Histone modification patterns and epigenetic codes

The eukaryotic DNA is wrapped around histone octamers, which consist of four different histones, H2A, H2B, H3 and H4. The N-terminal tail of each histone is post-transcriptionally modified. The modification patterns constitute codes that regulate chromatin organisation and DNA utilization processes,...

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Published inBiochimica et biophysica acta Vol. 1790; no. 9; pp. 863 - 868
Main Authors Lennartsson, Andreas, Ekwall, Karl
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.09.2009
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Abstract The eukaryotic DNA is wrapped around histone octamers, which consist of four different histones, H2A, H2B, H3 and H4. The N-terminal tail of each histone is post-transcriptionally modified. The modification patterns constitute codes that regulate chromatin organisation and DNA utilization processes, including transcription. Recent progress in technology development has made it possible to perform systematic genome-wide studies of histone modifications. This helps immensely in deciphering the histone codes and their biological influence. In this review, we discuss the histone modification patterns found in genome-wide studies in different biological models and how they influence cell differentiation and carcinogenesis.
AbstractList The eukaryotic DNA is wrapped around histone octamers, which consist of four different histones, H2A, H2B, H3 and H4. The N-terminal tail of each histone is post-transcriptionally modified. The modification patterns constitute codes that regulate chromatin organisation and DNA utilization processes, including transcription. Recent progress in technology development has made it possible to perform systematic genome-wide studies of histone modifications. This helps immensely in deciphering the histone codes and their biological influence. In this review, we discuss the histone modification patterns found in genome-wide studies in different biological models and how they influence cell differentiation and carcinogenesis.
Author Ekwall, Karl
Lennartsson, Andreas
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Cites_doi 10.1016/j.ydbio.2004.08.038
10.1074/jbc.M507407200
10.1016/j.tig.2005.08.009
10.1186/1471-213X-7-24
10.1016/j.cell.2006.02.043
10.1128/MCB.23.1.206-215.2003
10.4161/cbt.5.1.2288
10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X
10.1093/carcin/bgi364
10.1038/nature04219
10.1016/j.cell.2006.02.041
10.1586/14737140.7.4.583
10.1016/j.cell.2007.05.042
10.1371/journal.pbio.0030328
10.1016/j.cell.2004.05.023
10.1038/47412
10.1038/nature04733
10.1007/s00412-003-0244-6
10.1016/j.devcel.2005.10.017
10.1186/gb-2005-6-6-113
10.1016/j.bbagrm.2008.07.001
10.1038/sj.onc.1204336
10.1038/nature06906
10.1038/sj.emboj.7601926
10.1016/S1097-2765(00)80431-1
10.1038/nsmb.1432
10.1038/nature06561
10.1016/j.cell.2005.10.002
10.1038/ng.154
10.1158/0008-5472.CAN-07-2498
10.1038/nsmb0608-542
10.1038/nrg1748
10.1200/JCO.2007.11.2599
10.1038/ng1972
10.1101/gad.381706
10.1158/0008-5472.CAN-05-2481
10.1038/sj.emboj.7600516
10.1158/0008-5472.CAN-04-3063
10.1016/j.cell.2004.11.009
10.1016/j.molcel.2005.06.011
10.1038/ng1531
10.1038/nature03672
10.1128/MCB.01045-07
10.1186/1471-2199-8-31
10.1038/sj.emboj.7600758
10.3324/haematol.10758
10.1126/science.1124000
10.1016/j.cbpa.2006.11.022
10.1007/s00018-006-6026-6
10.1128/MCB.24.13.5710-5720.2004
10.1073/pnas.1933744100
10.1111/j.1464-410X.2006.06704.x
10.1038/scientificamerican1092-68
10.1016/j.mib.2005.06.007
10.1245/s10434-008-9927-9
10.1002/gene.10250
10.1101/gad.1198204
10.1038/nature05913
10.1016/j.spen.2006.11.004
10.1038/sj.onc.1210895
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Keywords Histone modification
Chromatin
Epigenetic
Cell differentiation
Histone code
Cancer
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References Kouskouti, Talianidis (bib6) 2005; 24
Schubeler, MacAlpine, Scalzo, Wirbelauer, Kooperberg, van Leeuwen, Gottschling, O, Neill, Turner, Delrow, Bell, Groudine (bib61) 2004; 18
