메뉴 건너뛰기




Volumn 19, Issue 4, 2013, Pages 719-733

Regulation and function of DNA and histone methylations

Author keywords

Chromatin modifications; DNA methylation; Epigenetics; Histone methylation

Indexed keywords

ADENOSYLHOMOCYSTEINASE; DNA METHYLTRANSFERASE; DNA METHYLTRANSFERASE 1; DNA METHYLTRANSFERASE 3A; DNA METHYLTRANSFERASE 3B; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; RNA POLYMERASE II; S ADENOSYLMETHIONINE;

EID: 84876697723     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161213804581990     Document Type: Review
Times cited : (6)

References (280)
  • 1
    • 78049440475 scopus 로고    scopus 로고
    • Chromatin landscape dictates HSF binding to target DNA elements
    • Guertin MJ, Lis JT. Chromatin landscape dictates HSF binding to target DNA elements. PLoS genetics 2010; 6.
    • (2010) PLoS genetics , pp. 6
    • Guertin, M.J.1    Lis, J.T.2
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001; 293: 1074-80.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • Luger K. Structure and dynamic behavior of nucleosomes. Curr Opin Genet Dev 2003; 13: 127-35.
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 127-135
    • Luger, K.1
  • 4
    • 81855212626 scopus 로고    scopus 로고
    • Gracefully ageing at 50, X-chromosome inactivation becomes a paradigm for RNA and chromatin control
    • Lee JT. Gracefully ageing at 50, X-chromosome inactivation becomes a paradigm for RNA and chromatin control. Nature reviews. Molecular cell biology 2011; 12: 815-26.
    • (2011) Nature reviews. Molecular cell biology , vol.12 , pp. 815-826
    • Lee, J.T.1
  • 7
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith BC, Denu JM. Chemical mechanisms of histone lysine and arginine modifications. Biochimica et biophysica acta 2009; 1789: 45-57.
    • (2009) Biochimica et biophysica acta , vol.1789 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 11
    • 31144449613 scopus 로고    scopus 로고
    • Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2
    • Goll MG, Kirpekar F, Maggert KA, et al. Methylation of tRNAAsp by the DNA methyltransferase homolog Dnmt2. Science 2006; 311: 395-8.
    • (2006) Science , vol.311 , pp. 395-398
    • Goll, M.G.1    Kirpekar, F.2    Maggert, K.A.3
  • 12
    • 0032722062 scopus 로고    scopus 로고
    • Recombinant human DNA (cytosine-5) methyltransferase. I. Expression, purification, and comparison of de novo and maintenance methylation
    • Pradhan S, Bacolla A, Wells RD, Roberts RJ. Recombinant human DNA (cytosine-5) methyltransferase. I. Expression, purification, and comparison of de novo and maintenance methylation. The Journal of biological chemistry 1999; 274: 33002-10.
    • (1999) The Journal of biological chemistry , vol.274 , pp. 33002-33010
    • Pradhan, S.1    Bacolla, A.2    Wells, R.D.3    Roberts, R.J.4
  • 13
    • 0036683055 scopus 로고    scopus 로고
    • Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases
    • Kim GD, Ni J, Kelesoglu N, Roberts RJ, Pradhan S. Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases. The EMBO journal 2002; 21: 4183-95.
    • (2002) The EMBO journal , vol.21 , pp. 4183-4195
    • Kim, G.D.1    Ni, J.2    Kelesoglu, N.3    Roberts, R.J.4    Pradhan, S.5
  • 14
    • 0042132027 scopus 로고    scopus 로고
    • Establishment and maintenance of genomic methylation patterns in mouse embryonic stem cells by Dnmt3a and Dnmt3b
    • Chen T, Ueda Y, Dodge JE, Wang Z, Li E. Establishment and maintenance of genomic methylation patterns in mouse embryonic stem cells by Dnmt3a and Dnmt3b. Molecular and cellular biology 2003; 23: 5594-605.
    • (2003) Molecular and cellular biology , vol.23 , pp. 5594-5605
    • Chen, T.1    Ueda, Y.2    Dodge, J.E.3    Wang, Z.4    Li, E.5
  • 16
    • 0030770835 scopus 로고    scopus 로고
    • Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1
    • Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF. Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science 1997; 277: 1996-2000.
    • (1997) Science , vol.277 , pp. 1996-2000
    • Chuang, L.S.1    Ian, H.I.2    Koh, T.W.3    Ng, H.H.4    Xu, G.5    Li, B.F.6
  • 17
    • 0033615717 scopus 로고    scopus 로고
    • DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development
    • Okano M, Bell DW, Haber DA, Li E. DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development. Cell 1999; 99: 247-57.
    • (1999) Cell , vol.99 , pp. 247-257
    • Okano, M.1    Bell, D.W.2    Haber, D.A.3    Li, E.4
  • 18
    • 43749098985 scopus 로고    scopus 로고
    • DNA methylation landscapes: Provocative insights from epigenomics
    • Suzuki MM, Bird A. DNA methylation landscapes: provocative insights from epigenomics. Nature reviews. Genetics 2008; 9: 465-76.
    • (2008) Nature reviews. Genetics , vol.9 , pp. 465-476
    • Suzuki, M.M.1    Bird, A.2
  • 19
    • 34250188803 scopus 로고    scopus 로고
    • Genomic patterns of DNA methylation: Targets and function of an epigenetic mark
    • Weber M, Schubeler D. Genomic patterns of DNA methylation: targets and function of an epigenetic mark. Current opinion in cell biology 2007; 19: 273-80.
    • (2007) Current opinion in cell biology , vol.19 , pp. 273-280
    • Weber, M.1    Schubeler, D.2
  • 21
    • 70450217879 scopus 로고    scopus 로고
    • Human DNA methylomes at base resolution show widespread epigenomic differences
    • Lister R, Pelizzola M, Dowen RH, et al. Human DNA methylomes at base resolution show widespread epigenomic differences. Nature 2009; 462: 315-22.
    • (2009) Nature , vol.462 , pp. 315-322
    • Lister, R.1    Pelizzola, M.2    Dowen, R.H.3
  • 22
    • 84355163093 scopus 로고    scopus 로고
    • DNA-binding factors shape the mouse methylome at distal regulatory regions
    • Stadler MB, Murr R, Burger L, et al. DNA-binding factors shape the mouse methylome at distal regulatory regions. Nature 2011; 480: 490-5.
    • (2011) Nature , vol.480 , pp. 490-495
    • Stadler, M.B.1    Murr, R.2    Burger, L.3
  • 23
    • 33847293264 scopus 로고    scopus 로고
    • Complete inactivation of DNMT1 leads to mitotic catastrophe in human cancer cells
    • Chen T, Hevi S, Gay F, et al. Complete inactivation of DNMT1 leads to mitotic catastrophe in human cancer cells. Nature genetics 2007; 39: 391-6.
    • (2007) Nature genetics , vol.39 , pp. 391-396
    • Chen, T.1    Hevi, S.2    Gay, F.3
  • 24
    • 0029803192 scopus 로고    scopus 로고
    • De novo DNA cytosine methyltransferase activities in mouse embryonic stem cells
    • Lei H, Oh SP, Okano M, et al. De novo DNA cytosine methyltransferase activities in mouse embryonic stem cells. Development 1996; 122: 3195-205.
    • (1996) Development , vol.122 , pp. 3195-3205
    • Lei, H.1    Oh, S.P.2    Okano, M.3
  • 25
    • 0026708177 scopus 로고
    • Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
    • Li E, Bestor TH, Jaenisch R. Targeted mutation of the DNA methyltransferase gene results in embryonic lethality. Cell 1992; 69: 915-26.
    • (1992) Cell , vol.69 , pp. 915-926
    • Li, E.1    Bestor, T.H.2    Jaenisch, R.3
  • 26
    • 3042584653 scopus 로고    scopus 로고
    • Essential role for de novo DNA methyltransferase Dnmt3a in paternal and maternal imprinting
    • Kaneda M, Okano M, Hata K, et al. Essential role for de novo DNA methyltransferase Dnmt3a in paternal and maternal imprinting. Nature 2004; 429: 900-3.
    • (2004) Nature , vol.429 , pp. 900-903
    • Kaneda, M.1    Okano, M.2    Hata, K.3
  • 27
    • 26444561533 scopus 로고    scopus 로고
    • Physical and functional interactions between the human DNMT3L protein and members of the de novo methyltransferase family
    • Chen ZX, Mann JR, Hsieh CL, Riggs AD, Chedin F. Physical and functional interactions between the human DNMT3L protein and members of the de novo methyltransferase family. Journal of cellular biochemistry 2005; 95: 902-17.
    • (2005) Journal of cellular biochemistry , vol.95 , pp. 902-917
    • Chen, Z.X.1    Mann, J.R.2    Hsieh, C.L.3    Riggs, A.D.4    Chedin, F.5
  • 28
    • 17144369504 scopus 로고    scopus 로고
    • Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B DNA-(cytosine-C5)-methyltransferases by Dnmt3L
    • Gowher H, Liebert K, Hermann A, Xu G, Jeltsch A. Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B DNA-(cytosine-C5)-methyltransferases by Dnmt3L. The Journal of biological chemistry 2005; 280: 13341-8.
    • (2005) The Journal of biological chemistry , vol.280 , pp. 13341-13348
    • Gowher, H.1    Liebert, K.2    Hermann, A.3    Xu, G.4    Jeltsch, A.5
  • 31
    • 0035930660 scopus 로고    scopus 로고
    • Dnmt3L and the establishment of maternal genomic imprints
    • Bourc'his D, Xu GL, Lin CS, Bollman B, Bestor TH. Dnmt3L and the establishment of maternal genomic imprints. Science 2001; 294: 2536-9.
    • (2001) Science , vol.294 , pp. 2536-2539
    • Bourc'his, D.1    Xu, G.L.2    Lin, C.S.3    Bollman, B.4    Bestor, T.H.5
  • 32
    • 79957623760 scopus 로고    scopus 로고
    • Mutations in DNMT1 cause hereditary sensory neuropathy with dementia and hearing loss
    • Klein CJ, Botuyan MV, Wu Y, et al. Mutations in DNMT1 cause hereditary sensory neuropathy with dementia and hearing loss. Nature genetics 2011; 43: 595-600.
    • (2011) Nature genetics , vol.43 , pp. 595-600
    • Klein, C.J.1    Botuyan, M.V.2    Wu, Y.3
  • 33
    • 0033547330 scopus 로고    scopus 로고
    • Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene
    • Xu GL, Bestor TH, Bourc'his D, et al. Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene. Nature 1999; 402: 187-91.
    • (1999) Nature , vol.402 , pp. 187-191
    • Xu, G.L.1    Bestor, T.H.2    Bourc'his, D.3
  • 37
    • 0033580326 scopus 로고    scopus 로고
    • A mammalian protein with specific demethylase activity for mCpG DNA
    • Bhattacharya SK, Ramchandani S, Cervoni N, Szyf M. A mammalian protein with specific demethylase activity for mCpG DNA. Nature 1999; 397: 579-83.
    • (1999) Nature , vol.397 , pp. 579-583
    • Bhattacharya, S.K.1    Ramchandani, S.2    Cervoni, N.3    Szyf, M.4
  • 39
    • 0034176639 scopus 로고    scopus 로고
    • Active demethylation of the paternal genome in the mouse zygote
    • Oswald J, Engemann S, Lane N, et al. Active demethylation of the paternal genome in the mouse zygote. Current biology: CB 2000; 10: 475-8.
    • (2000) Current biology: CB , vol.10 , pp. 475-478
    • Oswald, J.1    Engemann, S.2    Lane, N.3
  • 40
    • 38349100549 scopus 로고    scopus 로고
    • Epigenetic events in mammalian germ-cell development: Reprogramming and beyond. Nature reviews
    • Sasaki H, Matsui Y. Epigenetic events in mammalian germ-cell development: reprogramming and beyond. Nature reviews. Genetics 2008; 9: 129-40.
