{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T04:14:44Z","timestamp":1791087284555,"version":"4.1.0"},"reference-count":58,"publisher":"Springer Science and Business Media LLC","issue":"12","license":[{"start":{"date-parts":[[2011,11,13]],"date-time":"2011-11-13T00:00:00Z","timestamp":1321142400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2011,12]]},"DOI":"10.1038\/nsmb.2153","type":"journal-article","created":{"date-parts":[[2011,11,13]],"date-time":"2011-11-13T20:27:05Z","timestamp":1321216025000},"page":"1358-1365","source":"Crossref","is-referenced-by-count":130,"title":["Recognition of enhancer element\u2013specific histone methylation by TIP60 in transcriptional activation"],"prefix":"10.1038","volume":"18","author":[{"given":"Kwang Won","family":"Jeong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyunghwan","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan Jialun","family":"Situ","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tobias S","family":"Ulmer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Woojin","family":"An","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R","family":"Stallcup","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2011,11,13]]},"reference":[{"key":"BFnsmb2153_CR1","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1016\/S0955-0674(99)80045-3","volume":"11","author":"AJ Berk","year":"1999","unstructured":"Berk, A.J. Activation of RNA polymerase II transcription. Curr. Opin. Cell Biol. 11, 330\u2013335 (1999).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFnsmb2153_CR2","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1016\/S0092-8674(02)00641-4","volume":"108","author":"NJ McKenna","year":"2002","unstructured":"McKenna, N.J. & O'Malley, B.W. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108, 465\u2013474 (2002).","journal-title":"Cell"},{"key":"BFnsmb2153_CR3","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1007\/978-0-387-69080-3_12","volume":"617","author":"R Metivier","year":"2008","unstructured":"Metivier, R. et al. Dynamics of estrogen receptor-mediated transcriptional activation of responsive genes in vivo: apprehending transcription in four dimensions. Adv. Exp. Med. Biol. 617, 129\u2013138 (2008).","journal-title":"Adv. Exp. Med. Biol."},{"key":"BFnsmb2153_CR4","doi-asserted-by":"publisher","first-page":"751","DOI":"10.1016\/S0092-8674(03)00934-6","volume":"115","author":"R Metivier","year":"2003","unstructured":"Metivier, R. et al. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115, 751\u2013763 (2003).","journal-title":"Cell"},{"key":"BFnsmb2153_CR5","doi-asserted-by":"publisher","first-page":"843","DOI":"10.1016\/S0092-8674(00)00188-4","volume":"103","author":"Y Shang","year":"2000","unstructured":"Shang, Y., Hu, X., DiRenzo, J., Lazar, M.A. & Brown, M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103, 843\u2013852 (2000).","journal-title":"Cell"},{"key":"BFnsmb2153_CR6","doi-asserted-by":"publisher","first-page":"14359","DOI":"10.1074\/jbc.C200099200","volume":"277","author":"D Burakov","year":"2002","unstructured":"Burakov, D., Crofts, L.A., Chang, C.P. & Freedman, L.P. Reciprocal recruitment of DRIP\/mediator and p160 coactivator complexes in vivo by estrogen receptor. J. Biol. Chem. 277, 14359\u201314362 (2002).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR7","first-page":"203","volume":"274","author":"RT Utley","year":"2003","unstructured":"Utley, R.T. & Cote, J. The MYST family of histone acetyltransferases. Curr. Top. Microbiol. Immunol. 274, 203\u2013236 (2003).","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"BFnsmb2153_CR8","doi-asserted-by":"publisher","first-page":"2084","DOI":"10.1126\/science.1103455","volume":"306","author":"T Kusch","year":"2004","unstructured":"Kusch, T. et al. Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. Science 306, 2084\u20132087 (2004).","journal-title":"Science"},{"key":"BFnsmb2153_CR9","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1016\/S0092-8674(00)00051-9","volume":"102","author":"T Ikura","year":"2000","unstructured":"Ikura, T. et al. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102, 463\u2013473 (2000).","journal-title":"Cell"},{"key":"BFnsmb2153_CR10","doi-asserted-by":"publisher","first-page":"1496","DOI":"10.1016\/j.biocel.2006.03.003","volume":"38","author":"V Sapountzi","year":"2006","unstructured":"Sapountzi, V., Logan, I.R. & Robson, C.N. Cellular functions of TIP60. Int. J. Biochem. Cell Biol. 38, 1496\u20131509 (2006).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"BFnsmb2153_CR11","doi-asserted-by":"publisher","first-page":"789","DOI":"10.1046\/j.1365-2443.1998.00229.x","volume":"3","author":"A Kimura","year":"1998","unstructured":"Kimura, A. & Horikoshi, M. Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells 3, 789\u2013800 (1998).","journal-title":"Genes Cells"},{"key":"BFnsmb2153_CR12","doi-asserted-by":"publisher","first-page":"30595","DOI":"10.1074\/jbc.272.49.30595","volume":"272","author":"T Yamamoto","year":"1997","unstructured":"Yamamoto, T. & Horikoshi, M. Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. J. Biol. Chem. 272, 30595\u201330598 (1997).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR13","doi-asserted-by":"publisher","first-page":"827","DOI":"10.1016\/j.molcel.2006.11.021","volume":"24","author":"Y Tang","year":"2006","unstructured":"Tang, Y., Luo, J., Zhang, W. & Gu, W. Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24, 827\u2013839 (2006).","journal-title":"Mol. Cell"},{"key":"BFnsmb2153_CR14","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1016\/j.molcel.2006.11.026","volume":"24","author":"SM Sykes","year":"2006","unstructured":"Sykes, S.M. et al. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24, 841\u2013851 (2006).","journal-title":"Mol. Cell"},{"key":"BFnsmb2153_CR15","doi-asserted-by":"publisher","first-page":"13182","DOI":"10.1073\/pnas.0504211102","volume":"102","author":"Y Sun","year":"2005","unstructured":"Sun, Y., Jiang, X., Chen, S., Fernandes, N. & Price, B.D. A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc. Natl. Acad. Sci. USA 102, 13182\u201313187 (2005).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2153_CR16","doi-asserted-by":"publisher","first-page":"10826","DOI":"10.1128\/MCB.24.24.10826-10834.2004","volume":"24","author":"JH Patel","year":"2004","unstructured":"Patel, J.H. et al. The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5\/PCAF and TIP60. Mol. Cell Biol. 24, 10826\u201310834 (2004).","journal-title":"Mol. Cell Biol."},{"key":"BFnsmb2153_CR17","doi-asserted-by":"publisher","first-page":"17599","DOI":"10.1074\/jbc.274.25.17599","volume":"274","author":"ME Brady","year":"1999","unstructured":"Brady, M.E. et al. Tip60 is a nuclear hormone receptor coactivator. J. Biol. Chem. 274, 17599\u201317604 (1999).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR18","doi-asserted-by":"publisher","first-page":"25904","DOI":"10.1074\/jbc.M203423200","volume":"277","author":"L Gaughan","year":"2002","unstructured":"Gaughan, L., Logan, I.R., Cook, S., Neal, D.E. & Robson, C.N. Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor. J. Biol. Chem. 277, 25904\u201325913 (2002).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR19","doi-asserted-by":"publisher","first-page":"29298","DOI":"10.1074\/jbc.M109.037010","volume":"284","author":"KW Jeong","year":"2009","unstructured":"Jeong, K.W., Lee, Y.H. & Stallcup, M.R. Recruitment of the SWI\/SNF chromatin remodeling complex to steroid hormone-regulated promoters by nuclear receptor coactivator flightless-I. J. Biol. Chem. 284, 29298\u201329309 (2009).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR20","doi-asserted-by":"publisher","first-page":"32977","DOI":"10.1074\/jbc.M802024200","volume":"283","author":"YF Pan","year":"2008","unstructured":"Pan, Y.F. et al. Regulation of estrogen receptor-mediated long range transcription via evolutionarily conserved distal response elements. J. Biol. Chem. 283, 32977\u201332988 (2008).