Kurdistani, Tavazoie, Grunstein (bib13) 2004; 117
Bird (bib5) 2007; 447
Biron, McManus, Hu, Hendzel, Underhill (bib28) 2004; 276
Ohm, McGarvey, Yu, Cheng, Schuebel, Cope, Mohammad, Chen, Daniel, Yu, Berman, Jenuwein, Pruitt, Sharkis, Watkins, Herman, Baylin (bib42) 2007; 39
Bug, Schwarz, Schoch, Kampfmann, Henschler, Hoelzer, Ottmann, Ruthardt (bib64) 2007; 92
McGinty, Kim, Chatterjee, Roeder, Muir (bib34) 2008; 453
Frederiks, Tzouros, Oudgenoeg, van Welsem, Fornerod, Krijgsveld, van Leeuwen (bib33) 2008; 15
Mohamed, Greif, Diamond, Sharaf, Maxwell, Montironi, Young, Hamilton (bib48) 2007; 99
Strahl, Allis (bib2) 2000; 403
Fraga, Ballestar, Villar-Garea, Boix-Chornet, Espada, Schotta, Bonaldi, Haydon, Ropero, Petrie, Iyer, Perez-Rosado, Calvo, Lopez, Cano, Calasanz, Colomer, Piris, Ahn, Imhof, Caldas, Jenuwein, Esteller (bib49) 2005; 37
Pogribny, Ross, Tryndyak, Pogribna, Poirier, Karpinets (bib55) 2006; 27
Marchion, Munster (bib63) 2007; 7
Shogren-Knaak, Ishii, Sun, Pazin, Davie, Peterson (bib50) 2006; 311
Park, Jin, Kim, Yook, Kim, Jang (bib46) 2008; 15
Kondo, Shen, Issa (bib45) 2003; 23
Bell, Wirbelauer, Hild, Scharf, Schwaiger, MacAlpine, Zilbermann, van Leeuwen, Bell, Imhof, Garza, Peters, Schubeler (bib52) 2007; 26
Levenson, Sweatt (bib22) 2006; 63
Grunstein (bib1) 1992; 267
Yu, Yu, Rhodes, Tomlins, Cao, Chen, Mehra, Wang, Ghosh, Shah, Varambally, Pienta, Chinnaiyan (bib59) 2007; 67
Kimura, Tada, Nakatsuji, Tada (bib30) 2004; 24
Bracken, Dietrich, Pasini, Hansen, Helin (bib25) 2006; 20
Seligson, Horvath, Shi, Yu, Tze, Grunstein, Kurdistani (bib47) 2005; 435
Meshorer, Yellajoshula, George, Scambler, Brown, Misteli (bib23) 2006; 10
Minucci, Nervi, Lo Coco, Pelicci (bib21) 2001; 20
Sanders, Portoso, Mata, Bahler, Allshire, Kouzarides (bib27) 2004; 119
De Felice, Tatarelli, Mascolo, Gregorj, Agostini, Fiorini, Gelmetti, Pascale, Padula, Petrucci, Arcese, Nervi (bib18) 2005; 65
Boyer, Plath, Zeitlinger, Brambrink, Medeiros, Lee, Levine, Wernig, Tajonar, Ray, Bell, Otte, Vidal, Gifford, Young, Jaenisch (bib26) 2006; 441
Barlesi, Giaccone, Gallegos-Ruiz, Loundou, Span, Lefesvre, Kruyt, Rodriguez (bib57) 2007; 25
Peedicayil (bib38) 2007; 126
Snykers, Vanhaecke, De Becker, Papeleu, Vinken, Van Riet, Rogiers (bib19) 2007; 7
Liu, Kaplan, Kim, Buratowski, Schreiber, Friedman, Rando (bib14) 2005; 3
Zhang, Eugeni, Parthun, Freitas (bib4) 2003; 112
Tryndyak, Kovalchuk, Pogribny (bib54) 2006; 5
Turner (bib35) 2008; 15
Valls, Sanchez-Molina, Martinez-Balbas (bib7) 2005; 280
Akhtar, Becker (bib53) 2000; 5
Waggoner (bib39) 2007; 14
Kleer, Cao, Varambally, Shen, Ota, Tomlins, Ghosh, Sewalt, Otte, Hayes, Sabel, Livant, Weiss, Rubin, Chinnaiyan (bib58) 2003; 100
Wang, Zang, Rosenfeld, Schones, Barski, Cuddapah, Cui, Roh, Peng, Zhang, Zhao (bib12) 2008; 40
Chen, Zhang, Nicolas, Cam, Zofall, Grewal (bib9) 2008; 451
Raisner, Hartley, Meneghini, Bao, Liu, Schreiber, Rando, Madhani (bib15) 2005; 123
Lee, Jenner, Boyer, Guenther, Levine, Kumar, Chevalier, Johnstone, Cole, Isono, Koseki, Fuchikami, Abe, Murray, Zucker, Yuan, Bell, Herbolsheimer, Hannett, Sun, Odom, Otte, Volkert, Bartel, Melton, Gifford, Jaenisch, Young (bib24) 2006; 125
Wiren, Silverstein, Sinha, Walfridsson, Lee, Laurenson, Pillus, Robyr, Grunstein, Ekwall (bib51) 2005; 24
McGarvey, Fahrner, Greene, Martens, Jenuwein, Baylin (bib31) 2006; 66
Ralph, Scherf (bib40) 2005; 8
van Leeuwen, van Steensel (bib11) 2005; 6
Xin, Zhou, Song, Wu, Wei, Hao, Lv, Liu, Liang (bib8) 2007; 8
Turner (bib3) 2000; 22
Fahrner, Eguchi, Herman, Baylin (bib43) 2002; 62
Nguyen, Weisenberger, Velicescu, Gonzales, Lin, Liang, Jones (bib44) 2002; 62
Feinberg, Ohlsson, Henikoff (bib41) 2006; 7
Wiencke, Zheng, Morrison, Yeh (bib36) 2008; 27
Gupta, Guerin-Peyrou, Sharma, Park, Agarwal, Ganju, Pandita, Choi, Sukumar, Pandita, Ludwig, Pandita (bib56) 2008; 28
Guenther, Levine, Boyer, Jaenisch, Young (bib60) 2007; 130
Bernstein, Mikkelsen, Xie, Kamal, Huebert, Cuff, Fry, Meissner, Wernig, Plath, Jaenisch, Wagschal, Feil, Schreiber, Lander (bib29) 2006; 125