    • (2008) Genetics , vol.9 , pp. 129-140
    • Sasaki, H.1    Matsui, Y.2
  • 41
    • 73349104113 scopus 로고    scopus 로고
    • Active DNA demethylation mediated by DNA glycosylases
    • Zhu JK. Active DNA demethylation mediated by DNA glycosylases. Annual review of genetics 2009; 43: 143-66.
    • (2009) Annual review of genetics , vol.43 , pp. 143-166
    • Zhu, J.K.1
  • 43
    • 79959937861 scopus 로고    scopus 로고
    • Thymine DNA glycosylase is essential for active DNA demethylation by linked deaminationbase excision repair
    • Cortellino S, Xu J, Sannai M, et al. Thymine DNA glycosylase is essential for active DNA demethylation by linked deaminationbase excision repair. Cell 2011; 146: 67-79.
    • (2011) Cell , vol.146 , pp. 67-79
    • Cortellino, S.1    Xu, J.2    Sannai, M.3
  • 44
    • 80053917872 scopus 로고    scopus 로고
    • Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: Potential implications for active demethylation of CpG sites
    • Maiti A, Drohat AC. Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites. The Journal of biological chemistry 2011; 286: 35334-8.
    • (2011) The Journal of biological chemistry , vol.286 , pp. 35334-35338
    • Maiti, A.1    Drohat, A.C.2
  • 45
    • 80052495940 scopus 로고    scopus 로고
    • Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA
    • He YF, Li BZ, Li Z, et al. Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA. Science 2011; 333: 1303-7.
    • (2011) Science , vol.333 , pp. 1303-1307
    • He, Y.F.1    Li, B.Z.2    Li, Z.3
  • 46
    • 80052461558 scopus 로고    scopus 로고
    • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    • Ito S, Shen L, Dai Q, et al. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 2011; 333: 1300-3.
    • (2011) Science , vol.333 , pp. 1300-1303
    • Ito, S.1    Shen, L.2    Dai, Q.3
  • 47
    • 82955207588 scopus 로고    scopus 로고
    • Mechanisms and functions of Tet proteinmediated 5-methylcytosine oxidation
    • Wu H, Zhang Y. Mechanisms and functions of Tet proteinmediated 5-methylcytosine oxidation. Genes & development 2011; 25: 2436-52.
    • (2011) Genes & development , vol.25 , pp. 2436-2452
    • Wu, H.1    Zhang, Y.2
  • 48
    • 84555189745 scopus 로고    scopus 로고
    • DNA methylation: TET proteins-guardians of CpG islands?
    • Williams K, Christensen J, Helin K. DNA methylation: TET proteins-guardians of CpG islands? EMBO reports 2011; 13: 28-35.
    • (2011) EMBO reports , vol.13 , pp. 28-35
    • Williams, K.1    Christensen, J.2    Helin, K.3
  • 49
    • 79954457998 scopus 로고    scopus 로고
    • Genome-wide analysis of 5-hydroxymethylcytosine distribution reveals its dual function in transcriptional regulation in mouse embryonic stem cells
    • Wu H, D'Alessio AC, Ito S, et al. Genome-wide analysis of 5-hydroxymethylcytosine distribution reveals its dual function in transcriptional regulation in mouse embryonic stem cells. Genes & development 2011; 25: 679-84.
    • (2011) Genes & development , vol.25 , pp. 679-684
    • Wu, H.1    D'Alessio, A.C.2    Ito, S.3
  • 51
    • 79959859654 scopus 로고    scopus 로고
    • Integrating 5-hydroxymethylcytosine into the epigenomic landscape of human embryonic stem cells
    • Szulwach KE, Li X, Li Y, et al. Integrating 5-hydroxymethylcytosine into the epigenomic landscape of human embryonic stem cells. PLoS genetics 2011; 7: e1002154.
    • (2011) PLoS genetics , vol.7
    • Szulwach, K.E.1    Li, X.2    Li, Y.3
  • 52
    • 79959209733 scopus 로고    scopus 로고
    • 5-Hydroxymethylcytosine is associated with enhancers and gene bodies in human embryonic stem cells
    • Stroud H, Feng S, Morey Kinney S, Pradhan S, Jacobsen SE. 5-Hydroxymethylcytosine is associated with enhancers and gene bodies in human embryonic stem cells. Genome biology 2011; 12: R54.
    • (2011) Genome biology , vol.12
    • Stroud, H.1    Feng, S.2    Morey Kinney, S.3    Pradhan, S.4    Jacobsen, S.E.5
  • 53
    • 79551587102 scopus 로고    scopus 로고
    • Tet1 and Tet2 regulate 5-hydroxymethylcytosine production and cell lineage specification in mouse embryonic stem cells
    • Koh KP, Yabuuchi A, Rao S, et al. Tet1 and Tet2 regulate 5-hydroxymethylcytosine production and cell lineage specification in mouse embryonic stem cells. Cell stem cell 2011; 8: 200-13.
    • (2011) Cell stem cell , vol.8 , pp. 200-213
    • Koh, K.P.1    Yabuuchi, A.2    Rao, S.3
  • 54
    • 79961139741 scopus 로고    scopus 로고
    • Tet1 is dispensable for maintaining pluripotency and its loss is compatible with embryonic and postnatal development
    • Dawlaty MM, Ganz K, Powell BE, et al. Tet1 is dispensable for maintaining pluripotency and its loss is compatible with embryonic and postnatal development. Cell stem cell 2011; 9: 166-75.
    • (2011) Cell stem cell , vol.9 , pp. 166-175
    • Dawlaty, M.M.1    Ganz, K.2    Powell, B.E.3
  • 55
    • 0037099537 scopus 로고    scopus 로고
    • LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23)
    • Ono R, Taki T, Taketani T, Taniwaki M, Kobayashi H, Hayashi Y. LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23). Cancer research 2002; 62: 4075-80.
    • (2002) Cancer research , vol.62 , pp. 4075-4080
    • Ono, R.1    Taki, T.2    Taketani, T.3    Taniwaki, M.4    Kobayashi, H.5    Hayashi, Y.6
  • 57
    • 78650175023 scopus 로고    scopus 로고
    • Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2
    • Ko M, Huang Y, Jankowska AM, et al. Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2. Nature 2010; 468: 839-43.
    • (2010) Nature , vol.468 , pp. 839-843
    • Ko, M.1    Huang, Y.2    Jankowska, A.M.3
  • 58
    • 80052303426 scopus 로고    scopus 로고
    • TET family proteins and their role in stem cell differentiation and transformation
    • Cimmino L, Abdel-Wahab O, Levine RL, Aifantis I. TET family proteins and their role in stem cell differentiation and transformation. Cell stem cell 2011; 9: 193-204.
    • (2011) Cell stem cell , vol.9 , pp. 193-204
    • Cimmino, L.1    Abdel-Wahab, O.2    Levine, R.L.3    Aifantis, I.4
  • 59
    • 84863393235 scopus 로고    scopus 로고
    • Loss of 5-hydroxymethylcytosine is accompanied with malignant cellular transformation
    • Kudo Y, Tateishi K, Yamamoto K, et al. Loss of 5-hydroxymethylcytosine is accompanied with malignant cellular transformation. Cancer science 2012; 103: 670-6.
    • (2012) Cancer science , vol.103 , pp. 670-676
    • Kudo, Y.1    Tateishi, K.2    Yamamoto, K.3
  • 60
    • 80054097425 scopus 로고    scopus 로고
    • Replication-dependent loss of 5-hydroxymethylcytosine in mouse preimplantation embryos
    • Inoue A, Zhang Y. Replication-dependent loss of 5-hydroxymethylcytosine in mouse preimplantation embryos. Science 2011; 334: 194.
    • (2011) Science , vol.334 , pp. 194
    • Inoue, A.1    Zhang, Y.2
  • 61
    • 80053348585 scopus 로고    scopus 로고
    • The role of Tet3 DNA dioxygenase in epigenetic reprogramming by oocytes
    • Gu TP, Guo F, Yang H, et al. The role of Tet3 DNA dioxygenase in epigenetic reprogramming by oocytes. Nature 2011; 477: 606-10.
    • (2011) Nature , vol.477 , pp. 606-610
    • Gu, T.P.1    Guo, F.2    Yang, H.3
  • 62
    • 79952713567 scopus 로고    scopus 로고
    • 5-Hydroxymethylcytosine in the mammalian zygote is linked with epigenetic reprogramming
    • Wossidlo M, Nakamura T, Lepikhov K, et al. 5-Hydroxymethylcytosine in the mammalian zygote is linked with epigenetic reprogramming. Nature communications 2011; 2: 241.
    • (2011) Nature communications , vol.2 , pp. 241
    • Wossidlo, M.1    Nakamura, T.2    Lepikhov, K.3
  • 64
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997; 389: 251-60.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 65
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger SL. The complex language of chromatin regulation during transcription. Nature 2007; 447: 407-12.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 66
    • 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
  • 68
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature 2000; 403: 41-5.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 71
    • 0037188911 scopus 로고    scopus 로고
    • Histone methylation: Dynamic or static?
    • Bannister AJ, Schneider R, Kouzarides T. Histone methylation: dynamic or static? Cell 2002; 109: 801-6.
    • (2002) Cell , vol.109 , pp. 801-806
    • Bannister, A.J.1    Schneider, R.2    Kouzarides, T.3
  • 72
    • 0031658303 scopus 로고    scopus 로고
    • Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae
    • Singer MS, Kahana A, Wolf AJ, et al. Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae. Genetics 1998; 150: 613-32.
    • (1998) Genetics , vol.150 , pp. 613-632
    • Singer, M.S.1    Kahana, A.2    Wolf, A.J.3
  • 73
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng Q, Wang H, Ng HH, et al. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Current biology: CB 2002; 12: 1052-8.
    • (2002) Current biology: CB , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3
  • 75
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F, Gafken PR, Gottschling DE. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 2002; 109: 745-56.
    • (2002) Cell , vol.109 , pp. 745-756
    • van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 76
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng HH, Feng Q, Wang H, et al. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes & development 2002; 16: 1518-27.
    • (2002) Genes & development , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3
  • 77
    • 79959960773 scopus 로고    scopus 로고
    • The diverse functions of Dot1 and H3K79 methylation
    • Nguyen AT, Zhang Y. The diverse functions of Dot1 and H3K79 methylation. Genes & development 2011; 25: 1345-58.
    • (2011) Genes & development , vol.25 , pp. 1345-1358
    • Nguyen, A.T.1    Zhang, Y.2
  • 78
    • 27844525514 scopus 로고    scopus 로고
    • Replication-independent histone deposition by the HIR complex and Asf1
    • Green EM, Antczak AJ, Bailey AO, et al. Replication-independent histone deposition by the HIR complex and Asf1. Current biology: CB 2005; 15: 2044-9.
    • (2005) Current biology: CB , vol.15 , pp. 2044-2049
    • Green, E.M.1    Antczak, A.J.2    Bailey, A.O.3
  • 79
    • 84862908952 scopus 로고    scopus 로고
    • The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity
    • Silva AC, Xu X, Kim HS, et al. The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity. Journal of biological chemistry 2012; 287: 1709-18.
    • (2012) Journal of biological chemistry , vol.287 , pp. 1709-1718
    • Silva, A.C.1    Xu, X.2    Kim, H.S.3
  • 81
    • 4444372638 scopus 로고    scopus 로고
    • Histone deimination antagonizes arginine methylation
    • Cuthbert GL, Daujat S, Snowden AW, et al. Histone deimination antagonizes arginine methylation. Cell 2004; 118: 545-53.
    • (2004) Cell , vol.118 , pp. 545-553
    • Cuthbert, G.L.1    Daujat, S.2    Snowden, A.W.3
  • 82
    • 5044228483 scopus 로고    scopus 로고
    • Human PAD4 regulates histone arginine methylation levels via demethylimination
    • Wang Y, Wysocka J, Sayegh J, et al. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 2004; 306: 279-83.
    • (2004) Science , vol.306 , pp. 279-283
    • Wang, Y.1    Wysocka, J.2    Sayegh, J.3
  • 83
    • 78049286684 scopus 로고    scopus 로고
    • Histone demethylases in development and disease
    • Pedersen MT, Helin K. Histone demethylases in development and disease. Trends in cell biology 2010; 20: 662-71.
