{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T19:02:12Z","timestamp":1769022132635,"version":"3.49.0"},"reference-count":52,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[1998,8,1]],"date-time":"1998-08-01T00:00:00Z","timestamp":901929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":5464,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell"],"published-print":{"date-parts":[[1998,8]]},"DOI":"10.1016\/s0092-8674(00)81584-6","type":"journal-article","created":{"date-parts":[[2004,6,30]],"date-time":"2004-06-30T12:27:59Z","timestamp":1088598479000},"page":"427-438","source":"Crossref","is-referenced-by-count":185,"title":["Structure of the Histone Acetyltransferase Hat1"],"prefix":"10.1016","volume":"94","author":[{"given":"Robert N.","family":"Dutnall","sequence":"first","affiliation":[]},{"given":"Stefan T.","family":"Tafrov","sequence":"additional","affiliation":[]},{"given":"Rolf","family":"Sternglanz","sequence":"additional","affiliation":[]},{"given":"V.","family":"Ramakrishnan","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0092-8674(00)81584-6_BIB1","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1107\/S0907444995008754","article-title":"Methods used in the structure determination of bovine mitochondrial F1ATPase","volume":"52","author":"Abrahams","year":"1996","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB2","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/S0959-437X(96)80048-7","article-title":"Special HATs for special occasions","volume":"6","author":"Brownell","year":"1996","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB3","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/S0092-8674(00)81063-6","article-title":"Tetrahymena histone acetyltransferase A","volume":"84","author":"Brownell","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB4","series-title":"X-PLOR Version 3.843","author":"Br\u00fcnger","year":"1996"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB5","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1093\/emboj\/16.3.555","article-title":"Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo","volume":"16","author":"Candau","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB6","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1042\/bj3160697","article-title":"Structure and critical residues at the active site of spermidine\/spermine-N1-acetyltransferase","volume":"316","author":"Coleman","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB52","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite","volume":"50","author":"Collaborative Computational Project Number 4","year":"1994","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB7","doi-asserted-by":"crossref","first-page":"12165","DOI":"10.1016\/S0021-9258(18)33695-0","article-title":"Inhibition of histone acetylation by N-[2-(S-coenzyme A)acetyl] spermidine amide, a multisubstrate analog","volume":"257","author":"Cullis","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB8","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0014-5793(96)00401-2","article-title":"Purification and characterization of the cytoplasmic histone acetyltransferase B of maize embryos","volume":"386","author":"Eberharter","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB9","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1016\/S0959-440X(96)80009-1","article-title":"The diverse world of coenzyme A binding proteins","volume":"6","author":"Engel","year":"1996","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB10","doi-asserted-by":"crossref","first-page":"4250","DOI":"10.1021\/bi00313a036","article-title":"Differential inhibition of histone and polyamine acetylases by multisubstrate analogues","volume":"23","author":"Erwin","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB11","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1006\/prep.1994.1037","article-title":"Expression of chicken linker histones in E. coli","volume":"5","author":"Gerchman","year":"1994","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB12","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\/S0092-8674(00)81584-6_BIB13","doi-asserted-by":"crossref","first-page":"2054","DOI":"10.1093\/emboj\/16.8.2054","article-title":"mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila","volume":"16","author":"Hilfiker","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB14","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building protein models in electron density maps and the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB15","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0092-8674(00)80924-1","article-title":"Eukaryotic transcription","volume":"92","author":"Kadonaga","year":"1998","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB16","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/S0955-0674(96)80012-3","article-title":"Nucleosome assembly","volume":"8","author":"Kaufman","year":"1996","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB17","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1101\/gad.11.3.345","article-title":"Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cells lacking chromatin assembly factor-I","volume":"11","author":"Kaufman","year":"1997","journal-title":"Genes Dev."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB18","doi-asserted-by":"crossref","first-page":"24674","DOI":"10.1074\/jbc.270.42.24674","article-title":"Identification of a gene encoding a yeast histone H4 acetyltransferase","volume":"270","author":"Kleff","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB19","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/S0014-5793(97)01544-5","article-title":"Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver","volume":"421","author":"Kolle","year":"1998","journal-title":"FEBS Lett."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB20","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT\u2014a program to produce both detailed and schematic plots of protein structures","volume":"24","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB21","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/383269a0","article-title":"Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines","volume":"383","author":"Kuo","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB22","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1101\/gad.12.5.627","article-title":"Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo","volume":"12","author":"Kuo","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB23","doi-asserted-by":"crossref","first-page":"18920","DOI":"10.1074\/jbc.271.31.18920","article-title":"RGFGIGS is an amino acid sequence required for acetyl coenzyme A binding and activity of human spermidine\/spermine N1 acetyltransferase","volume":"271","author":"Lu","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB24","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1093\/emboj\/17.10.2886","article-title":"The acetyltransferase activity of CBP stimulates transcription","volume":"17","author":"Martinez-Balbas","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB25","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/S0076-6879(97)77028-9","article-title":"Raster3D","volume":"277","author":"Merritt","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB26","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1038\/371297a0","article-title":"The ancient regulatory-protein family of WD-repeat proteins","volume":"371","author":"Neer","year":"1994","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB27","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/S0968-0004(97)01034-7","article-title":"GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein","volume":"22","author":"Neuwald","year":"1997","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB28","first-page":"166","article-title":"GRASP","volume":"64","author":"Nicholls","year":"1993","journal-title":"Biophys. J."