Fischle, Tseng, Dormann, Ueberheide, Garcia, Shabanowitz, Hunt, Funabiki, Allis (bib32) 2005; 438
Ekwall (bib62) 2005; 21
Vakoc, Mandat, Olenchock, Blobel (bib37) 2005; 19
Garcia, Shabanowitz, Hunt (bib10) 2007; 11
Lee, Hart, Skalnik (bib17) 2004; 38
Wyrick, Parra (bib16) 2009; 1789
Munster, Troso-Sandoval, Rosen, Rifkind, Marks, Richon (bib20) 2001; 61
Feinberg (10.1016/j.bbagen.2008.12.006_bib41) 2006; 7
Kimura (10.1016/j.bbagen.2008.12.006_bib30) 2004; 24
Chen (10.1016/j.bbagen.2008.12.006_bib9) 2008; 451
Nguyen (10.1016/j.bbagen.2008.12.006_bib44) 2002; 62
Yu (10.1016/j.bbagen.2008.12.006_bib59) 2007; 67
Meshorer (10.1016/j.bbagen.2008.12.006_bib23) 2006; 10
Kouskouti (10.1016/j.bbagen.2008.12.006_bib6) 2005; 24
Turner (10.1016/j.bbagen.2008.12.006_bib3) 2000; 22
Wiencke (10.1016/j.bbagen.2008.12.006_bib36) 2008; 27
Turner (10.1016/j.bbagen.2008.12.006_bib35) 2008; 15
McGinty (10.1016/j.bbagen.2008.12.006_bib34) 2008; 453
McGarvey (10.1016/j.bbagen.2008.12.006_bib31) 2006; 66
Wyrick (10.1016/j.bbagen.2008.12.006_bib16) 2009; 1789
Snykers (10.1016/j.bbagen.2008.12.006_bib19) 2007; 7
Pogribny (10.1016/j.bbagen.2008.12.006_bib55) 2006; 27
Fischle (10.1016/j.bbagen.2008.12.006_bib32) 2005; 438
Sanders (10.1016/j.bbagen.2008.12.006_bib27) 2004; 119
Ekwall (10.1016/j.bbagen.2008.12.006_bib62) 2005; 21
Tryndyak (10.1016/j.bbagen.2008.12.006_bib54) 2006; 5
Waggoner (10.1016/j.bbagen.2008.12.006_bib39) 2007; 14
Lee (10.1016/j.bbagen.2008.12.006_bib24) 2006; 125
Shogren-Knaak (10.1016/j.bbagen.2008.12.006_bib50) 2006; 311
Akhtar (10.1016/j.bbagen.2008.12.006_bib53) 2000; 5
Zhang (10.1016/j.bbagen.2008.12.006_bib4) 2003; 112
Ohm (10.1016/j.bbagen.2008.12.006_bib42) 2007; 39
Liu (10.1016/j.bbagen.2008.12.006_bib14) 2005; 3
Kondo (10.1016/j.bbagen.2008.12.006_bib45) 2003; 23
Garcia (10.1016/j.bbagen.2008.12.006_bib10) 2007; 11
Marchion (10.1016/j.bbagen.2008.12.006_bib63) 2007; 7
Bracken (10.1016/j.bbagen.2008.12.006_bib25) 2006; 20
Kurdistani (10.1016/j.bbagen.2008.12.006_bib13) 2004; 117
Mohamed (10.1016/j.bbagen.2008.12.006_bib48) 2007; 99
van Leeuwen (10.1016/j.bbagen.2008.12.006_bib11) 2005; 6
Ralph (10.1016/j.bbagen.2008.12.006_bib40) 2005; 8
Seligson (10.1016/j.bbagen.2008.12.006_bib47) 2005; 435
Strahl (10.1016/j.bbagen.2008.12.006_bib2) 2000; 403
Park (10.1016/j.bbagen.2008.12.006_bib46) 2008; 15
Levenson (10.1016/j.bbagen.2008.12.006_bib22) 2006; 63
Wiren (10.1016/j.bbagen.2008.12.006_bib51) 2005; 24
Bernstein (10.1016/j.bbagen.2008.12.006_bib29) 2006; 125
Guenther (10.1016/j.bbagen.2008.12.006_bib60) 2007; 130
Bell (10.1016/j.bbagen.2008.12.006_bib52) 2007; 26
Wang (10.1016/j.bbagen.2008.12.006_bib12) 2008; 40
Peedicayil (10.1016/j.bbagen.2008.12.006_bib38) 2007; 126
Fahrner (10.1016/j.bbagen.2008.12.006_bib43) 2002; 62
Fraga (10.1016/j.bbagen.2008.12.006_bib49) 2005; 37
Bug (10.1016/j.bbagen.2008.12.006_bib64) 2007; 92
Boyer (10.1016/j.bbagen.2008.12.006_bib26) 2006; 441
Minucci (10.1016/j.bbagen.2008.12.006_bib21) 2001; 20
Raisner (10.1016/j.bbagen.2008.12.006_bib15) 2005; 123
Kleer (10.1016/j.bbagen.2008.12.006_bib58) 2003; 100
Bird (10.1016/j.bbagen.2008.12.006_bib5) 2007; 447
Biron (10.1016/j.bbagen.2008.12.006_bib28) 2004; 276
Munster (10.1016/j.bbagen.2008.12.006_bib20) 2001; 61
Valls (10.1016/j.bbagen.2008.12.006_bib7) 2005; 280
Xin (10.1016/j.bbagen.2008.12.006_bib8) 2007; 8
Gupta (10.1016/j.bbagen.2008.12.006_bib56) 2008; 28
Grunstein (10.1016/j.bbagen.2008.12.006_bib1) 1992; 267
De Felice (10.1016/j.bbagen.2008.12.006_bib18) 2005; 65
Frederiks (10.1016/j.bbagen.2008.12.006_bib33) 2008; 15
Barlesi (10.1016/j.bbagen.2008.12.006_bib57) 2007; 25
Lee (10.1016/j.bbagen.2008.12.006_bib17) 2004; 38
Schubeler (10.1016/j.bbagen.2008.12.006_bib61) 2004; 18
Vakoc (10.1016/j.bbagen.2008.12.006_bib37) 2005; 19
References_xml – volume: 100
  start-page: 11606
  year: 2003
  end-page: 11611
  ident: bib58
  article-title: EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 126
  start-page: 105
  year: 2007
  end-page: 111
  ident: bib38
  article-title: The role of epigenetics in mental disorders
  publication-title: Indian J. Med. Res.