    • (2010) Trends in cell biology , vol.20 , pp. 662-671
    • Pedersen, M.T.1    Helin, K.2
  • 84
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose RJ, Zhang Y. Regulation of histone methylation by demethylimination and demethylation. Nature reviews. Molecular cell biology 2007; 8: 307-18.
    • (2007) Nature reviews. Molecular cell biology , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 85
    • 66049096618 scopus 로고    scopus 로고
    • The basal initiation machinery: Beyond the general transcription factors
    • Sikorski TW, Buratowski S. The basal initiation machinery: beyond the general transcription factors. Current opinion in cell biology 2009; 21: 344-51.
    • (2009) Current opinion in cell biology , vol.21 , pp. 344-351
    • Sikorski, T.W.1    Buratowski, S.2
  • 87
    • 34848876313 scopus 로고    scopus 로고
    • Overlapping pathways dictate termination of RNA polymerase II transcription
    • Lykke-Andersen S, Jensen TH. Overlapping pathways dictate termination of RNA polymerase II transcription. Biochimie 2007; 89: 1177-82.
    • (2007) Biochimie , vol.89 , pp. 1177-1182
    • Lykke-Andersen, S.1    Jensen, T.H.2
  • 88
    • 70449641057 scopus 로고    scopus 로고
    • Progression through the RNA polymerase II CTD cycle
    • Buratowski S. Progression through the RNA polymerase II CTD cycle. Molecular cell 2009; 36: 541-6.
    • (2009) Molecular cell , vol.36 , pp. 541-546
    • Buratowski, S.1
  • 89
    • 0034307008 scopus 로고    scopus 로고
    • Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
    • Komarnitsky P, Cho EJ, Buratowski S. Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription. Genes & development 2000; 14: 2452-60.
    • (2000) Genes & development , vol.14 , pp. 2452-2460
    • Komarnitsky, P.1    Cho, E.J.2    Buratowski, S.3
  • 90
    • 0141557763 scopus 로고    scopus 로고
    • Bur1 kinase is required for efficient transcription elongation by RNA polymerase II
    • Keogh MC, Podolny V, Buratowski S. Bur1 kinase is required for efficient transcription elongation by RNA polymerase II. Molecular and cellular biology 2003; 23: 7005-18.
    • (2003) Molecular and cellular biology , vol.23 , pp. 7005-7018
    • Keogh, M.C.1    Podolny, V.2    Buratowski, S.3
  • 91
    • 0033600835 scopus 로고    scopus 로고
    • Yeast carboxyl-terminal domain kinase I positively and negatively regulates RNA polymerase II carboxyl-terminal domain phosphorylation
    • Patturajan M, Conrad NK, Bregman DB, Corden JL. Yeast carboxyl-terminal domain kinase I positively and negatively regulates RNA polymerase II carboxyl-terminal domain phosphorylation. The Journal of biological chemistry 1999; 274: 27823-8.
    • (1999) The Journal of biological chemistry , vol.274 , pp. 27823-27828
    • Patturajan, M.1    Conrad, N.K.2    Bregman, D.B.3    Corden, J.L.4
  • 92
    • 0038094496 scopus 로고    scopus 로고
    • Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II
    • Fabrega C, Shen V, Shuman S, Lima CD. Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II. Molecular cell 2003; 11: 1549-61.
    • (2003) Molecular cell , vol.11 , pp. 1549-1561
    • Fabrega, C.1    Shen, V.2    Shuman, S.3    Lima, C.D.4
  • 93
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng HH, Robert F, Young RA, Struhl K. Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Molecular cell 2003; 11: 709-19.
    • (2003) Molecular cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 94
    • 1542334001 scopus 로고    scopus 로고
    • Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing
    • Ahn SH, Kim M, Buratowski S. Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing. Molecular cell 2004; 13: 67-76.
    • (2004) Molecular cell , vol.13 , pp. 67-76
    • Ahn, S.H.1    Kim, M.2    Buratowski, S.3
  • 95
    • 1642441939 scopus 로고    scopus 로고
    • Coordination of transcription, RNA processing, and surveillance by P-TEFb kinase on heat shock genes
    • Ni Z, Schwartz BE, Werner J, Suarez JR, Lis JT. Coordination of transcription, RNA processing, and surveillance by P-TEFb kinase on heat shock genes. Molecular cell 2004; 13: 55-65.
    • (2004) Molecular cell , vol.13 , pp. 55-65
    • Ni, Z.1    Schwartz, B.E.2    Werner, J.3    Suarez, J.R.4    Lis, J.T.5
  • 96
    • 0037979272 scopus 로고    scopus 로고
    • Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II
    • Krogan NJ, Kim M, Tong A, et al. Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II. Molecular and cellular biology 2003; 23: 4207-18.
    • (2003) Molecular and cellular biology , vol.23 , pp. 4207-4218
    • Krogan, N.J.1    Kim, M.2    Tong, A.3
  • 97
    • 0038719825 scopus 로고    scopus 로고
    • The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation
    • Schaft D, Roguev A, Kotovic KM, et al. The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation. Nucleic acids research 2003; 31: 2475-82.
    • (2003) Nucleic acids research , vol.31 , pp. 2475-2482
    • Schaft, D.1    Roguev, A.2    Kotovic, K.M.3
  • 98
    • 0037336041 scopus 로고    scopus 로고
    • Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast
    • Xiao T, Hall H, Kizer KO, et al. Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast. Genes & development 2003; 17: 654-63.
    • (2003) Genes & development , vol.17 , pp. 654-663
    • Xiao, T.1    Hall, H.2    Kizer, K.O.3
  • 99
    • 0037512273 scopus 로고    scopus 로고
    • The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Li B, Howe L, Anderson S, Yates JR, 3rd, Workman JL. The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II. The Journal of biological chemistry 2003; 278: 8897-903.
    • (2003) The Journal of biological chemistry , vol.278 , pp. 8897-8903
    • Li, B.1    Howe, L.2    Anderson, S.3    Yates III, J.R.4    Workman, J.L.5
  • 100
    • 33751527233 scopus 로고    scopus 로고
    • Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
    • Taverna SD, Ilin S, Rogers RS, et al. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Molecular cell 2006; 24: 785-96.
    • (2006) Molecular cell , vol.24 , pp. 785-796
    • Taverna, S.D.1    Ilin, S.2    Rogers, R.S.3
  • 101
    • 33750328340 scopus 로고    scopus 로고
    • The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3
    • Martin DG, Baetz K, Shi X, et al. The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3. Molecular and cellular biology 2006; 26: 7871-9.
    • (2006) Molecular and cellular biology , vol.26 , pp. 7871-7879
    • Martin, D.G.1    Baetz, K.2    Shi, X.3
  • 102
    • 77955497472 scopus 로고    scopus 로고
    • Phosphorylated Pol II CTD recruits multiple HDACs, including Rpd3C(S), for methylationdependent deacetylation of ORF nucleosomes
    • Govind CK, Qiu H, Ginsburg DS, et al. Phosphorylated Pol II CTD recruits multiple HDACs, including Rpd3C(S), for methylationdependent deacetylation of ORF nucleosomes. Molecular cell 2010; 39: 234-46.
    • (2010) Molecular cell , vol.39 , pp. 234-246
    • Govind, C.K.1    Qiu, H.2    Ginsburg, D.S.3
  • 103
    • 64249111489 scopus 로고    scopus 로고
    • Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5' transcribed regions
    • Kim T, Buratowski S. Dimethylation of H3K4 by Set1 recruits the Set3 histone deacetylase complex to 5' transcribed regions. Cell 2009; 137: 259-72.
    • (2009) Cell , vol.137 , pp. 259-272
    • Kim, T.1    Buratowski, S.2
  • 104
    • 65549095078 scopus 로고    scopus 로고
    • Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription
    • Li B, Jackson J, Simon MD, et al. Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription. The Journal of biological chemistry 2009; 284: 7970-6.
    • (2009) The Journal of biological chemistry , vol.284 , pp. 7970-7976
    • Li, B.1    Jackson, J.2    Simon, M.D.3
  • 105
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
    • Li B, Gogol M, Carey M, Lee D, Seidel C, Workman JL. Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin. Science 2007; 316: 1050-4.
    • (2007) Science , vol.316 , pp. 1050-1054
    • Li, B.1    Gogol, M.2    Carey, M.3    Lee, D.4    Seidel, C.5    Workman, J.L.6
  • 106
    • 27744587302 scopus 로고    scopus 로고
    • Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex
    • Keogh MC, Kurdistani SK, Morris SA, et al. Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. Cell 2005; 123: 593-605.
    • (2005) Cell , vol.123 , pp. 593-605
    • Keogh, M.C.1    Kurdistani, S.K.2    Morris, S.A.3
  • 107
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • Carrozza MJ, Li B, Florens L, et al. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Cell 2005; 123: 581-92.
    • (2005) Cell , vol.123 , pp. 581-592
    • Carrozza, M.J.1    Li, B.2    Florens, L.3
  • 108
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: Intricacy of writing and reading a single epigenetic mark
    • Ruthenburg AJ, Allis CD, Wysocka J. Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Molecular cell 2007; 25: 15-30.
    • (2007) Molecular cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 109
    • 44649139771 scopus 로고    scopus 로고
    • Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation
    • Shilatifard A. Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation. Current opinion in cell biology 2008; 20: 341-8.
    • (2008) Current opinion in cell biology , vol.20 , pp. 341-348
    • Shilatifard, A.1
  • 112
    • 60149091656 scopus 로고    scopus 로고
    • ChIP-seq accurately predicts tissuespecific activity of enhancers
    • Visel A, Blow MJ, Li Z, et al. ChIP-seq accurately predicts tissuespecific activity of enhancers. Nature 2009; 457: 854-8.
    • (2009) Nature , vol.457 , pp. 854-858
    • Visel, A.1    Blow, M.J.2    Li, Z.3
  • 113
    • 33847334699 scopus 로고    scopus 로고
    • Distinct and predictive chromatin signatures of transcriptional promoters and enhancers in the human genome
    • Heintzman ND, Stuart RK, Hon G, et al. Distinct and predictive chromatin signatures of transcriptional promoters and enhancers in the human genome. Nature genetics 2007; 39: 311-8.
    • (2007) Nature genetics , vol.39 , pp. 311-318
    • Heintzman, N.D.1    Stuart, R.K.2    Hon, G.3
  • 114
    • 23944462969 scopus 로고    scopus 로고
    • Genome-wide map of nucleosome acetylation and methylation in yeast
    • Pokholok DK, Harbison CT, Levine S, et al. Genome-wide map of nucleosome acetylation and methylation in yeast. Cell 2005; 122: 517-27.
    • (2005) Cell , vol.122 , pp. 517-527
    • Pokholok, D.K.1    Harbison, C.T.2    Levine, S.3
  • 115
    • 26444508841 scopus 로고    scopus 로고
    • Single-nucleosome mapping of histone modifications in S. cerevisiae
    • Liu CL, Kaplan T, Kim M, et al. Single-nucleosome mapping of histone modifications in S. cerevisiae. PLoS biology 2005; 3: e328.
    • (2005) PLoS biology , vol.3
    • Liu, C.L.1    Kaplan, T.2    Kim, M.3
  • 116
    • 70449099301 scopus 로고    scopus 로고
    • Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain
    • Otani J, Nankumo T, Arita K, Inamoto S, Ariyoshi M, Shirakawa M. Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain. EMBO reports 2009; 10: 1235-41.
    • (2009) EMBO reports , vol.10 , pp. 1235-1241
    • Otani, J.1    Nankumo, T.2    Arita, K.3    Inamoto, S.4    Ariyoshi, M.5    Shirakawa, M.6
  • 117
    • 34547725157 scopus 로고    scopus 로고
    • DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
    • Ooi SK, Qiu C, Bernstein E, et al. DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA. Nature 2007; 448: 714-7.
