{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,9]],"date-time":"2026-04-09T15:02:49Z","timestamp":1775746969288,"version":"3.50.1"},"reference-count":61,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2002,4,1]],"date-time":"2002-04-01T00:00:00Z","timestamp":1017619200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Opinion in Genetics &amp; Development"],"published-print":{"date-parts":[[2002,4]]},"DOI":"10.1016\/s0959-437x(02)00279-4","type":"journal-article","created":{"date-parts":[[2002,10,8]],"date-time":"2002-10-08T15:17:01Z","timestamp":1034090221000},"page":"142-148","source":"Crossref","is-referenced-by-count":949,"title":["Histone modifications in transcriptional regulation"],"prefix":"10.1016","volume":"12","author":[{"given":"Shelley L","family":"Berger","sequence":"first","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0959-437X(02)00279-4_BIB1","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 acetyltransferases and deacetylases in gene regulation","volume":"20","author":"Kuo","year":"1998","journal-title":"BioEssays"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB2","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1128\/MMBR.64.2.435-459.2000","article-title":"Acetylation of histones and transcription-related factors","volume":"64","author":"Sterner","year":"2000","journal-title":"Microbiol Mol Biol Rev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB3","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1146\/annurev.biochem.70.1.81","article-title":"Histone acetyltransferases","volume":"70","author":"Roth","year":"2001","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB4","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\/S0959-437X(02)00279-4_BIB5","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1002\/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X","article-title":"Histone acetylation and an epigenetic code","volume":"22","author":"Turner","year":"2000","journal-title":"Bioessays"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB6","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/S1097-2765(00)80253-1","article-title":"Acetylation regulates transcription factor activity at multiple levels","volume":"5","author":"Soutoglou","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB7","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/S1097-2765(01)00414-2","article-title":"Acetylation of p53 activates transcription through recruitment of coactivators\/histone acetyltransferases","volume":"8","author":"Barlev","year":"2001","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB8","doi-asserted-by":"crossref","first-page":"3155","DOI":"10.1093\/emboj\/17.11.3155","article-title":"Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase","volume":"17","author":"Zhang","year":"1998","journal-title":"EMBO J"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB9","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1038\/35044127","article-title":"Global histone acetylation and deacetylation in yeast","volume":"408","author":"Vogelauer","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB10","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1016\/S1097-2765(00)00129-5","article-title":"Gcn4 activator targets Gcn5 histone acetyltransferase to specific promoters independently of transcription","volume":"6","author":"Kuo","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB11","doi-asserted-by":"crossref","first-page":"3144","DOI":"10.1101\/gad.931401","article-title":"Histone H3 specific acetyltransferases are essential for cell cycle progression","volume":"15","author":"Howe","year":"2001","journal-title":"Genes Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB12","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1038\/28886","article-title":"Transcriptional activators direct histone acetyltransferase complexes to nucleosomes","volume":"394","author":"Utley","year":"1998","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB13","doi-asserted-by":"crossref","first-page":"1640","DOI":"10.1101\/gad.11.13.1640","article-title":"Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt\/Ada) complex","volume":"11","author":"Grant","year":"1997","journal-title":"Genes Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB14","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/S1097-2765(00)80258-0","article-title":"Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription","volume":"5","author":"Galarneau","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB15","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1126\/science.1060214","article-title":"Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit","volume":"292","author":"Brown","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB16","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1101\/gad.900101","article-title":"The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis","volume":"15","author":"Park","year":"2001","journal-title":"Genes Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB17","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/S0092-8674(00)00051-9","article-title":"Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis","volume":"102","author":"Ikura","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB18","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/S0968-0004(00)89120-3","article-title":"Transcriptional coactivators in yeast and beyond","volume":"20","author":"Guarente","year":"1995","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB19","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1101\/gad.911501","article-title":"The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4","volume":"15","author":"Larschan","year":"2001","journal-title":"Genes Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB20","doi-asserted-by":"crossref","first-page":"1935","DOI":"10.1101\/gad.911401","article-title":"SAGA is an essential in vivo target of the yeast acidic activator Gal4p","volume":"15","author":"Bhaumik","year":"2001","journal-title":"Genes Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB21","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1128\/MCB.19.1.86","article-title":"Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction","volume":"19","author":"Sterner","year":"1999","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB22","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0959-437X(00)00068-X","article-title":"Promoter targeting and chromatin remodeling by the SWI\/SNF complex","volume":"10","author":"Peterson","year":"2000","journal-title":"Curr Opin Genet Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB23","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/S0092-8674(00)80740-0","article-title":"Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle and developmentally regulated promoter","volume":"97","author":"Cosma","year":"1999","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB24","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/S0092-8674(00)00081-7","article-title":"Global role for chromatin remodeling enzymes in mitotic gene expression","volume":"102","author":"Krebs","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB25","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/S0092-8674(00)00169-0","article-title":"Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter","volume":"103","author":"Agalioti","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB26","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/S1097-2765(00)00103-9","article-title":"ATP Driven chromatin remodeling activity and histone acetyltransferases act sequentially during transactivation by RAR\/RXR in vitro","volume":"6","author":"Dilworth","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB27","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/S1097-2765(01)00200-3","article-title":"A transient histone hyperacetylation signal marks nucleosomes for remodeling at the PHO8 promoter in vivo","volume":"7","author":"Reinke","year":"2001","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB28","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/S0092-8674(01)00279-3","article-title":"Histone acetyltransferase complexes stabilize Swi\/Snf binding to promoter nucleosomes","volume":"104","author":"Hassan","year":"2001","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB29","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1016\/S1097-2765(00)00102-7","article-title":"Histone acetylation and hSWI\/SNF remodeling act in concert to stimulate V(D)J cleavage of nucleosomal