– volume: 7
  start-page: 21
  year: 2006
  end-page: 33
  ident: bib41
  article-title: The epigenetic progenitor origin of human cancer
  publication-title: Nat. Rev. Genet.
– volume: 24
  start-page: 2906
  year: 2005
  end-page: 2918
  ident: bib51
  article-title: Genomewide analysis of nucleosome density histone acetylation and HDAC function in fission yeast
  publication-title: EMBO J.
– volume: 438
  start-page: 1116
  year: 2005
  end-page: 1122
  ident: bib32
  article-title: Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
  publication-title: Nature
– volume: 8
  start-page: 434
  year: 2005
  end-page: 440
  ident: bib40
  article-title: The epigenetic control of antigenic variation in
  publication-title: Curr. Opin. Microbiol.
– volume: 24
  start-page: 5710
  year: 2004
  end-page: 5720
  ident: bib30
  article-title: Histone code modifications on pluripotential nuclei of reprogrammed somatic cells
  publication-title: Mol. Cell. Biol.
– volume: 63
  start-page: 1009
  year: 2006
  end-page: 1016
  ident: bib22
  article-title: Epigenetic mechanisms: a common theme in vertebrate and invertebrate memory formation
  publication-title: Cell Mol. Life Sci.
– volume: 453
  start-page: 812
  year: 2008
  end-page: 816
  ident: bib34
  article-title: Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
  publication-title: Nature
– volume: 99
  start-page: 908
  year: 2007
  end-page: 915
  ident: bib48
  article-title: Epigenetic events, remodelling enzymes and their relationship to chromatin organization in prostatic intraepithelial neoplasia and prostatic adenocarcinoma
  publication-title: BJU Int.
– volume: 25
  start-page: 4358
  year: 2007
  end-page: 4364
  ident: bib57
  article-title: Global histone modifications predict prognosis of resected non small-cell lung cancer
  publication-title: J. Clin. Oncol.
– volume: 62
  start-page: 7213
  year: 2002
  end-page: 7218
  ident: bib43
  article-title: Dependence of histone modifications and gene expression on DNA hypermethylation in cancer
  publication-title: Cancer Res.
– volume: 119
  start-page: 603
  year: 2004
  end-page: 614
  ident: bib27
  article-title: Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
  publication-title: Cell
– volume: 7
  start-page: 583
  year: 2007
  end-page: 598
  ident: bib63
  article-title: Development of histone deacetylase inhibitors for cancer treatment
  publication-title: Expert Rev. Anticancer Ther.
– volume: 125
  start-page: 301
  year: 2006
  end-page: 313
  ident: bib24
  article-title: Control of developmental regulators by Polycomb in human embryonic stem cells
  publication-title: Cell
– volume: 67
  start-page: 10657
  year: 2007
  end-page: 10663
  ident: bib59
  article-title: A polycomb repression signature in metastatic prostate cancer predicts cancer outcome
  publication-title: Cancer Res.
– volume: 125
  start-page: 315
  year: 2006
  end-page: 326
  ident: bib29
  article-title: A bivalent chromatin structure marks key developmental genes in embryonic stem cells
  publication-title: Cell
– volume: 26
  start-page: 4974
  year: 2007
  end-page: 4984
  ident: bib52
  article-title: Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in
  publication-title: EMBO J.
– volume: 24
  start-page: 347
  year: 2005
  end-page: 357
  ident: bib6
  article-title: Histone modifications defining active genes persist after transcriptional and mitotic inactivation
  publication-title: EMBO J.
– volume: 451
  start-page: 734
  year: 2008
  end-page: 737
  ident: bib9
  article-title: Cell cycle control of centromeric repeat transcription and heterochromatin assembly
  publication-title: Nature
– volume: 61
  start-page: 8492
  year: 2001
  end-page: 8497
  ident: bib20
  article-title: The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
  publication-title: Cancer Res.
– volume: 38
  start-page: 32
  year: 2004
  end-page: 38
  ident: bib17
  article-title: Histone deacetylase activity is required for embryonic stem cell differentiation
  publication-title: Genesis
– volume: 20
  start-page: 1123
  year: 2006
  end-page: 1136
  ident: bib25
  article-title: Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions
  publication-title: Genes Dev.
– volume: 15
  start-page: 550
  year: 2008
  end-page: 557
  ident: bib33
  article-title: Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states
  publication-title: Nat. Struct. Mol. Biol.
– volume: 14
  start-page: 7
  year: 2007
  end-page: 14
  ident: bib39
  article-title: Mechanisms of disease: epigenesis
  publication-title: Semin. Pediatr. Neurol.