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB29","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","author":"Otwinowski","year":"1997"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB30","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0092-8674(00)81325-2","article-title":"The major cytoplasmic histone acetyltransferase in yeast","volume":"87","author":"Parthun","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB31","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","DOI":"10.1016\/S0076-6879(97)76077-4","article-title":"Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement","author":"Ramakrishnan","year":"1997"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB32","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1038\/362219a0","article-title":"Crystal structure of globular domain of histone H5 and its implications for nucleosome binding","volume":"362","author":"Ramakrishnan","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB33","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/0022-2836(73)90388-4","article-title":"Comparison of super-secondary structures in proteins","volume":"76","author":"Rao","year":"1973","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB34","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1038\/ng0996-42","article-title":"Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases","volume":"14","author":"Reifsnyder","year":"1996","journal-title":"Nat. Genet."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB35","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1083\/jcb.106.4.1017","article-title":"Micronuclei and the cytoplasm of growing Tetrahymena contain a histone acetylase activity which is highly specific for free histone H4","volume":"106","author":"Richman","year":"1988","journal-title":"J. Cell Biol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB36","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/S0092-8674(00)81316-1","article-title":"Histone acetylation and chromatin assembly","volume":"87","author":"Roth","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB37","doi-asserted-by":"crossref","first-page":"12599","DOI":"10.1074\/jbc.273.20.12599","article-title":"HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4","volume":"273","author":"Ruiz-Garc\u00eda","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB38","doi-asserted-by":"crossref","first-page":"3561","DOI":"10.1073\/pnas.95.7.3561","article-title":"ESA1 is a histone acetyltransferase that is essential for growth in yeast","volume":"95","author":"Smith","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB39","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1073\/pnas.92.4.1237","article-title":"Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4","volume":"92","author":"Sobel","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB40","first-page":"16","article-title":"CCD-based detector for X-ray crystallography","volume":"2278","author":"Stanton","year":"1994","journal-title":"Proc. Soc. Photo-Opt. Instr. Eng."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB41","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1101\/gad.12.5.599","article-title":"Histone acetylation and transcriptional regulatory mechanisms","volume":"12","author":"Struhl","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB42","series-title":"Biochemistry","author":"Stryer","year":"1995"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB43","first-page":"61","article-title":"Use of T7 RNA polymerase to direct expression of cloned genes","volume":"185","author":"Studier","year":"1990","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB44","doi-asserted-by":"crossref","first-page":"20270","DOI":"10.1016\/S0021-9258(19)88696-9","article-title":"Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae","volume":"267","author":"Tercero","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB45","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/S0076-6879(97)76076-2","article-title":"Multiwavelength anomalous diffraction phasing of macromolecular structures","volume":"276","author":"Terwilliger","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB46","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s000180050122","article-title":"Histone acetylation as an epigenetic determinant of long-term transcriptional competence","volume":"54","author":"Turner","year":"1998","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB47","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0092-8674(00)81326-4","article-title":"Nucleosome assembly by a complex of CAF-1 and acetylated histones H3\/H4","volume":"87","author":"Verreault","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB48","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/S0960-9822(98)70040-5","article-title":"Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase","volume":"8","author":"Verreault","year":"1998","journal-title":"Curr. Biol."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB49","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1101\/gad.12.5.640","article-title":"Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo","volume":"12","author":"Wang","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/S0092-8674(00)81584-6_BIB50","doi-asserted-by":"crossref","first-page":"4637","DOI":"10.1021\/bi00289a004","article-title":"Kinetic mechanism of the reaction catalyzed by nuclear histone acetyltransferase from calf thymus","volume":"22","author":"Wong","year":"1983","journal-title":"Biochemistry"},{"key":"10.1016\/S0092-8674(00)81584-6_BIB51","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/382319a0","article-title":"A p300\/CBP-associated factor that competes with the adenoviral oncoprotein E1A","volume":"382","author":"Yang","year":"1996","journal-title":"Nature"}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867400815846?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867400815846?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,23]],"date-time":"2021-06-23T21:45:35Z","timestamp":1624484735000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867400815846"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,8]]},"references-count":52,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1998,8]]}},"alternative-id":["S0092867400815846"],"URL":"https:\/\/doi.org\/10.1016\/s0092-8674(00)81584-6","relation":{},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[1998,8]]}}}