{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T23:53:17Z","timestamp":1767829997404,"version":"3.49.0"},"reference-count":103,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2009,2,1]],"date-time":"2009-02-01T00:00:00Z","timestamp":1233446400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Genetics and Genomics"],"published-print":{"date-parts":[[2009,2]]},"DOI":"10.1016\/s1673-8527(08)60094-6","type":"journal-article","created":{"date-parts":[[2009,2,14]],"date-time":"2009-02-14T10:11:32Z","timestamp":1234606292000},"page":"75-88","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":99,"title":["Histone modifications dictate specific biological readouts"],"prefix":"10.1016","volume":"36","author":[{"given":"Anjana","family":"Munshi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gowhar","family":"Shafi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nishat","family":"Aliya","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akka","family":"Jyothy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S1673-8527(08)60094-6_bib1","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0092-8674(02)01077-2","article-title":"Deciphering the transcriptional histone acetylation code for a human gene","volume":"111","author":"Agalioti","year":"2002","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib2","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1073\/pnas.51.5.786","article-title":"Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis","volume":"51","author":"Allfrey","year":"1964","journal-title":"Proc. Natl. Acad Sci. USA"},{"key":"10.1016\/S1673-8527(08)60094-6_bib3","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0014-5793(03)00451-4","article-title":"MAP kinase mediated phosphorylation of histone H3 and inducible gene regulation","volume":"546","author":"Allison","year":"2003","journal-title":"FEBS lett."},{"key":"10.1016\/S1673-8527(08)60094-6_bib4","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.mrfmmm.2006.09.009","article-title":"Histone modifications in response to DNA damage","volume":"618","author":"Altaf","year":"2007","journal-title":"Mutat. Res."},{"key":"10.1016\/S1673-8527(08)60094-6_bib5","doi-asserted-by":"crossref","first-page":"6470","DOI":"10.1128\/MCB.21.19.6470-6483.2001","article-title":"ETO, a target of t (8;21) in acute leukemia, makes distinct contact with multiple histones deacetylase and binds mSin3A through its oligomerization domain","volume":"21","author":"Amann","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib6","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/S0092-8674(03)01023-7","article-title":"Plasmodium biology: Genomic gleanings","volume":"115","author":"Aravind","year":"2003","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib7","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/S0959-437X(02)00279-4","article-title":"Histone modifications in transcriptional regulation","volume":"12","author":"Berger","year":"2002","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib8","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nature05915","article-title":"The complex language of chromatin regulation during transcription","volume":"447","author":"Berger","year":"2007","journal-title":"Nature"},{"key":"10.1016\/S1673-8527(08)60094-6_bib9","doi-asserted-by":"crossref","first-page":"E5","DOI":"10.1371\/journal.pbio.0000005","article-title":"The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum","volume":"1","author":"Bozdech","year":"2003","journal-title":"PLoS Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib10","doi-asserted-by":"crossref","first-page":"3286","DOI":"10.1101\/gad.940201","article-title":"Histone H3 lysine 4 methylation is mediated by Set 1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae","volume":"15","author":"Briggs","year":"2001","journal-title":"Genes Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib11","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/S0959-437X(96)80048-7","article-title":"Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation","volume":"6","author":"Brownell","year":"1996","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib12","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0960-9822(01)00652-2","article-title":"Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism","volume":"12","author":"Bryk","year":"2002","journal-title":"Curr. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib13","doi-asserted-by":"crossref","first-page":"2257","DOI":"10.1111\/j.1432-1033.2004.04167.x","article-title":"K8 and K12 are biotinylated in human histone H4","volume":"271","author":"Camporeale","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib14","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/S0168-9525(03)00115-X","article-title":"The diverse functions of histone acetyltransferase complexes","volume":"19","author":"Carrozza","year":"2003","journal-title":"Trends Genet."},{"key":"10.1016\/S1673-8527(08)60094-6_bib15","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1038\/ncb1004","article-title":"Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks","volume":"5","author":"Celeste","year":"2003","journal-title":"Nat. Cell. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib16","doi-asserted-by":"crossref","first-page":"9009","DOI":"10.1158\/0008-5472.CAN-06-0101","article-title":"Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells","volume":"66","author":"Chen","year":"2006","journal-title":"Cancer Res."},{"key":"10.1016\/S1673-8527(08)60094-6_bib17","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0003-9861(02)00564-7","article-title":"The acetylation of in Drosophilla melanogaster","volume":"408","author":"Chen","year":"2002","journal-title":"Archives Biochem. Bioph."},{"key":"10.1016\/S1673-8527(08)60094-6_bib18","first-page":"295","article-title":"Roles of dynamic and reversible histone acetylation in plant development and polyploidy","volume":"1769","author":"Chen","year":"2007","journal-title":"Biochem. Biophys. Acta"},{"key":"10.1016\/S1673-8527(08)60094-6_bib19","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0092-8674(00)00118-5","article-title":"Signaling to chromatin through histone modifications","volume":"103","author":"Cheung","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib20","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1016\/S1471-4914(02)02303-1","article-title":"Histone modification: The \u2018next wave\u2019 in cancer therapeutics","volume":"8","author":"Chung","year":"2002","journal-title":"Trends Mol. Med."},{"key":"10.1016\/S1673-8527(08)60094-6_bib21","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.molcel.2006.06.017","article-title":"Enhanced histone acetylation and transcription: A dynamic perspective","volume":"23","author":"Clayton","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib22","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1128\/MCB.22.3.874-885.2002","article-title":"Mitotic phosphorylation of histone H3: Spatio-temporal regulation by mammalian Aurora kinases","volume":"22","author":"Crosio","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib23","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0959-437X(98)80138-X","article-title":"Covalent modifications of histones: Expression from chromatin templates","volume":"8","author":"Davie","year":"1998","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib24","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/S0168-9525(02)02648-3","article-title":"Unraveling heterochromatin: Competition between positive and negative factors regulates accessibility","volume":"18","author":"Dillon","year":"2002","journal-title":"Trends Genet."},{"key":"10.1016\/S1673-8527(08)60094-6_bib25","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1083\/jcb.200202131","article-title":"Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin","volume":"158","author":"Dou","year":"2002","journal-title":"J. Cell Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib26","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S1097-2765(00)00024-1","article-title":"Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch","volume":"6","author":"Dou","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib27","doi-asserted-by":"crossref","first-page":"6142","DOI":"10.1073\/pnas.092029599","article-title":"Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites","volume":"99","author":"Dou","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1673-8527(08)60094-6_bib28","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/S1097-2765(00)80215-4","article-title":"Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal","volume":"4","author":"Dou","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib29","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1016\/j.molcel.2004.12.003","article-title":"Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites","volume":"16","author":"Downs","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib30","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1038\/35050000","article-title":"A role for Saccharomyces cerevisiae histone H2A in DNA repair","volume":"408","author":"Downs","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S1673-8527(08)60094-6_bib31","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/S0092-8674(00)80492-4","article-title":"Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres","volume":"91","author":"Ekwall","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib32","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1038\/ncb884","article-title":"DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1","volume":"4","author":"Fernandez-Capetillo","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib33","doi-asserted-by":"crossref","first-page":"2032","DOI":"10.1021\/pr050188r","article-title":"Resetting the epigenetic histone code in the MRL-lpr\/lpr mouse model of lupus by histone deacetylase inhibition","volume":"4","author":"Garcia","year":"2005","journal-title":"J. Proteome Res."