– volume: 267
  start-page: 68
  year: 1992
  end-page: 74B
  ident: bib1
  article-title: Histones as regulators of genes
  publication-title: Sci. Am.
– volume: 130
  start-page: 77
  year: 2007
  end-page: 88
  ident: bib60
  article-title: A chromatin landmark and transcription initiation at most promoters in human cells
  publication-title: Cell
– volume: 447
  start-page: 396
  year: 2007
  end-page: 398
  ident: bib5
  article-title: Perceptions of epigenetics
  publication-title: Nature
– volume: 5
  start-page: 367
  year: 2000
  end-page: 375
  ident: bib53
  article-title: Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in
  publication-title: Mol. Cell
– volume: 92
  start-page: 542
  year: 2007
  end-page: 545
  ident: bib64
  article-title: Effect of histone deacetylase inhibitor valproic acid on progenitor cells of acute myeloid leukemia
  publication-title: Haematologica
– volume: 311
  start-page: 844
  year: 2006
  end-page: 847
  ident: bib50
  article-title: Histone H4-K16 acetylation controls chromatin structure and protein interactions
  publication-title: Science
– volume: 11
  start-page: 66
  year: 2007
  end-page: 73
  ident: bib10
  article-title: Characterization of histones and their post-translational modifications by mass spectrometry
  publication-title: Curr. Opin. Chem. Biol.
– volume: 65
  start-page: 1505
  year: 2005
  end-page: 1513
  ident: bib18
  article-title: Histone deacetylase inhibitor valproic acid enhances the cytokine-induced expansion of human hematopoietic stem cells
  publication-title: Cancer Res.
– volume: 37
  start-page: 391
  year: 2005
  end-page: 400
  ident: bib49
  article-title: Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
  publication-title: Nat. Genet.
– volume: 21
  start-page: 608
  year: 2005
  end-page: 615
  ident: bib62
  article-title: Genome-wide analysis of HDAC function
  publication-title: Trends Genet.
– volume: 8
  start-page: 31
  year: 2007
  ident: bib8
  article-title: Exploring cellular memory molecules marking competent and active transcriptions
  publication-title: BMC Mol. Biol.
– volume: 1789
  start-page: 37
  year: 2009
  end-page: 44
  ident: bib16
  article-title: The role of histone H2A and H2B post-translational modifications in transcription: a genomic perspective
  publication-title: Biochim. Biophys. Acta
– volume: 20
  start-page: 3110
  year: 2001
  end-page: 3115
  ident: bib21
  article-title: Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias
  publication-title: Oncogene
– volume: 276
  start-page: 337
  year: 2004
  end-page: 351
  ident: bib28
  article-title: Distinct dynamics and distribution of histone methyl-lysine derivatives in mouse development
  publication-title: Dev. Biol.
– volume: 18
  start-page: 1263
  year: 2004
  end-page: 1271
  ident: bib61
  article-title: The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
  publication-title: Genes Dev.
– volume: 123
  start-page: 233
  year: 2005
  end-page: 248
  ident: bib15
  article-title: Histone variant H2A.Z marks the 5′ ends of both active and inactive genes in euchromatin
  publication-title: Cell
– volume: 15
  start-page: 1968
  year: 2008
  end-page: 1976
  ident: bib46
  article-title: The global histone modification pattern correlates with cancer recurrence and overall survival in gastric adenocarcinoma
  publication-title: Ann. Surg. Oncol.
– volume: 28
  start-page: 397
  year: 2008
  end-page: 409
  ident: bib56
  article-title: The mammalian ortholog of
  publication-title: Mol. Cell. Biol.
– volume: 66
  start-page: 3541
  year: 2006
  end-page: 3549
  ident: bib31
  article-title: Silenced tumor suppressor genes reactivated by DNA demethylation do not return to a fully euchromatic chromatin state
  publication-title: Cancer Res.
– volume: 6
  start-page: 113
  year: 2005
  ident: bib11
  article-title: Histone modifications: from genome-wide maps to functional insights
  publication-title: Genome Biol.
– volume: 39
  start-page: 237
  year: 2007
  end-page: 242
  ident: bib42
  article-title: A stem cell-like chromatin pattern may predispose tumor suppressor genes to DNA hypermethylation and heritable silencing
  publication-title: Nat. Genet.
– volume: 22
  start-page: 836
  year: 2000
  end-page: 845
  ident: bib3
  article-title: Histone acetylation and an epigenetic code
  publication-title: BioEssays
– volume: 7
  start-page: 24
  year: 2007
  ident: bib19
  article-title: Chromatin remodeling agent trichostatin A: a key-factor in the hepatic differentiation of human mesenchymal stem cells derived of adult bone marrow
  publication-title: BMC Dev. Biol.
– volume: 15
  start-page: 542
  year: 2008
  end-page: 544
  ident: bib35
  article-title: Simplifying a complex code
  publication-title: Nat. Struct. Mol. Biol.
– volume: 40
  start-page: 897
  year: 2008
  end-page: 903
  ident: bib12
  article-title: Combinatorial patterns of histone acetylations and methylations in the human genome
  publication-title: Nat. Genet.
– volume: 5
  start-page: 65
  year: 2006
  end-page: 70
  ident: bib54
  article-title: 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
  publication-title: Cancer Biol. Ther.