DNA","volume":"6","author":"Kwon","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB30","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0092-8674(01)00196-9","article-title":"Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein","volume":"104","author":"Seo","year":"2001","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB31","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1128\/MCB.21.2.476-487.2001","article-title":"Stimulation of CREB binding protein nucleosomal histone acetyltransferase activity by a class of transcriptional activators","volume":"21","author":"Chen","year":"2001","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB32","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1093\/emboj\/20.8.1984","article-title":"Transcription factor-dependent regulation of CBP and P\/CAF histone acetyltransferase activity","volume":"20","author":"Soutoglou","year":"2001","journal-title":"EMBO J"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB33","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/79973","article-title":"Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during mouse development","volume":"26","author":"Xu","year":"2000","journal-title":"Nat Genet"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB34","doi-asserted-by":"crossref","first-page":"11303","DOI":"10.1073\/pnas.97.21.11303","article-title":"Distinct but overlapping roles of histone acetylase PCAF and of the closely related PCAF-B\/GCN5 in mouse embryogenesis","volume":"97","author":"Yamauchi","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB35","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1126\/science.1058783","article-title":"A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60","volume":"293","author":"Cao","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB36","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/35099568","article-title":"Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila","volume":"413","author":"Steffan","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB37","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\/S0959-437X(02)00279-4_BIB38","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/0092-8674(91)90385-C","article-title":"Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors","volume":"65","author":"Mahadevan","year":"1991","journal-title":"Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB39","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1126\/science.285.5429.886","article-title":"Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3","volume":"285","author":"Sassone-Corsi","year":"1999","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB40","doi-asserted-by":"crossref","first-page":"4779","DOI":"10.1093\/emboj\/18.17.4779","article-title":"The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3\/HMG-14 kinase","volume":"18","author":"Thomson","year":"1999","journal-title":"EMBO J"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB41","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1126\/science.1062322","article-title":"Snf1 \u2014 a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription","volume":"293","author":"Lo","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB42","doi-asserted-by":"crossref","first-page":"3003","DOI":"10.1101\/gad.848800","article-title":"Phosphorylation of histone H3 correlates with transcriptionally active loci","volume":"14","author":"Nowak","year":"2000","journal-title":"Genes Dev"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB43","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.1126\/science.284.5423.2174","article-title":"Regulation of transcription by a protein methyltransferase","volume":"284","author":"Chen","year":"1999","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB44","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1126\/science.1060781","article-title":"Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor","volume":"293","author":"Wang","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB45","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/35020506","article-title":"Regulation of chromatin structure by site-specific histone H3 methyltransferases","volume":"406","author":"Rea","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB46","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1126\/science.1060118","article-title":"Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly","volume":"292","author":"Nakayama","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB47","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/35065138","article-title":"Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain","volume":"410","author":"Bannister","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB48","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1038\/35065132","article-title":"Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins","volume":"410","author":"Lachner","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB49","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/35087620","article-title":"Rb targets histone H3 methylation and HP1 to promoters","volume":"412","author":"Nielsen","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB50","doi-asserted-by":"crossref","first-page":"6484","DOI":"10.1128\/MCB.21.19.6484-6494.2001","article-title":"Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase","volume":"21","author":"Vandel","year":"2001","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB51","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1126\/science.1064150","article-title":"Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries","volume":"293","author":"Noma","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB52","doi-asserted-by":"crossref","first-page":"2453","DOI":"10.1126\/science.1064413","article-title":"Correlation between histone lysine methylation and developmental changes at the chicken beta-globin locus","volume":"293","author":"Litt","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB53","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\/S0959-437X(02)00279-4_BIB54","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1126\/science.289.5488.2357","article-title":"Ubiquitin-activating\/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila","volume":"289","author":"Pham","year":"2000","journal-title":"Science"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB55","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1016\/S1097-2765(00)80256-7","article-title":"Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation","volume":"5","author":"Cheung","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB56","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1016\/S1097-2765(00)80257-9","article-title":"Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14","volume":"5","author":"Lo","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB57","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\/S0959-437X(02)00279-4_BIB58","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1128\/MCB.20.6.2167-2175.2000","article-title":"The H3-H4 N-terminal tail domains are the primary mediators of transcription factor IIIA access to 5S DNA within a nucleosome","volume":"20","author":"Vitolo","year":"2000","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB59","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1006\/jmbi.2001.4528","article-title":"Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites","volume":"307","author":"Anderson","year":"2001","journal-title":"J Mol Biol"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB60","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/20974","article-title":"Structure and ligand of a histone acetyltransferase bromodomain","volume":"399","author":"Dhalluin","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0959-437X(02)00279-4_BIB61","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1126\/science.288.5470.1422","article-title":"Structure and function of a human TAFII250 double bromodomain module","volume":"288","author":"Jacobson","year":"2000","journal-title":"Science"}],"container-title":["Current Opinion in Genetics &amp; Development"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959437X02002794?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959437X02002794?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,4,8]],"date-time":"2019-04-08T20:25:07Z","timestamp":1554755107000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959437X02002794"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,4]]},"references-count":61,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2002,4]]}},"alternative-id":["S0959437X02002794"],"URL":"https:\/\/doi.org\/10.1016\/s0959-437x(02)00279-4","relation":{},"ISSN":["0959-437X"],"issn-type":[{"value":"0959-437X","type":"print"}],"subject":[],"published":{"date-parts":[[2002,4]]}}}