    • (2007) Nature , vol.448 , pp. 714-717
    • Ooi, S.K.1    Qiu, C.2    Bernstein, E.3
  • 119
    • 49649125042 scopus 로고    scopus 로고
    • Genome-scale DNA methylation maps of pluripotent and differentiated cells
    • Meissner A, Mikkelsen TS, Gu H, et al. Genome-scale DNA methylation maps of pluripotent and differentiated cells. Nature 2008; 454: 766-70.
    • (2008) Nature , vol.454 , pp. 766-770
    • Meissner, A.1    Mikkelsen, T.S.2    Gu, H.3
  • 120
    • 34047116826 scopus 로고    scopus 로고
    • Distribution, silencing potential and evolutionary impact of promoter DNA methylation in the human genome
    • Weber M, Hellmann I, Stadler MB, et al. Distribution, silencing potential and evolutionary impact of promoter DNA methylation in the human genome. Nature genetics 2007; 39: 457-66.
    • (2007) Nature genetics , vol.39 , pp. 457-466
    • Weber, M.1    Hellmann, I.2    Stadler, M.B.3
  • 121
    • 33947245128 scopus 로고    scopus 로고
    • RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3
    • Christensen J, Agger K, Cloos PA, et al. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell 2007; 128: 1063-76.
    • (2007) Cell , vol.128 , pp. 1063-1076
    • Christensen, J.1    Agger, K.2    Cloos, P.A.3
  • 122
    • 78049518884 scopus 로고    scopus 로고
    • Prognostic relevance of global histone H3 lysine 4 (H3K4) methylation in renal cell carcinoma. International journal of cancer
    • Ellinger J, Kahl P, Mertens C, et al. Prognostic relevance of global histone H3 lysine 4 (H3K4) methylation in renal cell carcinoma. International journal of cancer. Journal international du cancer 2010; 127: 2360-6.
    • (2010) Journal international du cancer , vol.127 , pp. 2360-2366
    • Ellinger, J.1    Kahl, P.2    Mertens, C.3
  • 124
    • 65949086183 scopus 로고    scopus 로고
    • Global histone modifications in breast cancer correlate with tumor phenotypes, prognostic factors, and patient outcome
    • Elsheikh SE, Green AR, Rakha EA, et al. Global histone modifications in breast cancer correlate with tumor phenotypes, prognostic factors, and patient outcome. Cancer research 2009; 69: 3802-9.
    • (2009) Cancer research , vol.69 , pp. 3802-3809
    • Elsheikh, S.E.1    Green, A.R.2    Rakha, E.A.3
  • 126
    • 21744457108 scopus 로고    scopus 로고
    • Global histone modification patterns predict risk of prostate cancer recurrence
    • Seligson DB, Horvath S, Shi T, et al. Global histone modification patterns predict risk of prostate cancer recurrence. Nature 2005; 435: 1262-6.
    • (2005) Nature , vol.435 , pp. 1262-1266
    • Seligson, D.B.1    Horvath, S.2    Shi, T.3
  • 127
    • 35548934558 scopus 로고    scopus 로고
    • MLL translocations, histone modifications and leukaemia stem-cell development
    • Krivtsov AV, Armstrong SA. MLL translocations, histone modifications and leukaemia stem-cell development. Nature reviews. Cancer 2007; 7: 823-33.
    • (2007) Nature reviews. Cancer , vol.7 , pp. 823-833
    • Krivtsov, A.V.1    Armstrong, S.A.2
  • 129
    • 78649815150 scopus 로고    scopus 로고
    • Overexpression of LSD1 contributes to human carcinogenesis through chromatin regulation in various cancers. International journal of cancer
    • Hayami S, Kelly JD, Cho HS, et al. Overexpression of LSD1 contributes to human carcinogenesis through chromatin regulation in various cancers. International journal of cancer. Journal international du cancer 2011; 128: 574-86.
    • (2011) Journal international du cancer , vol.128 , pp. 574-586
    • Hayami, S.1    Kelly, J.D.2    Cho, H.S.3
  • 130
    • 62449197931 scopus 로고    scopus 로고
    • Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: Implications for therapy
    • Schulte JH, Lim S, Schramm A, et al. Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: implications for therapy. Cancer research 2009; 69: 2065-71.
    • (2009) Cancer research , vol.69 , pp. 2065-2071
    • Schulte, J.H.1    Lim, S.2    Schramm, A.3
  • 131
    • 38549139593 scopus 로고    scopus 로고
    • Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
    • Edmunds JW, Mahadevan LC, Clayton AL. Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. The EMBO journal 2008; 27: 406-20.
    • (2008) The EMBO journal , vol.27 , pp. 406-420
    • Edmunds, J.W.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 132
    • 0034917123 scopus 로고    scopus 로고
    • Identification of the full-length huntingtin-interacting protein p231HBP/HYPB as a DNA-binding factor
    • Rega S, Stiewe T, Chang DI, et al. Identification of the full-length huntingtin-interacting protein p231HBP/HYPB as a DNA-binding factor. Molecular and cellular neurosciences 2001; 18: 68-79.
    • (2001) Molecular and cellular neurosciences , vol.18 , pp. 68-79
    • Rega, S.1    Stiewe, T.2    Chang, D.I.3
  • 134
    • 13144302844 scopus 로고    scopus 로고
    • Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning
    • Mao M, Fu G, Wu JS, et al. Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proceedings of the National Academy of Sciences of the United States of America 1998; 95: 8175-80.
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , pp. 8175-8180
    • Mao, M.1    Fu, G.2    Wu, J.S.3
  • 136
    • 0037599617 scopus 로고    scopus 로고
    • NSD1 is essential for early post-implantation development and has a catalytically active SET domain
    • Rayasam GV, Wendling O, Angrand PO, et al. NSD1 is essential for early post-implantation development and has a catalytically active SET domain. The EMBO journal 2003; 22: 3153-63.
    • (2003) The EMBO journal , vol.22 , pp. 3153-3163
    • Rayasam, G.V.1    Wendling, O.2    Angrand, P.O.3
  • 137
    • 37149047905 scopus 로고    scopus 로고
    • Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in Drosophila
    • Bell O, Wirbelauer C, Hild M, et al. Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in Drosophila. The EMBO journal 2007; 26: 4974-84.
    • (2007) The EMBO journal , vol.26 , pp. 4974-4984
    • Bell, O.1    Wirbelauer, C.2    Hild, M.3
  • 139
    • 71749121455 scopus 로고    scopus 로고
    • The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate
    • Li Y, Trojer P, Xu CF, et al. The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate. The Journal of biological chemistry 2009; 284: 34283-95.
    • (2009) The Journal of biological chemistry , vol.284 , pp. 34283-34295
    • Li, Y.1    Trojer, P.2    Xu, C.F.3
  • 140
    • 70049111751 scopus 로고    scopus 로고
    • The mRNA expression of SETD2 in human breast cancer: Correlation with clinico-pathological parameters
    • Al Sarakbi W, Sasi W, Jiang WG, Roberts T, Newbold RF, Mokbel K. The mRNA expression of SETD2 in human breast cancer: correlation with clinico-pathological parameters. BMC cancer 2009; 9: 290.
    • (2009) BMC cancer , vol.9 , pp. 290
    • Al Sarakbi, W.1    Sasi, W.2    Jiang, W.G.3    Roberts, T.4    Newbold, R.F.5    Mokbel, K.6
  • 141
    • 77953170322 scopus 로고    scopus 로고
    • Histone methyltransferase gene SETD2 is a novel tumor suppressor gene in clear cell renal cell carcinoma
    • Duns G, van den Berg E, van Duivenbode I, et al. Histone methyltransferase gene SETD2 is a novel tumor suppressor gene in clear cell renal cell carcinoma. Cancer research 2010; 70: 4287-91.
    • (2010) Cancer research , vol.70 , pp. 4287-4291
    • Duns, G.1    van den Berg, E.2    van Duivenbode, I.3
  • 142
    • 34347392874 scopus 로고    scopus 로고
    • NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis
    • Wang GG, Cai L, Pasillas MP, Kamps MP. NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis. Nature cell biology 2007; 9: 804-12.
    • (2007) Nature cell biology , vol.9 , pp. 804-812
    • Wang, G.G.1    Cai, L.2    Pasillas, M.P.3    Kamps, M.P.4
  • 143
    • 64549093255 scopus 로고    scopus 로고
    • A clinical study of Sotos syndrome patients with review of the literature
    • Leventopoulos G, Kitsiou-Tzeli S, Kritikos K, et al. A clinical study of Sotos syndrome patients with review of the literature. Pediatric neurology 2009; 40: 357-64.
    • (2009) Pediatric neurology , vol.40 , pp. 357-364
    • Leventopoulos, G.1    Kitsiou-Tzeli, S.2    Kritikos, K.3
  • 144
    • 18544384537 scopus 로고    scopus 로고
    • Haploinsufficiency of NSD1 causes Sotos syndrome
    • Kurotaki N, Imaizumi K, Harada N, et al. Haploinsufficiency of NSD1 causes Sotos syndrome. Nature genetics 2002; 30: 365-6.
    • (2002) Nature genetics , vol.30 , pp. 365-366
    • Kurotaki, N.1    Imaizumi, K.2    Harada, N.3
  • 145
    • 15444373985 scopus 로고    scopus 로고
    • The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1
    • Giannattasio M, Lazzaro F, Plevani P, Muzi-Falconi M. The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1. The Journal of biological chemistry 2005; 280: 9879-86.
    • (2005) The Journal of biological chemistry , vol.280 , pp. 9879-9886
    • Giannattasio, M.1    Lazzaro, F.2    Plevani, P.3    Muzi-Falconi, M.4
  • 146
    • 0033786367 scopus 로고    scopus 로고
    • Role for the silencing protein Dot1 in meiotic checkpoint control
    • San-Segundo PA, Roeder GS. Role for the silencing protein Dot1 in meiotic checkpoint control. Molecular biology of the cell 2000; 11: 3601-15.
    • (2000) Molecular biology of the cell , vol.11 , pp. 3601-3615
    • San-Segundo, P.A.1    Roeder, G.S.2
  • 147
    • 25444466892 scopus 로고    scopus 로고
    • Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9
    • Wysocki R, Javaheri A, Allard S, Sha F, Cote J, Kron SJ. Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Molecular and cellular biology 2005; 25: 8430-43.
    • (2005) Molecular and cellular biology , vol.25 , pp. 8430-8443
    • Wysocki, R.1    Javaheri, A.2    Allard, S.3    Sha, F.4    Cote, J.5    Kron, S.J.6
  • 148
    • 69749117490 scopus 로고    scopus 로고
    • Linking cell cycle to histone modifications: SBF and H2B monoubiquitination machinery and cell-cycle regulation of H3K79 dimethylation
    • Schulze JM, Jackson J, Nakanishi S, et al. Linking cell cycle to histone modifications: SBF and H2B monoubiquitination machinery and cell-cycle regulation of H3K79 dimethylation. Molecular cell 2009; 35: 626-41.
    • (2009) Molecular cell , vol.35 , pp. 626-641
    • Schulze, J.M.1    Jackson, J.2    Nakanishi, S.3
  • 149
    • 42149146774 scopus 로고    scopus 로고
    • DOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cells
    • Steger DJ, Lefterova MI, Ying L, et al. DOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cells. Molecular and cellular biology 2008; 28: 2825-39.
    • (2008) Molecular and cellular biology , vol.28 , pp. 2825-2839
    • Steger, D.J.1    Lefterova, M.I.2    Ying, L.3
  • 150
    • 2642570305 scopus 로고    scopus 로고
    • The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
    • Schubeler D, MacAlpine DM, Scalzo D, et al. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes & development 2004; 18: 1263-71.
    • (2004) Genes & development , vol.18 , pp. 1263-1271
    • Schubeler, D.1    MacAlpine, D.M.2    Scalzo, D.3
  • 151
    • 44849112242 scopus 로고    scopus 로고
    • Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states
    • Frederiks F, Tzouros M, Oudgenoeg G, et al. Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states. Nature structural & molecular biology 2008; 15: 550-7.