– volume: 27
  start-page: 2412
  year: 2008
  end-page: 2421
  ident: bib36
  article-title: Differentially expressed genes are marked by histone 3 lysine 9 trimethylation in human cancer cells
  publication-title: Oncogene
– volume: 10
  start-page: 105
  year: 2006
  end-page: 116
  ident: bib23
  article-title: Hyperdynamic plasticity of chromatin proteins in pluripotent embryonic stem cells
  publication-title: Dev. Cell
– volume: 27
  start-page: 1180
  year: 2006
  end-page: 1186
  ident: bib55
  article-title: Histone H3 lysine 9 and H4 lysine 20 trimethylation and the expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in hepatocarcinogenesis induced by methyl deficiency in rats
  publication-title: Carcinogenesis
– volume: 280
  start-page: 42592
  year: 2005
  end-page: 42600
  ident: bib7
  article-title: Role of histone modifications in marking and activating genes through mitosis
  publication-title: J. Biol. Chem.
– volume: 403
  start-page: 41
  year: 2000
  end-page: 45
  ident: bib2
  article-title: The language of covalent histone modifications
  publication-title: Nature
– volume: 117
  start-page: 721
  year: 2004
  end-page: 733
  ident: bib13
  article-title: Mapping global histone acetylation patterns to gene expression
  publication-title: Cell
– volume: 3
  start-page: e328
  year: 2005
  ident: bib14
  article-title: Single-nucleosome mapping of histone modifications in
  publication-title: PLoS Biol.
– volume: 112
  start-page: 77
  year: 2003
  end-page: 86
  ident: bib4
  article-title: Identification of novel histone post-translational modifications by peptide mass fingerprinting
  publication-title: Chromosoma
– volume: 19
  start-page: 381
  year: 2005
  end-page: 391
  ident: bib37
  article-title: Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin
  publication-title: Mol. Cell
– volume: 441
  start-page: 349
  year: 2006
  end-page: 353
  ident: bib26
  article-title: Polycomb complexes repress developmental regulators in murine embryonic stem cells
  publication-title: Nature
– volume: 62
  start-page: 6456
  year: 2002
  end-page: 6461
  ident: bib44
  article-title: Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2′-deoxycytidine
  publication-title: Cancer Res.
– volume: 435
  start-page: 1262
  year: 2005
  end-page: 1266
  ident: bib47
  article-title: Global histone modification patterns predict risk of prostate cancer recurrence
  publication-title: Nature
– volume: 23
  start-page: 206
  year: 2003
  end-page: 215
  ident: bib45
  article-title: Critical role of histone methylation in tumor suppressor gene silencing in colorectal cancer
  publication-title: Mol. Cell. Biol.
– volume: 276
  start-page: 337
  year: 2004
  ident: 10.1016/j.bbagen.2008.12.006_bib28
  article-title: Distinct dynamics and distribution of histone methyl-lysine derivatives in mouse development
  publication-title: Dev. Biol.
  doi: 10.1016/j.ydbio.2004.08.038
– volume: 280
  start-page: 42592
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib7
  article-title: Role of histone modifications in marking and activating genes through mitosis
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M507407200
– volume: 21
  start-page: 608
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib62
  article-title: Genome-wide analysis of HDAC function
  publication-title: Trends Genet.
  doi: 10.1016/j.tig.2005.08.009
– volume: 7
  start-page: 24
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib19
  article-title: Chromatin remodeling agent trichostatin A: a key-factor in the hepatic differentiation of human mesenchymal stem cells derived of adult bone marrow
  publication-title: BMC Dev. Biol.
  doi: 10.1186/1471-213X-7-24
– volume: 125
  start-page: 301
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib24
  article-title: Control of developmental regulators by Polycomb in human embryonic stem cells
  publication-title: Cell
  doi: 10.1016/j.cell.2006.02.043
– volume: 23
  start-page: 206
  year: 2003
  ident: 10.1016/j.bbagen.2008.12.006_bib45
  article-title: Critical role of histone methylation in tumor suppressor gene silencing in colorectal cancer
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.23.1.206-215.2003
– volume: 5
  start-page: 65
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib54
  article-title: 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
  publication-title: Cancer Biol. Ther.
  doi: 10.4161/cbt.5.1.2288
– volume: 61
  start-page: 8492
  year: 2001
  ident: 10.1016/j.bbagen.2008.12.006_bib20
  article-title: The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
  publication-title: Cancer Res.
– volume: 22
  start-page: 836
  year: 2000
  ident: 10.1016/j.bbagen.2008.12.006_bib3
  article-title: Histone acetylation and an epigenetic code
  publication-title: BioEssays
  doi: 10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X
– volume: 27
  start-page: 1180
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib55
  article-title: Histone H3 lysine 9 and H4 lysine 20 trimethylation and the expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in hepatocarcinogenesis induced by methyl deficiency in rats
  publication-title: Carcinogenesis
  doi: 10.1093/carcin/bgi364
– volume: 438
  start-page: 1116
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib32
  article-title: Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
  publication-title: Nature
  doi: 10.1038/nature04219
– volume: 125
  start-page: 315
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib29
  article-title: A bivalent chromatin structure marks key developmental genes in embryonic stem cells
  publication-title: Cell
  doi: 10.1016/j.cell.2006.02.041
– volume: 7
  start-page: 583
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib63
  article-title: Development of histone deacetylase inhibitors for cancer treatment
  publication-title: Expert Rev. Anticancer Ther.