},{"key":"10.1016\/S1673-8527(08)60094-6_bib34","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1083\/jcb.152.4.669","article-title":"Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis","volume":"152","author":"Giet","year":"2001","journal-title":"J. Cell Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib35","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/38664","article-title":"Histone acetylation in chromatin structure and transcription","volume":"389","author":"Grunstein","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S1673-8527(08)60094-6_bib36","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1534\/genetics.104.038570","article-title":"Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair","volume":"170","author":"Harvey","year":"2005","journal-title":"Genetics"},{"key":"10.1016\/S1673-8527(08)60094-6_bib37","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0092-8674(01)00598-0","article-title":"Methylation of histone H3 at Lys-9 is an early mark on the X chromosome during X inactivation","volume":"107","author":"Heard","year":"2001","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib38","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1002\/j.1460-2075.1988.tb02956.x","article-title":"A direct link between core histone acetylation and transcriptionally active chromatin","volume":"7","author":"Hebbes","year":"1988","journal-title":"EMBO J."},{"key":"10.1016\/S1673-8527(08)60094-6_bib39","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/0161-5890(89)90143-0","article-title":"A \u2018minimal epitope\u2019 anti-protein antibody that recognizes a single modified amino-acid","volume":"26","author":"Hebbes","year":"1989","journal-title":"Mol. Immunol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib40","doi-asserted-by":"crossref","first-page":"13587","DOI":"10.1074\/jbc.M011196200","article-title":"Decreased expression of specific genes in yeast cells lacking histone H1","volume":"276","author":"Hellauer","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib41","doi-asserted-by":"crossref","first-page":"2711","DOI":"10.1007\/s00018-005-5287-9","article-title":"Heterochromatin protein 1: A pervasive controlling influence","volume":"62","author":"Hiragami","year":"2005","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/S1673-8527(08)60094-6_bib42","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/BF00223526","article-title":"Phosphorylation of H1 histones","volume":"57","author":"Hohmann","year":"1983","journal-title":"Mol. Cell Biochem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib43","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1038\/nature03114","article-title":"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks","volume":"432","author":"Huyen","year":"2004","journal-title":"Nature"},{"key":"10.1016\/S1673-8527(08)60094-6_bib44","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1006\/bmme.1995.1059","article-title":"Biotinylation of histones by human serum biotinidase: Assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency","volume":"56","author":"Hymes","year":"1995","journal-title":"Biochem. Mol. Med."},{"key":"10.1016\/S1673-8527(08)60094-6_bib45","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/S0959-437X(03)00020-0","article-title":"Functional consequences of histone modifications","volume":"13","author":"Iizuka","year":"2003","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib46","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/S0962-8924(01)02001-3","article-title":"Re-SET-ting heterochromatin by histone methyltransferases","volume":"11","author":"Jenuwein","year":"2001","journal-title":"Trends Cell. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib47","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1126\/science.1063127","article-title":"Translating the histone code","volume":"293","author":"Jenuwein","year":"2001","journal-title":"Science"},{"key":"10.1016\/S1673-8527(08)60094-6_bib48","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/0092-8674(93)90419-Q","article-title":"The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression","volume":"74","author":"Jeppesen","year":"1993","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib49","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1101\/gad.1272805","article-title":"Histone variants: Deviants?","volume":"19","author":"Kamakaka","year":"2005","journal-title":"Genes Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib50","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0168-9525(02)02746-4","article-title":"Connecting the DOTs: Covalent histone modifications and the formation of silent chromatin","volume":"18","author":"Khan","year":"2000","journal-title":"Trends Genet."},{"key":"10.1016\/S1673-8527(08)60094-6_bib51","first-page":"A55","article-title":"Biotinylation of histones depends on the cell cycle in NCI-H69 small cell lung cancer cells","volume":"19","author":"Kothapalli","year":"2005","journal-title":"FASEB J."