로고
    • Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate
    • Koivisto AM, Ala-Mello S, Lemmela S, Komu HA, Rautio J, Jarvela I. Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate. Clin Genet 2007; 72: 145-9.
    • (2007) Clin Genet , vol.72 , pp. 145-149
    • Koivisto, A.M.1    Ala-Mello, S.2    Lemmela, S.3    Komu, H.A.4    Rautio, J.5    Jarvela, I.6
  • 109
    • 84859099457 scopus 로고    scopus 로고
    • Histone demethylase JMJD5 is essential for embryonic development
    • Oh S, Janknecht R. Histone demethylase JMJD5 is essential for embryonic development. Biochem Biophys Res Commun 2012; 420: 61-5.
    • (2012) Biochem Biophys Res Commun , vol.420 , pp. 61-65
    • Oh, S.1    Janknecht, R.2
  • 110
    • 78649718101 scopus 로고    scopus 로고
    • Essential functions of the histone demethylase lid
    • Li L, Greer C, Eisenman RN, Secombe J. Essential functions of the histone demethylase lid. PLoS Genet 2010; 6: e1001221.
    • (2010) PLoS Genet , vol.6
    • Li, L.1    Greer, C.2    Eisenman, R.N.3    Secombe, J.4
  • 111
    • 84856514914 scopus 로고    scopus 로고
    • Coordinating developmental signaling: Novel roles for the Hippo pathway
    • Varelas X, Wrana JL. Coordinating developmental signaling: novel roles for the Hippo pathway. Trends Cell Biol 2011; 22: 88-96.
    • (2011) Trends Cell Biol , vol.22 , pp. 88-96
    • Varelas, X.1    Wrana, J.L.2
  • 120
    • 79959745269 scopus 로고    scopus 로고
    • Epigenetics of estrogen receptor signaling: Role in hormonal cancer progression and therapy
    • Mann M, Cortez V, Vadlamudi RK. Epigenetics of estrogen receptor signaling: role in hormonal cancer progression and therapy. Cancers (Basel) 2011; 3: 1691-1707.
    • (2011) Cancers (Basel) , vol.3 , pp. 1691-1707
    • Mann, M.1    Cortez, V.2    Vadlamudi, R.K.3
  • 122
    • 77953121401 scopus 로고    scopus 로고
    • PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptoralpha target gene activation by regulating lysine demethylase 1 specificity
    • Nair SS, Nair BC, Cortez V, Chakravarty D, Metzger E, Schüle R, Brann DW, Tekmal RR, Vadlamudi RK. PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptoralpha target gene activation by regulating lysine demethylase 1 specificity. EMBO Rep 2010; 11: 438-44.
    • (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    Schüle, R.6    Brann, D.W.7    Tekmal, R.R.8    Vadlamudi, R.K.9
  • 123
  • 124
    • 77955757491 scopus 로고    scopus 로고
    • The histone demethylase JMJD2B is regulated by estrogen receptor alpha and hypoxia, and is a key mediator of estrogen induced growth
    • Yang J, Jubb AM, Pike L, Buffa FM, Turley H, Baban D, Leek R, Gatter KC, Ragoussis J, Harris AL. The histone demethylase JMJD2B is regulated by estrogen receptor alpha and hypoxia, and is a key mediator of estrogen induced growth. Cancer Res 2010; 70: 6456-66.
    • (2010) Cancer Res , vol.70 , pp. 6456-6466
    • Yang, J.1    Jubb, A.M.2    Pike, L.3    Buffa, F.M.4    Turley, H.5    Baban, D.6    Leek, R.7    Gatter, K.C.8    Ragoussis, J.9    Harris, A.L.10
  • 125
    • 84866788126 scopus 로고    scopus 로고
    • Genome-wide analysis reveals that Smad3 and JMJD3 HDM co-activate the neural developmental program
    • Estaras C, Akizu N, Garcia A, Beltran S, de la Cruz X, Martinez- Balbas MA. Genome-wide analysis reveals that Smad3 and JMJD3 HDM co-activate the neural developmental program. Development 2012; 139: 2681-91.
    • (2012) Development , vol.139 , pp. 2681-2691
    • Estaras, C.1    Akizu, N.2    Garcia, A.3    Beltran, S.4    De La Cruz, X.5    Martinez-Balbas, M.A.6
  • 126
    • 77954112841 scopus 로고    scopus 로고
    • Epigenetic disruption of the WNT/ β-catenin signaling pathway in human cancers
    • Ying Y, Tao Q. Epigenetic disruption of the WNT/ β -catenin signaling pathway in human cancers. Epigenetics 2009; 4: 307-12.
    • (2009) Epigenetics , vol.4 , pp. 307-312
    • Ying, Y.1    Tao, Q.2
  • 127
    • 84863232569 scopus 로고    scopus 로고
    • Oligoamine analogues in combination with 2-difluoromethylornithine synergistically induce re-expression of aberrantly silenced tumour-suppressor genes
    • Wu Y, Steinbergs N, Murray-Stewart T, Marton LJ, Casero RA. Oligoamine analogues in combination with 2-difluoromethylornithine synergistically induce re-expression of aberrantly silenced tumour-suppressor genes. Biochem J 2012; 442: 693-701.
    • (2012) Biochem J , vol.442 , pp. 693-701
    • Wu, Y.1    Steinbergs, N.2    Murray-Stewart, T.3    Marton, L.J.4    Casero, R.A.5
  • 128
    • 47549090432 scopus 로고    scopus 로고
    • TGF β in Cancer
    • Massague J. TGF β in Cancer. Cell 2008; 134: 215-30.
    • (2008) Cell , vol.134 , pp. 215-230
    • Massague, J.1
  • 129
  • 131
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer S, Kristensen MM, Jensen KS, Johansen JV, Staller P. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J Biol Chem 2008; 283: 36542-52.
    • (2008) J Biol Chem , vol.283 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5
  • 133
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 α enhances hypoxic gene expression and tumor growth
    • Krieg AJ, Rankin EB, Chan D, Razorenova O., Fernandez S., Giaccia AJ. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 α enhances hypoxic gene expression and tumor growth. Mol Cell Biol 2010; 30: 344-53.
    • (2010) Mol Cell Biol , vol.30 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 135
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006; 127: 635-48.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 137
    • 77954274181 scopus 로고    scopus 로고
    • Lysine methylation regulates E2F1-induced cell death
    • Kontaki H, Talianidis I. Lysine methylation regulates E2F1-induced cell death. Mol Cell 2010; 39: 152-60.
    • (2010) Mol Cell , vol.39 , pp. 152-160
    • Kontaki, H.1    Talianidis, I.2
  • 140
    • 84055211870 scopus 로고    scopus 로고
    • Lysine demethylases inhibitors
    • Suzuki T, Miyata N. Lysine demethylases inhibitors. J Med Chem 2011; 54: 8236-50.
    • (2011) J Med Chem , vol.54 , pp. 8236-8250
    • Suzuki, T.1    Miyata, N.2


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