  doi: 10.1586/14737140.7.4.583
– volume: 130
  start-page: 77
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib60
  article-title: A chromatin landmark and transcription initiation at most promoters in human cells
  publication-title: Cell
  doi: 10.1016/j.cell.2007.05.042
– volume: 3
  start-page: e328
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib14
  article-title: Single-nucleosome mapping of histone modifications in S. cerevisiae
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.0030328
– volume: 117
  start-page: 721
  year: 2004
  ident: 10.1016/j.bbagen.2008.12.006_bib13
  article-title: Mapping global histone acetylation patterns to gene expression
  publication-title: Cell
  doi: 10.1016/j.cell.2004.05.023
– volume: 403
  start-page: 41
  year: 2000
  ident: 10.1016/j.bbagen.2008.12.006_bib2
  article-title: The language of covalent histone modifications
  publication-title: Nature
  doi: 10.1038/47412
– volume: 441
  start-page: 349
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib26
  article-title: Polycomb complexes repress developmental regulators in murine embryonic stem cells
  publication-title: Nature
  doi: 10.1038/nature04733
– volume: 112
  start-page: 77
  year: 2003
  ident: 10.1016/j.bbagen.2008.12.006_bib4
  article-title: Identification of novel histone post-translational modifications by peptide mass fingerprinting
  publication-title: Chromosoma
  doi: 10.1007/s00412-003-0244-6
– volume: 62
  start-page: 6456
  year: 2002
  ident: 10.1016/j.bbagen.2008.12.006_bib44
  article-title: Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2′-deoxycytidine
  publication-title: Cancer Res.
– volume: 10
  start-page: 105
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib23
  article-title: Hyperdynamic plasticity of chromatin proteins in pluripotent embryonic stem cells
  publication-title: Dev. Cell
  doi: 10.1016/j.devcel.2005.10.017
– volume: 6
  start-page: 113
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib11
  article-title: Histone modifications: from genome-wide maps to functional insights
  publication-title: Genome Biol.
  doi: 10.1186/gb-2005-6-6-113
– volume: 1789
  start-page: 37
  year: 2009
  ident: 10.1016/j.bbagen.2008.12.006_bib16
  article-title: The role of histone H2A and H2B post-translational modifications in transcription: a genomic perspective
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbagrm.2008.07.001
– volume: 20
  start-page: 3110
  year: 2001
  ident: 10.1016/j.bbagen.2008.12.006_bib21
  article-title: Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1204336
– volume: 453
  start-page: 812
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib34
  article-title: Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
  publication-title: Nature
  doi: 10.1038/nature06906
– volume: 26
  start-page: 4974
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib52
  article-title: Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in Drosophila
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7601926
– volume: 5
  start-page: 367
  year: 2000
  ident: 10.1016/j.bbagen.2008.12.006_bib53
  article-title: Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila
  publication-title: Mol. Cell
  doi: 10.1016/S1097-2765(00)80431-1
– volume: 15
  start-page: 550
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib33
  article-title: Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1432
– volume: 451
  start-page: 734
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib9
  article-title: Cell cycle control of centromeric repeat transcription and heterochromatin assembly
  publication-title: Nature
  doi: 10.1038/nature06561
– volume: 123
  start-page: 233
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib15
  article-title: Histone variant H2A.Z marks the 5′ ends of both active and inactive genes in euchromatin
  publication-title: Cell
  doi: 10.1016/j.cell.2005.10.002
– volume: 40
  start-page: 897
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib12
  article-title: Combinatorial patterns of histone acetylations and methylations in the human genome
  publication-title: Nat. Genet.
  doi: 10.1038/ng.154
– volume: 126
  start-page: 105
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib38
  article-title: The role of epigenetics in mental disorders
  publication-title: Indian J. Med. Res.
– volume: 67
  start-page: 10657
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib59
  article-title: A polycomb repression signature in metastatic prostate cancer predicts cancer outcome
  publication-title: Cancer Res.
  doi: 10.1158/0008-5472.CAN-07-2498
– volume: 15
  start-page: 542
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib35
  article-title: Simplifying a complex code
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb0608-542
– volume: 7
  start-page: 21
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib41
  article-title: The epigenetic progenitor origin of human cancer
  publication-title: Nat. Rev. Genet.
  doi: 10.1038/nrg1748
– volume: 25
  start-page: 4358
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib57
  article-title: Global histone modifications predict prognosis of resected non small-cell lung cancer
  publication-title: J. Clin. Oncol.
  doi: 10.1200/JCO.2007.11.2599
– volume: 39
  start-page: 237
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib42
  article-title: A stem cell-like chromatin pattern may predispose tumor suppressor genes to DNA hypermethylation and heritable silencing
  publication-title: Nat. Genet.
  doi: 10.1038/ng1972
– volume: 20
  start-page: 1123
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib25
  article-title: Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions
  publication-title: Genes Dev.
  doi: 10.1101/gad.381706
– volume: 66
  start-page: 3541
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib31
  article-title: Silenced tumor suppressor genes reactivated by DNA demethylation do not return to a fully euchromatic chromatin state
  publication-title: Cancer Res.
  doi: 10.1158/0008-5472.CAN-05-2481
– volume: 24
  start-page: 347
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib6
  article-title: Histone modifications defining active genes persist after transcriptional and mitotic inactivation
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7600516
– volume: 65
  start-page: 1505
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib18
  article-title: Histone deacetylase inhibitor valproic acid enhances the cytokine-induced expansion of human hematopoietic stem cells
  publication-title: Cancer Res.