    • (2008) Nature structural & molecular biology , vol.15 , pp. 550-557
    • Frederiks, F.1    Tzouros, M.2    Oudgenoeg, G.3
  • 152
    • 0344837759 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
    • Min J, Feng Q, Li Z, Zhang Y, Xu RM. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 2003; 112: 711-23.
    • (2003) Cell , vol.112 , pp. 711-723
    • Min, J.1    Feng, Q.2    Li, Z.3    Zhang, Y.4    Xu, R.M.5
  • 153
    • 52949107241 scopus 로고    scopus 로고
    • The histone H3K79 methyltransferase Dot1L is essential for mammalian development and heterochromatin structure
    • Jones B, Su H, Bhat A, et al. The histone H3K79 methyltransferase Dot1L is essential for mammalian development and heterochromatin structure. PLoS genetics 2008; 4: e1000190.
    • (2008) PLoS genetics , vol.4
    • Jones, B.1    Su, H.2    Bhat, A.3
  • 154
    • 13744259076 scopus 로고    scopus 로고
    • Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase
    • Shanower GA, Muller M, Blanton JL, Honti V, Gyurkovics H, Schedl P. Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase. Genetics 2005; 169: 173-84.
    • (2005) Genetics , vol.169 , pp. 173-184
    • Shanower, G.A.1    Muller, M.2    Blanton, J.L.3    Honti, V.4    Gyurkovics, H.5    Schedl, P.6
  • 156
    • 1242269799 scopus 로고    scopus 로고
    • Structure and regulation of the mDot1 gene, a mouse histone H3 methyltransferase
    • Zhang W, Hayashizaki Y, Kone BC. Structure and regulation of the mDot1 gene, a mouse histone H3 methyltransferase. The Biochemical journal 2004; 377: 641-51.
    • (2004) The Biochemical journal , vol.377 , pp. 641-651
    • Zhang, W.1    Hayashizaki, Y.2    Kone, B.C.3
  • 157
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng HH, Xu RM, Zhang Y, Struhl K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. The Journal of biological chemistry 2002; 277: 34655-7.
    • (2002) The Journal of biological chemistry , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 158
    • 0036682364 scopus 로고    scopus 로고
    • Gene silencing: Trans-histone regulatory pathway in chromatin
    • Briggs SD, Xiao T, Sun ZW, et al. Gene silencing: trans-histone regulatory pathway in chromatin. Nature 2002; 418: 498.
    • (2002) Nature , vol.418 , pp. 498
    • Briggs, S.D.1    Xiao, T.2    Sun, Z.W.3
  • 159
    • 0037248944 scopus 로고    scopus 로고
    • Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter
    • Wood A, Krogan NJ, Dover J, et al. Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter. Molecular cell 2003; 11: 267-74.
    • (2003) Molecular cell , vol.11 , pp. 267-274
    • Wood, A.1    Krogan, N.J.2    Dover, J.3
  • 160
    • 22544461653 scopus 로고    scopus 로고
    • Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1
    • Shahbazian MD, Zhang K, Grunstein M. Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1. Molecular cell 2005; 19: 271-7.
    • (2005) Molecular cell , vol.19 , pp. 271-277
    • Shahbazian, M.D.1    Zhang, K.2    Grunstein, M.3
  • 161
    • 13444292904 scopus 로고    scopus 로고
    • Histone modifications defining active genes persist after transcriptional and mitotic inactivation
    • Kouskouti A, Talianidis I. Histone modifications defining active genes persist after transcriptional and mitotic inactivation. The EMBO journal 2005; 24: 347-57.
    • (2005) The EMBO journal , vol.24 , pp. 347-357
    • Kouskouti, A.1    Talianidis, I.2
  • 162
    • 0037524702 scopus 로고    scopus 로고
    • The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation
    • Krogan NJ, Dover J, Wood A, et al. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Molecular cell 2003; 11: 721-9.
    • (2003) Molecular cell , vol.11 , pp. 721-729
    • Krogan, N.J.1    Dover, J.2    Wood, A.3
  • 163
    • 77949563562 scopus 로고    scopus 로고
    • Targeting DOT1L action and interactions in leukemia: The role of DOT1L in transformation and development
    • Barry ER, Corry GN, Rasmussen TP. Targeting DOT1L action and interactions in leukemia: the role of DOT1L in transformation and development. Expert opinion on therapeutic targets 2010; 14: 405-18.
    • (2010) Expert opinion on therapeutic targets , vol.14 , pp. 405-418
    • Barry, E.R.1    Corry, G.N.2    Rasmussen, T.P.3
  • 164
    • 78651463452 scopus 로고    scopus 로고
    • Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of alpha-ketoglutarate-dependent dioxygenases
    • Xu W, Yang H, Liu Y, et al. Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of alpha-ketoglutarate-dependent dioxygenases. Cancer cell 2011; 19: 17-30.
    • (2011) Cancer cell , vol.19 , pp. 17-30
    • Xu, W.1    Yang, H.2    Liu, Y.3
  • 165
  • 166
    • 0345275880 scopus 로고    scopus 로고
    • Inactivation of a histone methyltransferase by mutations in human cancers
    • Kim KC, Geng L, Huang S. Inactivation of a histone methyltransferase by mutations in human cancers. Cancer research 2003; 63: 7619-23.
    • (2003) Cancer research , vol.63 , pp. 7619-7623
    • Kim, K.C.1    Geng, L.2    Huang, S.3
  • 167
    • 2342505217 scopus 로고    scopus 로고
    • Differential histone H3 Lys-9 and Lys-27 methylation profiles on the X chromosome
    • Rougeulle C, Chaumeil J, Sarma K, et al. Differential histone H3 Lys-9 and Lys-27 methylation profiles on the X chromosome. Molecular and cellular biology 2004; 24: 5475-84.
    • (2004) Molecular and cellular biology , vol.24 , pp. 5475-5484
    • Rougeulle, C.1    Chaumeil, J.2    Sarma, K.3
  • 168
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison C, Bailly D, Peters AH, et al. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nature genetics 2002; 30: 329-34.
    • (2002) Nature genetics , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3
  • 169
    • 0037022129 scopus 로고    scopus 로고
    • Histone H3 lysine 9 methylation occurs rapidly at the onset of random X chromosome inactivation
    • Mermoud JE, Popova B, Peters AH, Jenuwein T, Brockdorff N. Histone H3 lysine 9 methylation occurs rapidly at the onset of random X chromosome inactivation. Current biology: CB 2002; 12: 247-51.
    • (2002) Current biology: CB , vol.12 , pp. 247-251
    • Mermoud, J.E.1    Popova, B.2    Peters, A.H.3    Jenuwein, T.4    Brockdorff, N.5
  • 170
    • 0036338205 scopus 로고    scopus 로고
    • Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin
    • Peters AH, Mermoud JE, O'Carroll D, et al. Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin. Nature genetics 2002; 30: 77-80.
    • (2002) Nature genetics , vol.30 , pp. 77-80
    • Peters, A.H.1    Mermoud, J.E.2    O'Carroll, D.3
  • 171
    • 0036337759 scopus 로고    scopus 로고
    • Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes
    • Boggs BA, Cheung P, Heard E, Spector DL, Chinault AC, Allis CD. Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes. Nature genetics 2002; 30: 73-6.
    • (2002) Nature genetics , vol.30 , pp. 73-76
    • Boggs, B.A.1    Cheung, P.2    Heard, E.3    Spector, D.L.4    Chinault, A.C.5    Allis, C.D.6
  • 172
    • 0035839110 scopus 로고    scopus 로고
    • Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries
    • Noma K, Allis CD, Grewal SI. Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries. Science 2001; 293: 1150-5.
    • (2001) Science , vol.293 , pp. 1150-1155
    • Noma, K.1    Allis, C.D.2    Grewal, S.I.3
  • 173
    • 0035964869 scopus 로고    scopus 로고
    • Correlation between histone lysine methylation and developmental changes at the chicken beta-globin locus
    • Litt MD, Simpson M, Gaszner M, Allis CD, Felsenfeld G. Correlation between histone lysine methylation and developmental changes at the chicken beta-globin locus. Science 2001; 293: 2453-5.
    • (2001) Science , vol.293 , pp. 2453-2455
    • Litt, M.D.1    Simpson, M.2    Gaszner, M.3    Allis, C.D.4    Felsenfeld, G.5
  • 174
    • 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, et al. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes & development 2005; 19: 815-26.
    • (2005) Genes & development , vol.19 , pp. 815-826
    • Tachibana, M.1    Ueda, J.2    Fukuda, M.3
  • 175
    • 9144268924 scopus 로고    scopus 로고
    • Partitioning and plasticity of repressive histone methylation states in mammalian chromatin
    • Peters AH, Kubicek S, Mechtler K, et al. Partitioning and plasticity of repressive histone methylation states in mammalian chromatin. Molecular cell 2003; 12: 1577-89.
    • (2003) Molecular cell , vol.12 , pp. 1577-1589
    • Peters, A.H.1    Kubicek, S.2    Mechtler, K.3
  • 176
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, Eisenhaber F, O'Carroll D, et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 2000; 406: 593-9.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3
  • 177
    • 0242412194 scopus 로고    scopus 로고
    • Human heterochromatin protein 1 isoforms HP1(Hsalpha) and HP1(Hsbeta) interfere with hTERT-telomere interactions and correlate with changes in cell growth and response to ionizing radiation
    • Sharma GG, Hwang KK, Pandita RK, et al. Human heterochromatin protein 1 isoforms HP1(Hsalpha) and HP1(Hsbeta) interfere with hTERT-telomere interactions and correlate with changes in cell growth and response to ionizing radiation. Molecular and cellular biology 2003; 23: 8363-76.
    • (2003) Molecular and cellular biology , vol.23 , pp. 8363-8376
    • Sharma, G.G.1    Hwang, K.K.2    Pandita, R.K.3
  • 178
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard L, Laible G, Selenko P, et al. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. The EMBO journal 1999; 18: 1923-38.
    • (1999) The EMBO journal , vol.18 , pp. 1923-1938
    • Aagaard, L.1    Laible, G.2    Selenko, P.3
  • 179
    • 0017247814 scopus 로고
    • Biological and clinical significance of differences between RBC membrane (Rh) and non membrane (ABH, MN, P) antigenic sites
    • Moore BP. Biological and clinical significance of differences between RBC membrane (Rh) and non membrane (ABH, MN, P) antigenic sites. Revue francaise de transfusion et immunohematologie 1976; 19: 629-30.
    • (1976) Revue francaise de transfusion et immunohematologie , vol.19 , pp. 629-630
    • Moore, B.P.1
  • 180
    • 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, et al. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes & development 2002; 16: 1779-91.
    • (2002) Genes & development , vol.16 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3
  • 181
    • 54349114603 scopus 로고    scopus 로고
    • DNA methylation in ES cells requires the lysine methyltransferase G9a but not its catalytic activity
    • Dong KB, Maksakova IA, Mohn F, et al. DNA methylation in ES cells requires the lysine methyltransferase G9a but not its catalytic activity. The EMBO journal 2008; 27: 2691-701.
    • (2008) The EMBO journal , vol.27 , pp. 2691-2701
    • Dong, K.B.1    Maksakova, I.A.2    Mohn, F.3
  • 182
    • 44249128891 scopus 로고    scopus 로고
    • Downregulation of histone H3 lysine 9 methyltransferase G9a induces centrosome disruption and chromosome instability in cancer cells
    • Kondo Y, Shen L, Ahmed S, Boumber Y, Sekido Y, Haddad BR, Issa JP. Downregulation of histone H3 lysine 9 methyltransferase G9a induces centrosome disruption and chromosome instability in cancer cells. PloS one 2008; 3: e2037.
    • (2008) PloS one , vol.3
    • Kondo, Y.1    Shen, L.2    Ahmed, S.3    Boumber, Y.4    Sekido, Y.5    Haddad, B.R.6    Issa, J.P.7
  • 183
    • 77952488976 scopus 로고    scopus 로고
    • Structural biology of human H3K9 methyltransferases
    • Wu H, Min J, Lunin VV, et al. Structural biology of human H3K9 methyltransferases. PloS one 2010; 5: e8570.