},{"key":"10.1016\/S1673-8527(08)60094-6_bib52","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1016\/j.jnutbio.2005.03.025","article-title":"Biological functions of biotinylated histones","volume":"16","author":"Kothapalli","year":"2005","journal-title":"J. Nutr. Biochem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib53","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1002\/(SICI)1521-1878(199808)20:8<615::AID-BIES4>3.0.CO;2-H","article-title":"Roles of histone acetyltranferases and deacetylases in gene regulation","volume":"20","author":"Kou","year":"1998","journal-title":"Bioessays"},{"key":"10.1016\/S1673-8527(08)60094-6_bib54","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/S0955-0674(02)00335-6","article-title":"The many faces of histone lysine methylation","volume":"14","author":"Lachner","year":"2002","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib55","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0960-9822(02)00660-7","article-title":"Histone H3 lysine 9 methylation occurs rapidly at the onset of random X chromosome inactivation","volume":"12","author":"Mermoud","year":"2002","journal-title":"Curr. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib56","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.gene.2005.10.022","article-title":"The malaria parasite Plasmodium falciparum histones: Organization, expression, and acetylation","volume":"369","author":"Miao","year":"2006","journal-title":"Gene"},{"key":"10.1016\/S1673-8527(08)60094-6_bib57","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1006\/bbrc.1996.5903","article-title":"Major role of the histone H3-H4 in the folding of the chromatin fiber","volume":"230","author":"Moore","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1673-8527(08)60094-6_bib58","doi-asserted-by":"crossref","first-page":"6215","DOI":"10.1128\/MCB.24.14.6215-6230.2004","article-title":"Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast","volume":"24","author":"Nakamura","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib59","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1093\/hmg\/ddh006","article-title":"Reduced histone biotinylation in multiple carboxylase deficiency patients: A nuclear role for holocarboxylase synthetase","volume":"13","author":"Narang","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/S1673-8527(08)60094-6_bib60","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/S1357-2725(02)00079-1","article-title":"Senescence and epigenetic dysregulation in cancer","volume":"34","author":"Neumeister","year":"2002","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib61","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1038\/sj.bjc.6600554","article-title":"Mutation analysis of CBP and PCAF reveals rare inactivating mutations in cancer cell lines but not in primary tumours","volume":"87","author":"Ozdag","year":"2002","journal-title":"Br. J. Cancer"},{"key":"10.1016\/S1673-8527(08)60094-6_bib62","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0092-8674(00)81325-2","article-title":"The major cytoplasmic histone acetylatransferase in yeast: Links to chromatin replication and histone metabolism","volume":"87","author":"Parthun","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib63","doi-asserted-by":"crossref","first-page":"C878","DOI":"10.1152\/ajpcell.00107.2002","article-title":"Exposure to UV light causes increased biotinylation of histones in Jurkat cells","volume":"283","author":"Peters","year":"2002","journal-title":"Am. J. Cell Physiol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib64","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1101\/gad.1182704","article-title":"Cellular machineries for chromosomal DNA repair","volume":"18","author":"Peterson","year":"2004","journal-title":"Genes. Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib65","doi-asserted-by":"crossref","first-page":"R546","DOI":"10.1016\/j.cub.2004.07.007","article-title":"Histones and histone modifications","volume":"14","author":"Peterson","year":"2004","journal-title":"Curr. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib66","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1007\/s00436-003-0874-x","article-title":"The histone H4 gene of Plasmodium falciparum is developmentally transcribed in asexual parasites","volume":"90","author":"Przyborski","year":"2003","journal-title":"Parasitol. Res."},{"key":"10.1016\/S1673-8527(08)60094-6_bib67","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1016\/S1097-2765(01)00269-6","article-title":"Histone H2A.Z acetylation modulates an essential charge patch","volume":"7","author":"Ren","year":"2001","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib68","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1016\/S1097-2765(03)00479-9","article-title":"Histone methyltransferases direct different degrees of methylation of define distinct chromatin domains","volume":"12","author":"Rice","year":"2003","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib69","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1126\/science.287.5452.501","article-title":"Rad6-dependent ubiquitination of histone H2B in yeast","volume":"287","author":"Robzyk","year":"2000","journal-title":"Science"},{"key":"10.1016\/S1673-8527(08)60094-6_bib70","doi-asserted-by":"crossref","first-page":"5858","DOI":"10.1074\/jbc.273.10.5858","article-title":"DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139","volume":"27","author":"Rogakou","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib71","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0968-0004(92)90243-3","article-title":"Chromatinacondensation. Does