  doi: 10.1158/0008-5472.CAN-04-3063
– volume: 119
  start-page: 603
  year: 2004
  ident: 10.1016/j.bbagen.2008.12.006_bib27
  article-title: Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
  publication-title: Cell
  doi: 10.1016/j.cell.2004.11.009
– volume: 19
  start-page: 381
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib37
  article-title: Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2005.06.011
– volume: 37
  start-page: 391
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib49
  article-title: Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
  publication-title: Nat. Genet.
  doi: 10.1038/ng1531
– volume: 435
  start-page: 1262
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib47
  article-title: Global histone modification patterns predict risk of prostate cancer recurrence
  publication-title: Nature
  doi: 10.1038/nature03672
– volume: 28
  start-page: 397
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib56
  article-title: The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.01045-07
– volume: 8
  start-page: 31
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib8
  article-title: Exploring cellular memory molecules marking competent and active transcriptions
  publication-title: BMC Mol. Biol.
  doi: 10.1186/1471-2199-8-31
– volume: 24
  start-page: 2906
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib51
  article-title: Genomewide analysis of nucleosome density histone acetylation and HDAC function in fission yeast
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7600758
– volume: 62
  start-page: 7213
  year: 2002
  ident: 10.1016/j.bbagen.2008.12.006_bib43
  article-title: Dependence of histone modifications and gene expression on DNA hypermethylation in cancer
  publication-title: Cancer Res.
– volume: 92
  start-page: 542
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib64
  article-title: Effect of histone deacetylase inhibitor valproic acid on progenitor cells of acute myeloid leukemia
  publication-title: Haematologica
  doi: 10.3324/haematol.10758
– volume: 311
  start-page: 844
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib50
  article-title: Histone H4-K16 acetylation controls chromatin structure and protein interactions
  publication-title: Science
  doi: 10.1126/science.1124000
– volume: 11
  start-page: 66
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib10
  article-title: Characterization of histones and their post-translational modifications by mass spectrometry
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/j.cbpa.2006.11.022
– volume: 63
  start-page: 1009
  year: 2006
  ident: 10.1016/j.bbagen.2008.12.006_bib22
  article-title: Epigenetic mechanisms: a common theme in vertebrate and invertebrate memory formation
  publication-title: Cell Mol. Life Sci.
  doi: 10.1007/s00018-006-6026-6
– volume: 24
  start-page: 5710
  year: 2004
  ident: 10.1016/j.bbagen.2008.12.006_bib30
  article-title: Histone code modifications on pluripotential nuclei of reprogrammed somatic cells
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.24.13.5710-5720.2004
– volume: 100
  start-page: 11606
  year: 2003
  ident: 10.1016/j.bbagen.2008.12.006_bib58
  article-title: EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1933744100
– volume: 99
  start-page: 908
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib48
  article-title: Epigenetic events, remodelling enzymes and their relationship to chromatin organization in prostatic intraepithelial neoplasia and prostatic adenocarcinoma
  publication-title: BJU Int.
  doi: 10.1111/j.1464-410X.2006.06704.x
– volume: 267
  start-page: 68
  year: 1992
  ident: 10.1016/j.bbagen.2008.12.006_bib1
  article-title: Histones as regulators of genes
  publication-title: Sci. Am.
  doi: 10.1038/scientificamerican1092-68
– volume: 8
  start-page: 434
  year: 2005
  ident: 10.1016/j.bbagen.2008.12.006_bib40
  article-title: The epigenetic control of antigenic variation in Plasmodium falciparum
  publication-title: Curr. Opin. Microbiol.
  doi: 10.1016/j.mib.2005.06.007
– volume: 15
  start-page: 1968
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib46
  article-title: The global histone modification pattern correlates with cancer recurrence and overall survival in gastric adenocarcinoma
  publication-title: Ann. Surg. Oncol.
  doi: 10.1245/s10434-008-9927-9
– volume: 38
  start-page: 32
  year: 2004
  ident: 10.1016/j.bbagen.2008.12.006_bib17
  article-title: Histone deacetylase activity is required for embryonic stem cell differentiation
  publication-title: Genesis
  doi: 10.1002/gene.10250
– volume: 18
  start-page: 1263
  year: 2004
  ident: 10.1016/j.bbagen.2008.12.006_bib61
  article-title: The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
  publication-title: Genes Dev.
  doi: 10.1101/gad.1198204
– volume: 447
  start-page: 396
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib5
  article-title: Perceptions of epigenetics
  publication-title: Nature
  doi: 10.1038/nature05913
– volume: 14
  start-page: 7
  year: 2007
  ident: 10.1016/j.bbagen.2008.12.006_bib39
  article-title: Mechanisms of disease: epigenesis
  publication-title: Semin. Pediatr. Neurol.
  doi: 10.1016/j.spen.2006.11.004
– volume: 27
  start-page: 2412
  year: 2008
  ident: 10.1016/j.bbagen.2008.12.006_bib36
  article-title: Differentially expressed genes are marked by histone 3 lysine 9 trimethylation in human cancer cells
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1210895
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Snippet The eukaryotic DNA is wrapped around histone octamers, which consist of four different histones, H2A, H2B, H3 and H4. The N-terminal tail of each histone is...
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SubjectTerms Animals
Cancer
Cell Differentiation
Chromatin
Epigenesis, Genetic
Epigenetic
Histone code
Histone modification
Histones - metabolism
Humans
Neoplasms - etiology
Title Histone modification patterns and epigenetic codes
URI https://dx.doi.org/10.1016/j.bbagen.2008.12.006
https://www.ncbi.nlm.nih.gov/pubmed/19168116
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