    • (2010) PloS one , vol.5
    • Wu, H.1    Min, J.2    Lunin, V.V.3
  • 184
    • 43749093216 scopus 로고    scopus 로고
    • Protein lysine methyltransferase G9a acts on non-histone targets
    • Rathert P, Dhayalan A, Murakami M, et al. Protein lysine methyltransferase G9a acts on non-histone targets. Nature chemical biology 2008; 4: 344-6.
    • (2008) Nature chemical biology , vol.4 , pp. 344-346
    • Rathert, P.1    Dhayalan, A.2    Murakami, M.3
  • 185
    • 25444471273 scopus 로고    scopus 로고
    • Sequence specificity and role of proximal amino acids of the histone H3 tail on catalysis of murine G9A lysine 9 histone H3 methyltransferase
    • Chin HG, Pradhan M, Esteve PO, Patnaik D, Evans TC, Jr., Pradhan S. Sequence specificity and role of proximal amino acids of the histone H3 tail on catalysis of murine G9A lysine 9 histone H3 methyltransferase. Biochemistry 2005; 44: 12998-3006.
    • (2005) Biochemistry , vol.44 , pp. 12998-13006
    • Chin, H.G.1    Pradhan, M.2    Esteve, P.O.3    Patnaik, D.4    Evans Jr., T.C.5    Pradhan, S.6
  • 186
    • 74049135429 scopus 로고    scopus 로고
    • A subset of the histone H3 lysine 9 methyltransferases Suv39h1, G9a, GLP, and SETDB1 participate in a multimeric complex
    • Fritsch L, Robin P, Mathieu JR, et al. A subset of the histone H3 lysine 9 methyltransferases Suv39h1, G9a, GLP, and SETDB1 participate in a multimeric complex. Molecular cell 2010; 37: 46-56.
    • (2010) Molecular cell , vol.37 , pp. 46-56
    • Fritsch, L.1    Robin, P.2    Mathieu, J.R.3
  • 187
    • 33745999467 scopus 로고    scopus 로고
    • Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP
    • Ueda J, Tachibana M, Ikura T, Shinkai Y. Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP. The Journal of biological chemistry 2006; 281: 20120-8.
    • (2006) The Journal of biological chemistry , vol.281 , pp. 20120-20128
    • Ueda, J.1    Tachibana, M.2    Ikura, T.3    Shinkai, Y.4
  • 188
    • 0141992115 scopus 로고    scopus 로고
    • mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression
    • Wang H, An W, Cao R, et al. mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Molecular cell 2003; 12: 475-87.
    • (2003) Molecular cell , vol.12 , pp. 475-487
    • Wang, H.1    An, W.2    Cao, R.3
  • 189
    • 33745811234 scopus 로고    scopus 로고
    • The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells
    • Li H, Rauch T, Chen ZX, Szabo PE, Riggs AD, Pfeifer GP. The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells. The Journal of biological chemistry 2006; 281: 19489-500.
    • (2006) The Journal of biological chemistry , vol.281 , pp. 19489-19500
    • Li, H.1    Rauch, T.2    Chen, Z.X.3    Szabo, P.E.4    Riggs, A.D.5    Pfeifer, G.P.6
  • 190
    • 34347353316 scopus 로고    scopus 로고
    • Genome-wide analysis of KAP1 binding suggests autoregulation of KRAB-ZNFs
    • O'Geen H, Squazzo SL, Iyengar S, et al. Genome-wide analysis of KAP1 binding suggests autoregulation of KRAB-ZNFs. PLoS genetics 2007; 3: e89.
    • (2007) PLoS genetics , vol.3
    • O'Geen, H.1    Squazzo, S.L.2    Iyengar, S.3
  • 191
    • 33751007001 scopus 로고    scopus 로고
    • The KAP1 corepressor functions to coordinate the assembly of de novo HP1-demarcated microenvironments of heterochromatin required for KRAB zinc finger protein-mediated transcriptional repression
    • Sripathy SP, Stevens J, Schultz DC. The KAP1 corepressor functions to coordinate the assembly of de novo HP1-demarcated microenvironments of heterochromatin required for KRAB zinc finger protein-mediated transcriptional repression. Molecular and cellular biology 2006; 26: 8623-38.
    • (2006) Molecular and cellular biology , vol.26 , pp. 8623-8638
    • Sripathy, S.P.1    Stevens, J.2    Schultz, D.C.3
  • 192
    • 35748960839 scopus 로고    scopus 로고
    • A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-gamma transactivation
    • Takada I, Mihara M, Suzawa M, et al. A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-gamma transactivation. Nature cell biology 2007; 9: 1273-85.
    • (2007) Nature cell biology , vol.9 , pp. 1273-1285
    • Takada, I.1    Mihara, M.2    Suzawa, M.3
  • 194
    • 67650096728 scopus 로고    scopus 로고
    • The HP1alpha-CAF1-SetDB1-containing complex provides H3K9me1 for Suv39-mediated K9me3 in pericentric heterochromatin
    • Loyola A, Tagami H, Bonaldi T, et al. The HP1alpha-CAF1-SetDB1-containing complex provides H3K9me1 for Suv39-mediated K9me3 in pericentric heterochromatin. EMBO reports 2009; 10: 769-75.
    • (2009) EMBO reports , vol.10 , pp. 769-775
    • Loyola, A.1    Tagami, H.2    Bonaldi, T.3
  • 195
    • 67650270690 scopus 로고    scopus 로고
    • Multiple SET methyltransferases are required to maintain normal heterochromatin domains in the genome of Drosophila melanogaster
    • Brower-Toland B, Riddle NC, Jiang H, Huisinga KL, Elgin SC. Multiple SET methyltransferases are required to maintain normal heterochromatin domains in the genome of Drosophila melanogaster. Genetics 2009; 181: 1303-19.
    • (2009) Genetics , vol.181 , pp. 1303-1319
    • Brower-Toland, B.1    Riddle, N.C.2    Jiang, H.3    Huisinga, K.L.4    Elgin, S.C.5
  • 196
    • 48249117935 scopus 로고    scopus 로고
    • dSETDB1 and SU(VAR)3-9 sequentially function during germline-stem cell differentiation in Drosophila melanogaster
    • Yoon J, Lee KS, Park JS, Yu K, Paik SG, Kang YK. dSETDB1 and SU(VAR)3-9 sequentially function during germline-stem cell differentiation in Drosophila melanogaster. PloS one 2008; 3: e2234.
    • (2008) PloS one , vol.3
    • Yoon, J.1    Lee, K.S.2    Park, J.S.3    Yu, K.4    Paik, S.G.5    Kang, Y.K.6
  • 197
    • 44849113182 scopus 로고    scopus 로고
    • Monoallele deletion of CBP leads to pericentromeric heterochromatin condensation through ESET expression and histone H3 (K9) methylation
    • Lee J, Hagerty S, Cormier KA, et al. Monoallele deletion of CBP leads to pericentromeric heterochromatin condensation through ESET expression and histone H3 (K9) methylation. Human molecular genetics 2008; 17: 1774-82.
    • (2008) Human molecular genetics , vol.17 , pp. 1774-1782
    • Lee, J.1    Hagerty, S.2    Cormier, K.A.3
  • 198
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profiling of histone methylations in the human genome
    • Barski A, Cuddapah S, Cui K, et al. High-resolution profiling of histone methylations in the human genome. Cell 2007; 129: 823-37.
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1    Cuddapah, S.2    Cui, K.3
  • 199
    • 77950678085 scopus 로고    scopus 로고
    • Coordinated chromatin control: Structural and functional linkage of DNA and histone methylation
    • Cheng X, Blumenthal RM. Coordinated chromatin control: structural and functional linkage of DNA and histone methylation. Biochemistry 2010; 49: 2999-3008.
    • (2010) Biochemistry , vol.49 , pp. 2999-3008
    • Cheng, X.1    Blumenthal, R.M.2
  • 200
    • 0037112369 scopus 로고    scopus 로고
    • Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2'-deoxycytidine
    • Nguyen CT, Weisenberger DJ, Velicescu M, Gonzales FA, Lin JC, Liang G, Jones PA. Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2'-deoxycytidine. Cancer research 2002; 62: 6456-61.
    • (2002) Cancer research , vol.62 , pp. 6456-6461
    • Nguyen, C.T.1    Weisenberger, D.J.2    Velicescu, M.3    Gonzales, F.A.4    Lin, J.C.5    Liang, G.6    Jones, P.A.7
  • 201
    • 77951233574 scopus 로고    scopus 로고
    • G9a and Glp methylate lysine 373 in the tumor suppressor p53
    • Huang J, Dorsey J, Chuikov S, et al. G9a and Glp methylate lysine 373 in the tumor suppressor p53. The Journal of biological chemistry 2010; 285: 9636-41.
    • (2010) The Journal of biological chemistry , vol.285 , pp. 9636-9641
    • Huang, J.1    Dorsey, J.2    Chuikov, S.3
  • 202
    • 46149100720 scopus 로고    scopus 로고
    • The global histone modification pattern correlates with cancer recurrence and overall survival in gastric adenocarcinoma
    • Park YS, Jin MY, Kim YJ, Yook JH, Kim BS, Jang SJ. The global histone modification pattern correlates with cancer recurrence and overall survival in gastric adenocarcinoma. Annals of surgical oncology 2008; 15: 1968-76.
    • (2008) Annals of surgical oncology , vol.15 , pp. 1968-1976
    • Park, Y.S.1    Jin, M.Y.2    Kim, Y.J.3    Yook, J.H.4    Kim, B.S.5    Jang, S.J.6
  • 204
    • 33746332412 scopus 로고    scopus 로고
    • The putative oncogene GASC1 demethylates tri-and dimethylated lysine 9 on histone H3
    • Cloos PA, Christensen J, Agger K, et al. The putative oncogene GASC1 demethylates tri-and dimethylated lysine 9 on histone H3. Nature 2006; 442: 307-11.
    • (2006) Nature , vol.442 , pp. 307-311
    • Cloos, P.A.1    Christensen, J.2    Agger, K.3
  • 205
    • 0034282790 scopus 로고    scopus 로고
    • Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines
    • Yang ZQ, Imoto I, Fukuda Y, et al. Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines. Cancer research 2000; 60: 4735-9.
    • (2000) Cancer research , vol.60 , pp. 4735-4739
    • Yang, Z.Q.1    Imoto, I.2    Fukuda, Y.3
  • 207
    • 72449186524 scopus 로고    scopus 로고
    • Genomic amplification and oncogenic properties of the GASC1 histone demethylase gene in breast cancer
    • Liu G, Bollig-Fischer A, Kreike B, et al. Genomic amplification and oncogenic properties of the GASC1 histone demethylase gene in breast cancer. Oncogene 2009; 28: 4491-500.
    • (2009) Oncogene , vol.28 , pp. 4491-4500
    • Liu, G.1    Bollig-Fischer, A.2    Kreike, B.3
  • 208
    • 20144388722 scopus 로고    scopus 로고
    • Genome-wide association study in esophageal cancer using GeneChip mapping 10K array
    • Hu N, Wang C, Hu Y, et al. Genome-wide association study in esophageal cancer using GeneChip mapping 10K array. Cancer research 2005; 65: 2542-6.
    • (2005) Cancer research , vol.65 , pp. 2542-2546
    • Hu, N.1    Wang, C.2    Hu, Y.3
  • 209
    • 0035003039 scopus 로고    scopus 로고
    • A novel amplicon at 9p23-24 in squamous cell carcinoma of the esophagus that lies proximal to GASC1 and harbors NFIB
    • Yang ZQ, Imoto I, Pimkhaokham A, et al. A novel amplicon at 9p23-24 in squamous cell carcinoma of the esophagus that lies proximal to GASC1 and harbors NFIB. Japanese journal of cancer research: Gann 2001; 92: 423-8.
    • (2001) Japanese journal of cancer research: Gann , vol.92 , pp. 423-428
    • Yang, Z.Q.1    Imoto, I.2    Pimkhaokham, A.3
  • 210
    • 33646070846 scopus 로고    scopus 로고
    • A bivalent chromatin structure marks key developmental genes in embryonic stem cells
    • Bernstein BE, Mikkelsen TS, Xie X, et al. A bivalent chromatin structure marks key developmental genes in embryonic stem cells. Cell 2006; 125: 315-26.