H1 dephosphorylation play a role?","volume":"17","author":"Roth","year":"1992","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/S1673-8527(08)60094-6_bib72","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1146\/annurev.biochem.70.1.81","article-title":"Histone acetylatransferases","volume":"70","author":"Roth","year":"2001","journal-title":"Ann. Rev. Biochem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib73","doi-asserted-by":"crossref","first-page":"2381","DOI":"10.1016\/j.ejca.2005.08.010","article-title":"Chromatin modifier enzymes, the histone code and cancer","volume":"41","author":"Rosa","year":"2005","journal-title":"Eur. J. Cancer"},{"key":"10.1016\/S1673-8527(08)60094-6_bib74","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nature01080","article-title":"Active genes are tri-methylated at K4 of histone H3","volume":"419","author":"Rosa","year":"2002","journal-title":"Nature"},{"key":"10.1016\/S1673-8527(08)60094-6_bib75","first-page":"A103","article-title":"Biotinylation of human Histone H3 and interactions with biotinidase","volume":"18","author":"Sarath","year":"2004","journal-title":"FASEB J."},{"key":"10.1016\/S1673-8527(08)60094-6_bib76","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1038\/nrg2218","article-title":"Histone lysine demethylases emerging roles in development, physiology and disease","volume":"8","author":"Shi","year":"2007","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/S1673-8527(08)60094-6_bib77","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/j.cell.2004.12.012","article-title":"Histone demethylation mediated by the nuclear amine oxidase homolog LSD1","volume":"1197","author":"Shi","year":"2004","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib78","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1016\/j.cub.2004.09.047","article-title":"Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break","volume":"14","author":"Shroff","year":"2004","journal-title":"Curr. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib79","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1101\/gad.1536807","article-title":"Functional cooperation Hp1 and DNMT 1 mediates gene silencing","volume":"21","author":"Smallwood","year":"2007","journal-title":"Genes Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib80","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/j.ctrv.2004.04.006","article-title":"Histone deacetylase inhibitors?a new tool to treat cancer","volume":"30","author":"Somech","year":"2004","journal-title":"Cancer Treat. Rev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib81","first-page":"5424","article-title":"Biotinylation of histones in human cells: Effects of cell proliferation","volume":"268","author":"Stanley","year":"2001","journal-title":"FEBS J."},{"key":"10.1016\/S1673-8527(08)60094-6_bib82","doi-asserted-by":"crossref","first-page":"2390","DOI":"10.1158\/0008-5472.CAN-03-3207","article-title":"ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation","volume":"64","author":"Stiff","year":"2004","journal-title":"Cancer Res."},{"key":"10.1016\/S1673-8527(08)60094-6_bib83","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/47412","article-title":"The language of covalent histone modifications","volume":"403","author":"Strahl","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S1673-8527(08)60094-6_bib84","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/j.molcel.2004.11.026","article-title":"Postreplicative recruitment of cohesin to double-stranded breaks in required for DNA repair","volume":"16","author":"Strom","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib85","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.ijms.2006.07.009","article-title":"Hunting for post-translational modifications that underline the histone code","volume":"259","author":"Taverna","year":"2007","journal-title":"Int. J. Mass Spectrom."},{"key":"10.1016\/S1673-8527(08)60094-6_bib86","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/j.molcel.2005.05.008","article-title":"Chromatin in need of a fix: Phosphorylation of H2AX connects chromatin to DNA repair","volume":"18","author":"Thiriet","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib87","doi-asserted-by":"crossref","first-page":"11381","DOI":"10.1021\/bi970801n","article-title":"Hybrid trypsinized nucleosomal arrays: Identification of multiple functional roles of the H2A\/H2B and H3\/H4 N-termini in chromatin fibre compaction","volume":"36","author":"Tse","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S1673-8527(08)60094-6_bib88","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/S0092-8674(05)80078-9","article-title":"Decoding the nucleosome","volume":"75","author":"Turner","year":"1993","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib89","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/0092-8674(92)90417-B","article-title":"Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei","volume":"69","author":"Turner","year":"1992","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib90","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.ijms.2006.09.001","article-title":"Deciphering the histone code using mass spectrometry","volume":"259","author":"Ueberheide","year":"2007","journal-title":"Int. J. Mass Spectrom."