    • (2006) Cell , vol.125 , pp. 315-326
    • Bernstein, B.E.1    Mikkelsen, T.S.2    Xie, X.3
  • 212
    • 55949132133 scopus 로고    scopus 로고
    • Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms
    • Margueron R, Li G, Sarma K, et al. Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Molecular cell 2008; 32: 503-18.
    • (2008) Molecular cell , vol.32 , pp. 503-518
    • Margueron, R.1    Li, G.2    Sarma, K.3
  • 213
    • 55949124844 scopus 로고    scopus 로고
    • EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency
    • Shen X, Liu Y, Hsu YJ, et al. EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Molecular cell 2008; 32: 491-502.
    • (2008) Molecular cell , vol.32 , pp. 491-502
    • Shen, X.1    Liu, Y.2    Hsu, Y.J.3
  • 214
    • 33845799903 scopus 로고    scopus 로고
    • Polycomb silencing mechanisms and the management of genomic programmes
    • Schwartz YB, Pirrotta V. Polycomb silencing mechanisms and the management of genomic programmes. Nature reviews. Genetics 2007; 8: 9-22.
    • (2007) Nature reviews. Genetics , vol.8 , pp. 9-22
    • Schwartz, Y.B.1    Pirrotta, V.2
  • 215
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • Margueron R, Justin N, Ohno K, et al. Role of the polycomb protein EED in the propagation of repressive histone marks. Nature 2009; 461: 762-7.
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1    Justin, N.2    Ohno, K.3
  • 216
    • 8144230178 scopus 로고    scopus 로고
    • Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity
    • Pasini D, Bracken AP, Jensen MR, Lazzerini Denchi E, Helin K. Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity. The EMBO journal 2004; 23: 4061-71.
    • (2004) The EMBO journal , vol.23 , pp. 4061-4071
    • Pasini, D.1    Bracken, A.P.2    Jensen, M.R.3    Lazzerini Denchi, E.4    Helin, K.5
  • 217
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EEDEZH2 complex
    • Cao R, Zhang Y. SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EEDEZH2 complex. Molecular cell 2004; 15: 57-67.
    • (2004) Molecular cell , vol.15 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 220
    • 72249119297 scopus 로고    scopus 로고
    • Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells
    • Peng JC, Valouev A, Swigut T, et al. Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells. Cell 2009; 139: 1290-302.
    • (2009) Cell , vol.139 , pp. 1290-1302
    • Peng, J.C.1    Valouev, A.2    Swigut, T.3
  • 221
    • 72249104107 scopus 로고    scopus 로고
    • Jumonji modulates polycomb activity and self-renewal versus differentiation of stem cells
    • Shen X, Kim W, Fujiwara Y, et al. Jumonji modulates polycomb activity and self-renewal versus differentiation of stem cells. Cell 2009; 139: 1303-14.
    • (2009) Cell , vol.139 , pp. 1303-1314
    • Shen, X.1    Kim, W.2    Fujiwara, Y.3
  • 222
    • 40749126138 scopus 로고    scopus 로고
    • Role of hPHF1 in H3K27 methylation and Hox gene silencing
    • Cao R, Wang H, He J, et al. Role of hPHF1 in H3K27 methylation and Hox gene silencing. Molecular and cellular biology 2008; 28: 1862-72.
    • (2008) Molecular and cellular biology , vol.28 , pp. 1862-1872
    • Cao, R.1    Wang, H.2    He, J.3
  • 224
    • 75349104610 scopus 로고    scopus 로고
    • Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation
    • Walker E, Chang WY, Hunkapiller J, et al. Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation. Cell stem cell 2010; 6: 153-66.
    • (2010) Cell stem cell , vol.6 , pp. 153-166
    • Walker, E.1    Chang, W.Y.2    Hunkapiller, J.3
  • 225
    • 79952135845 scopus 로고    scopus 로고
    • PRC2 complexes with JARID2, MTF2, and esPRC2p48 in ES cells to modulate ES cell pluripotency and somatic cell reprogramming
    • Zhang Z, Jones A, Sun CW, et al. PRC2 complexes with JARID2, MTF2, and esPRC2p48 in ES cells to modulate ES cell pluripotency and somatic cell reprogramming. Stem cells 2011; 29: 229-40.
    • (2011) Stem cells , vol.29 , pp. 229-240
    • Zhang, Z.1    Jones, A.2    Sun, C.W.3
  • 226
    • 79951540680 scopus 로고    scopus 로고
    • Functional characterization of human Polycomb-like 3 isoforms identifies them as components of distinct EZH2 protein complexes
    • Boulay G, Rosnoblet C, Guerardel C, Angrand PO, Leprince D. Functional characterization of human Polycomb-like 3 isoforms identifies them as components of distinct EZH2 protein complexes. The Biochemical journal 2011; 434: 333-42.
    • (2011) The Biochemical journal , vol.434 , pp. 333-342
    • Boulay, G.1    Rosnoblet, C.2    Guerardel, C.3    Angrand, P.O.4    Leprince, D.5
  • 227
    • 9244265488 scopus 로고    scopus 로고
    • A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers
    • Wang S, Robertson GP, Zhu J. A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers. Gene 2004; 343: 69-78.
    • (2004) Gene , vol.343 , pp. 69-78
    • Wang, S.1    Robertson, G.P.2    Zhu, J.3
  • 228
    • 77953120646 scopus 로고    scopus 로고
    • Jarid2 is a PRC2 component in embryonic stem cells required for multi-lineage differentiation and recruitment of PRC1 and RNA Polymerase II to developmental regulators
    • Landeira D, Sauer S, Poot R, et al. Jarid2 is a PRC2 component in embryonic stem cells required for multi-lineage differentiation and recruitment of PRC1 and RNA Polymerase II to developmental regulators. Nature cell biology 2010; 12: 618-24.
    • (2010) Nature cell biology , vol.12 , pp. 618-624
    • Landeira, D.1    Sauer, S.2    Poot, R.3
  • 230
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R, Wang L, Wang H, et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 2002; 298: 1039-43.
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3
  • 231
    • 36749089980 scopus 로고    scopus 로고
    • Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells
    • Stock JK, Giadrossi S, Casanova M, et al. Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells. Nature cell biology 2007; 9: 1428-35.
    • (2007) Nature cell biology , vol.9 , pp. 1428-1435
    • Stock, J.K.1    Giadrossi, S.2    Casanova, M.3
  • 232
    • 9444244427 scopus 로고    scopus 로고
    • Chromatin compaction by a polycomb group protein complex
    • Francis NJ, Kingston RE, Woodcock CL. Chromatin compaction by a polycomb group protein complex. Science 2004; 306: 1574-7.
    • (2004) Science , vol.306 , pp. 1574-1577
    • Francis, N.J.1    Kingston, R.E.2    Woodcock, C.L.3
  • 233
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang H, Wang L, Erdjument-Bromage H, et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 2004; 431: 873-8.
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1    Wang, L.2    Erdjument-Bromage, H.3
  • 234
    • 0242362735 scopus 로고    scopus 로고
    • Genome-wide prediction of Polycomb/Trithorax response elements in Drosophila melanogaster
    • Ringrose L, Rehmsmeier M, Dura JM, Paro R. Genome-wide prediction of Polycomb/Trithorax response elements in Drosophila melanogaster. Developmental cell 2003; 5: 759-71.
    • (2003) Developmental cell , vol.5 , pp. 759-771
    • Ringrose, L.1    Rehmsmeier, M.2    Dura, J.M.3    Paro, R.4
  • 235
    • 69449086947 scopus 로고    scopus 로고
    • A vertebrate Polycomb response element governs segmentation of the posterior hindbrain
    • Sing A, Pannell D, Karaiskakis A, et al. A vertebrate Polycomb response element governs segmentation of the posterior hindbrain. Cell 2009; 138: 885-97.
    • (2009) Cell , vol.138 , pp. 885-897
    • Sing, A.1    Pannell, D.2    Karaiskakis, A.3
  • 237
    • 78650684739 scopus 로고    scopus 로고
    • GC-rich sequence elements recruit PRC2 in mammalian ES cells
    • Mendenhall EM, Koche RP, Truong T, et al. GC-rich sequence elements recruit PRC2 in mammalian ES cells. PLoS genetics 2010; 6: e1001244.
    • (2010) PLoS genetics , vol.6
    • Mendenhall, E.M.1    Koche, R.P.2    Truong, T.3
  • 238
    • 73149111929 scopus 로고    scopus 로고
    • A region of the human HOXD cluster that confers polycomb-group responsiveness
    • Woo CJ, Kharchenko PV, Daheron L, Park PJ, Kingston RE. A region of the human HOXD cluster that confers polycomb-group responsiveness. Cell 2010; 140: 99-110.
    • (2010) Cell , vol.140 , pp. 99-110
    • Woo, C.J.1    Kharchenko, P.V.2    Daheron, L.3    Park, P.J.4    Kingston, R.E.5
  • 239
    • 55549103314 scopus 로고    scopus 로고
    • A model for transmission of the H3K27me3 epigenetic mark
    • Hansen KH, Bracken AP, Pasini D, et al. A model for transmission of the H3K27me3 epigenetic mark. Nature cell biology 2008; 10: 1291-300.
    • (2008) Nature cell biology , vol.10 , pp. 1291-1300
    • Hansen, K.H.1    Bracken, A.P.2    Pasini, D.3
  • 240
    • 70350149728 scopus 로고    scopus 로고
    • Recruitment of polycomb group complexes and their role in the dynamic regulation of cell fate choice
    • Schuettengruber B, Cavalli G. Recruitment of polycomb group complexes and their role in the dynamic regulation of cell fate choice. Development 2009; 136: 3531-42.
    • (2009) Development , vol.136 , pp. 3531-3542
    • Schuettengruber, B.1    Cavalli, G.2
  • 241
    • 58049191558 scopus 로고    scopus 로고
    • Chromatin signatures in multipotent human hematopoietic stem cells indicate the fate of bivalent genes during differentiation
    • Cui K, Zang C, Roh TY, et al. Chromatin signatures in multipotent human hematopoietic stem cells indicate the fate of bivalent genes during differentiation. Cell stem cell 2009; 4: 80-93.
    • (2009) Cell stem cell , vol.4 , pp. 80-93
    • Cui, K.1    Zang, C.2    Roh, T.Y.3
  • 242
    • 78650587058 scopus 로고    scopus 로고
    • Epigenetic factors in cancer development: Polycomb group proteins
    • Piunti A, Pasini D. Epigenetic factors in cancer development: polycomb group proteins. Future oncology 2011; 7: 57-75.
    • (2011) Future oncology , vol.7 , pp. 57-75
    • Piunti, A.1    Pasini, D.2
  • 243
    • 35148898348 scopus 로고    scopus 로고
    • A histone H3 lysine 27 demethylase regulates animal posterior development
    • Lan F, Bayliss PE, Rinn JL, et al. A histone H3 lysine 27 demethylase regulates animal posterior development. Nature 2007; 449: 689-94.
    • (2007) Nature , vol.449 , pp. 689-694
    • Lan, F.1    Bayliss, P.E.2    Rinn, J.L.3
  • 244
    • 35348993743 scopus 로고    scopus 로고
    • Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination
    • Lee MG, Villa R, Trojer P, et al. Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination. Science 2007; 318: 447-50.
    • (2007) Science , vol.318 , pp. 447-450
    • Lee, M.G.1    Villa, R.2    Trojer, P.3
  • 245
    • 35148867907 scopus 로고    scopus 로고
    • UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
    • Agger K, Cloos PA, Christensen J, et al. UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 2007; 449: 731-4.
    • (2007) Nature , vol.449 , pp. 731-734
    • Agger, K.1    Cloos, P.A.2    Christensen, J.3
  • 247
    • 66149138053 scopus 로고    scopus 로고
    • The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4AARF locus in response to oncogene-and stress-induced senescence
    • Agger K, Cloos PA, Rudkjaer L, et al. The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4AARF locus in response to oncogene-and stress-induced senescence. Genes & development 2009; 23: 1171-6.
    • (2009) Genes & development , vol.23 , pp. 1171-1176
    • Agger, K.1    Cloos, P.A.2    Rudkjaer, L.3
  • 248
    • 33947134834 scopus 로고    scopus 로고
    • The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells
    • Bracken AP, Kleine-Kohlbrecher D, Dietrich N, et al. The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells. Genes & development 2007; 21: 525-30.
    • (2007) Genes & development , vol.21 , pp. 525-530
    • Bracken, A.P.1    Kleine-Kohlbrecher, D.2    Dietrich, N.3
  • 249
    • 77953973940 scopus 로고    scopus 로고
    • Characterization of an antagonistic switch between histone H3 lysine 27 methylation and acetylation in the transcriptional regulation of Polycomb group target genes
    • Pasini D, Malatesta M, Jung HR, et al. Characterization of an antagonistic switch between histone H3 lysine 27 methylation and acetylation in the transcriptional regulation of Polycomb group target genes. Nucleic acids research 2010; 38: 4958-69.
    • (2010) Nucleic acids research , vol.38 , pp. 4958-4969
    • Pasini, D.1    Malatesta, M.2    Jung, H.R.3
  • 250
    • 67349203626 scopus 로고    scopus 로고
    • Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer
    • van Haaften G, Dalgliesh GL, et al. Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer. Nature genetics 2009; 41: 521-3.
    • (2009) Nature genetics , vol.41 , pp. 521-523
    • van Haaften, G.1    Dalgliesh, G.L.2
  • 251
    • 79955470771 scopus 로고    scopus 로고
    • The H3K27me3 demethylase, KDM6B, is induced by Epstein-Barr virus and overexpressed in Hodgkin's Lymphoma
    • Anderton JA, Bose S, Vockerodt M, et al. The H3K27me3 demethylase, KDM6B, is induced by Epstein-Barr virus and overexpressed in Hodgkin's Lymphoma. Oncogene 2011; 30: 2037-43.
    • (2011) Oncogene , vol.30 , pp. 2037-2043
    • Anderton, J.A.1    Bose, S.2    Vockerodt, M.3
  • 253
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • Schotta G, Lachner M, Sarma K, et al. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes & development 2004; 18: 1251-62.
    • (2004) Genes & development , vol.18 , pp. 1251-1262
    • Schotta, G.1    Lachner, M.2    Sarma, K.3
  • 254
    • 3042858906 scopus 로고    scopus 로고
    • Heterochromatin and tri-methylated lysine 20 of histone H4 in animals
    • Kourmouli N, Jeppesen P, Mahadevhaiah S, et al. Heterochromatin and tri-methylated lysine 20 of histone H4 in animals. Journal of cell science 2004; 117: 2491-501.
    • (2004) Journal of cell science , vol.117 , pp. 2491-2501
    • Kourmouli, N.1    Jeppesen, P.2    Mahadevhaiah, S.3
  • 255
    • 18444392703 scopus 로고    scopus 로고
    • PR-Set7 is a nucleosomespecific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin
    • Nishioka K, Rice JC, Sarma K, et al. PR-Set7 is a nucleosomespecific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin. Molecular cell 2002; 9: 1201-13.
    • (2002) Molecular cell , vol.9 , pp. 1201-1213
    • Nishioka, K.1    Rice, J.C.2    Sarma, K.3
  • 256
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture JF, Collazo E, Brunzelle JS, Trievel RC. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes & development 2005; 19: 1455-65.
    • (2005) Genes & development , vol.19 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 257
    • 22344455665 scopus 로고    scopus 로고
    • Specificity and mechanism of the histone methyltransferase Pr-Set7
    • Xiao B, Jing C, Kelly G, et al. Specificity and mechanism of the histone methyltransferase Pr-Set7. Genes & development 2005; 19: 1444-54.
    • (2005) Genes & development , vol.19 , pp. 1444-1454
    • Xiao, B.1    Jing, C.2    Kelly, G.3
  • 258
    • 0037046802 scopus 로고    scopus 로고
    • Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase
    • Fang J, Feng Q, Ketel CS, et al. Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Current biology: CB 2002; 12: 1086-99.
    • (2002) Current biology: CB , vol.12 , pp. 1086-1099
    • Fang, J.1    Feng, Q.2    Ketel, C.S.3
  • 259
    • 77954954200 scopus 로고    scopus 로고
    • PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression
    • Liu W, Tanasa B, Tyurina OV, et al. PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression. Nature 2010; 466: 508-12.
    • (2010) Nature , vol.466 , pp. 508-512
    • Liu, W.1    Tanasa, B.2    Tyurina, O.V.3
  • 260
    • 77954957901 scopus 로고    scopus 로고
    • Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development
    • Qi HH, Sarkissian M, Hu GQ, et al. Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development. Nature 2010; 466: 503-7.
    • (2010) Nature , vol.466 , pp. 503-507
    • Qi, H.H.1    Sarkissian, M.2    Hu, G.Q.3
  • 261
    • 50349085791 scopus 로고    scopus 로고
    • Catalytic function of the PR-Set7 histone H4 lysine 20 monomethyltransferase is essential for mitotic entry and genomic stability
    • Houston SI, McManus KJ, Adams MM, et al. Catalytic function of the PR-Set7 histone H4 lysine 20 monomethyltransferase is essential for mitotic entry and genomic stability. The Journal of biological chemistry 2008; 283: 19478-88.
    • (2008) The Journal of biological chemistry , vol.283 , pp. 19478-19488
    • Houston, S.I.1    McManus, K.J.2    Adams, M.M.3
  • 262
    • 0036714189 scopus 로고    scopus 로고
    • Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes
    • Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD. Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes. Genes & development 2002; 16: 2225-30.
    • (2002) Genes & development , vol.16 , pp. 2225-2230
    • Rice, J.C.1    Nishioka, K.2    Sarma, K.3    Steward, R.4    Reinberg, D.5    Allis, C.D.6
  • 263
    • 45549087777 scopus 로고    scopus 로고
    • Direct interaction between SET8 and proliferating cell nuclear antigen couples H4-K20 methylation with DNA replication
    • Huen MS, Sy SM, van Deursen JM, Chen J. Direct interaction between SET8 and proliferating cell nuclear antigen couples H4-K20 methylation with DNA replication. The Journal of biological chemistry 2008; 283: 11073-7.
    • (2008) The Journal of biological chemistry , vol.283 , pp. 11073-11077
    • Huen, M.S.1    Sy, S.M.2    van Deursen, J.M.3    Chen, J.4
  • 264
    • 38049075810 scopus 로고    scopus 로고
    • The histone methyltransferase SET8 is required for S-phase progression
    • Jorgensen S, Elvers I, Trelle MB, et al. The histone methyltransferase SET8 is required for S-phase progression. The Journal of cell biology 2007; 179: 1337-45.
    • (2007) The Journal of cell biology , vol.179 , pp. 1337-1345
    • Jorgensen, S.1    Elvers, I.2    Trelle, M.B.3
  • 265
    • 38049025837 scopus 로고    scopus 로고
    • PR-Set7-dependent lysine methylation ensures genome replication and stability through S phase
    • Tardat M, Murr R, Herceg Z, Sardet C, Julien E. PR-Set7-dependent lysine methylation ensures genome replication and stability through S phase. The Journal of cell biology 2007; 179: 1413-26.
    • (2007) The Journal of cell biology , vol.179 , pp. 1413-1426
    • Tardat, M.1    Murr, R.2    Herceg, Z.3    Sardet, C.4    Julien, E.5
  • 266
    • 78149423004 scopus 로고    scopus 로고
    • Regulation of the histone H4 monomethylase PR-Set7 by CRL4(Cdt2)-mediated PCNAdependent degradation during DNA damage
    • Oda H, Hubner MR, Beck DB, et al. Regulation of the histone H4 monomethylase PR-Set7 by CRL4(Cdt2)-mediated PCNAdependent degradation during DNA damage. Molecular cell 2010; 40: 364-76.
    • (2010) Molecular cell , vol.40 , pp. 364-376
    • Oda, H.1    Hubner, M.R.2    Beck, D.B.3
  • 267
    • 78149281634 scopus 로고    scopus 로고
    • The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
    • Tardat M, Brustel J, Kirsh O, et al. The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells. Nature cell biology 2010; 12: 1086-93.
    • (2010) Nature cell biology , vol.12 , pp. 1086-1093
    • Tardat, M.1    Brustel, J.2    Kirsh, O.3
  • 268
    • 77957367739 scopus 로고    scopus 로고
    • CRL4(Cdt2)-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase
    • Centore RC, Havens CG, Manning AL, et al. CRL4(Cdt2)-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase. Molecular cell 2010; 40: 22-33.
    • (2010) Molecular cell , vol.40 , pp. 22-33
    • Centore, R.C.1    Havens, C.G.2    Manning, A.L.3
  • 269
    • 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, et al. Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. Molecular and cellular biology 2009; 29: 2278-95.
    • (2009) Molecular and cellular biology , vol.29 , pp. 2278-2295
    • Oda, H.1    Okamoto, I.2    Murphy, N.3
  • 271
    • 32544452237 scopus 로고    scopus 로고
    • Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins
    • Tryndyak VP, Kovalchuk O, Pogribny IP. Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins. Cancer biology & therapy 2006; 5: 65-70.
    • (2006) Cancer biology & therapy , vol.5 , pp. 65-70
    • Tryndyak, V.P.1    Kovalchuk, O.2    Pogribny, I.P.3
  • 272
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
    • Fraga MF, Ballestar E, Villar-Garea A, et al. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nature genetics 2005; 37: 391-400.
    • (2005) Nature genetics , vol.37 , pp. 391-400
    • Fraga, M.F.1    Ballestar, E.2    Villar-Garea, A.3
  • 273
    • 77953934846 scopus 로고    scopus 로고
    • Derepression of CLDN3 and CLDN4 during ovarian tumorigenesis is associated with loss of repressive histone modifications
    • Kwon MJ, Kim SS, Choi YL, et al. Derepression of CLDN3 and CLDN4 during ovarian tumorigenesis is associated with loss of repressive histone modifications. Carcinogenesis 2010; 31: 974-83.
    • (2010) Carcinogenesis , vol.31 , pp. 974-983
    • Kwon, M.J.1    Kim, S.S.2    Choi, Y.L.3
  • 274
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell 2011; 144: 646-74.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 275
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones PA, Baylin SB. The epigenomics of cancer. Cell 2007; 128: 683-92.
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 276
    • 33750379420 scopus 로고    scopus 로고
    • Polycomb silencers control cell fate, development and cancer
    • Sparmann A, van Lohuizen M. Polycomb silencers control cell fate, development and cancer. Nature reviews. Cancer 2006; 6: 846-56.
    • (2006) Nature reviews. Cancer , vol.6 , pp. 846-856
    • Sparmann, A.1    van Lohuizen, M.2
  • 277
    • 84876742643 scopus 로고    scopus 로고
    • Colorectal Cancer Microenvirnoment: Between Nutrition, Gut Microbiota, Inflammation and Epigenetics
    • Garagnani P, Pirazzini C, Franceschi C. Colorectal Cancer Microenvirnoment: between Nutrition, Gut Microbiota, Inflammation and Epigenetics. Curr Pharm Des 2013; 19(4): 765-78.
    • (2013) Curr Pharm Des , vol.19 , Issue.4 , pp. 765-778
    • Garagnani, P.1    Pirazzini, C.2    Franceschi, C.3
  • 278
    • 84870693696 scopus 로고    scopus 로고
    • Modulation of epigenetic targets for anticancer therapy: Clinicopathological relevance, structural data and drug discovery perspectives
    • Andreoli F, Barbosa AJM, Parenti MD, Del Rio A. Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives. Curr Pharm Des 201; 19(4): 578-613.
    • (2011) Curr Pharm Des , vol.19 , Issue.4 , pp. 578-613
    • Andreoli, F.1    Barbosa, A.J.M.2    Parenti, M.D.3    Del Rio, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.