},{"key":"10.1016\/S1673-8527(08)60094-6_bib91","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1016\/j.molcel.2004.11.027","article-title":"DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain","volume":"16","author":"Unal","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib92","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1038\/nrm1737","article-title":"The histone code at DNA breaks: A guide to repair?","volume":"6","author":"van Attikum","year":"2005","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib93","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/S0092-8674(02)00759-6","article-title":"Dot1p modulates silencing in yeast by methylation of nucleosome core","volume":"109","author":"van Leeuwen","year":"2002","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib94","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/S0960-9822(98)70040-5","article-title":"Nucleosomal DNA regulates the core\u2013histone-binding subunit of the human Hat1 acetyltranferases","volume":"8","author":"Varreault","year":"1998","journal-title":"Curr. Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib95","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/S0168-9525(03)00073-8","article-title":"Class II histone deacetylases: Versatile regulators","volume":"19","author":"Verdin","year":"2003","journal-title":"Trends Genet."},{"key":"10.1016\/S1673-8527(08)60094-6_bib96","doi-asserted-by":"crossref","first-page":"4912","DOI":"10.1016\/S0021-9258(18)53482-7","article-title":"Histone synthesis and turnover in alfalfa. Fast loss of highly acetylated replacement histone variant H3","volume":"268","author":"Waterborg","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1673-8527(08)60094-6_bib97","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.cell.2006.03.028","article-title":"Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases","volume":"125","author":"Whetstine","year":"2006","journal-title":"Cell"},{"key":"10.1016\/S1673-8527(08)60094-6_bib98","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/S1471-4892(01)00060-1","article-title":"Scoring a bull's-eye against cancer genome targets","volume":"1","author":"Workman","year":"2001","journal-title":"Curr. Opin. Pharmacol,"},{"key":"10.1016\/S1673-8527(08)60094-6_bib99","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.ceb.2006.02.008","article-title":"Histone post translational modifications and the response to DNA double strands breaks","volume":"18","author":"Wurtele","year":"2006","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/S1673-8527(08)60094-6_bib100","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1093\/genetics\/164.1.47","article-title":"Multiple roles for Saccharomyces cerevisiae histone H2A in telomere position effect, Spt phenotypes and double-strand break repair","volume":"164","author":"Wyatt","year":"2003","journal-title":"Genetics"},{"key":"10.1016\/S1673-8527(08)60094-6_bib101","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/400_010","article-title":"Structure and function of protein modules in chromatin biology","volume":"41","author":"Yap","year":"2006","journal-title":"Results. Probl. Cell Differ."},{"key":"10.1016\/S1673-8527(08)60094-6_bib102","doi-asserted-by":"crossref","first-page":"2343","DOI":"10.1101\/gad.927301","article-title":"Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails","volume":"15","author":"Zhang","year":"2001","journal-title":"Genes Dev."},{"key":"10.1016\/S1673-8527(08)60094-6_bib103","doi-asserted-by":"crossref","first-page":"2782","DOI":"10.1128\/MCB.26.7.2782-2790.2006","article-title":"Acetylation of p53 at lysine373\/382 by the histone deacetylase inhibitor Depsipeptide induces expression of p21Waf1\/Cip1","volume":"26","author":"Zhao","year":"2006","journal-title":"Mol. Cell. Biol."}],"container-title":["Journal of Genetics and Genomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1673852708600946?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1673852708600946?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T11:21:14Z","timestamp":1761650474000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1673852708600946"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,2]]},"references-count":103,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2009,2]]}},"alternative-id":["S1673852708600946"],"URL":"https:\/\/doi.org\/10.1016\/s1673-8527(08)60094-6","relation":{},"ISSN":["1673-8527"],"issn-type":[{"value":"1673-8527","type":"print"}],"subject":[],"published":{"date-parts":[[2009,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Histone modifications dictate specific biological readouts","name":"articletitle","label":"Article Title"},{"value":"Journal of Genetics and Genomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/S1673-8527(08)60094-6","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2009 Institute of Genetics and Developmental Biology and the Genetics Society of China. Published by Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}