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR21","doi-asserted-by":"publisher","first-page":"2651","DOI":"10.1210\/me.2007-0082","volume":"21","author":"J Sun","year":"2007","unstructured":"Sun, J., Nawaz, Z. & Slingerland, J.M. Long-range activation of GREB1 by estrogen receptor via three distal consensus estrogen-responsive elements in breast cancer cells. Mol. Endocrinol. 21, 2651\u20132662 (2007).","journal-title":"Mol. Endocrinol."},{"key":"BFnsmb2153_CR22","doi-asserted-by":"publisher","first-page":"1289","DOI":"10.1038\/ng1901","volume":"38","author":"JS Carroll","year":"2006","unstructured":"Carroll, J.S. et al. Genome-wide analysis of estrogen receptor binding sites. Nat. Genet. 38, 1289\u20131297 (2006).","journal-title":"Nat. Genet."},{"key":"BFnsmb2153_CR23","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1016\/j.molonc.2008.05.004","volume":"2","author":"N Bretschneider","year":"2008","unstructured":"Bretschneider, N. et al. E2-mediated cathepsin D (CTSD) activation involves looping of distal enhancer elements. Mol. Oncol. 2, 182\u2013190 (2008).","journal-title":"Mol. Oncol."},{"key":"BFnsmb2153_CR24","doi-asserted-by":"publisher","first-page":"46841","DOI":"10.1074\/jbc.M103710200","volume":"276","author":"L Gaughan","year":"2001","unstructured":"Gaughan, L., Brady, M.E., Cook, S., Neal, D.E. & Robson, C.N. Tip60 is a co-activator specific for class I nuclear hormone receptors. J. Biol. Chem. 276, 46841\u201346848 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR25","doi-asserted-by":"publisher","first-page":"4279","DOI":"10.1002\/j.1460-2075.1993.tb06112.x","volume":"12","author":"C Muchardt","year":"1993","unstructured":"Muchardt, C. & Yaniv, M. A human homologue of Saccharomyces cerevisiae SNF2\/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J. 12, 4279\u20134290 (1993).","journal-title":"EMBO J."},{"key":"BFnsmb2153_CR26","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1016\/0092-8674(94)90405-7","volume":"79","author":"JL Dunaief","year":"1994","unstructured":"Dunaief, J.L. et al. The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79, 119\u2013130 (1994).","journal-title":"Cell"},{"key":"BFnsmb2153_CR27","doi-asserted-by":"publisher","first-page":"1906","DOI":"10.1101\/gr.078519.108","volume":"18","author":"AG Robertson","year":"2008","unstructured":"Robertson, A.G. et al. Genome-wide relationship between histone H3 lysine 4 mono- and tri-methylation and transcription factor binding. Genome Res. 18, 1906\u20131917 (2008).","journal-title":"Genome Res."},{"key":"BFnsmb2153_CR28","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1038\/ng1966","volume":"39","author":"ND Heintzman","year":"2007","unstructured":"Heintzman, N.D. et al. Distinct and predictive chromatin signatures of transcriptional promoters and enhancers in the human genome. Nat. Genet. 39, 311\u2013318 (2007).","journal-title":"Nat. Genet."},{"key":"BFnsmb2153_CR29","doi-asserted-by":"publisher","first-page":"8695","DOI":"10.1073\/pnas.082249499","volume":"99","author":"BE Bernstein","year":"2002","unstructured":"Bernstein, B.E. et al. Methylation of histone H3 Lys 4 in coding regions of active genes. Proc. Natl. Acad. Sci. USA 99, 8695\u20138700 (2002).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2153_CR30","doi-asserted-by":"publisher","first-page":"876","DOI":"10.1038\/nature03877","volume":"436","author":"TH Kim","year":"2005","unstructured":"Kim, T.H. et al. A high-resolution map of active promoters in the human genome. Nature 436, 876\u2013880 (2005).","journal-title":"Nature"},{"key":"BFnsmb2153_CR31","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1016\/j.cell.2007.05.009","volume":"129","author":"A Barski","year":"2007","unstructured":"Barski, A. et al. High-resolution profiling of histone methylations in the human genome. Cell 129, 823\u2013837 (2007).","journal-title":"Cell"},{"key":"BFnsmb2153_CR32","doi-asserted-by":"publisher","first-page":"2080","DOI":"10.1126\/science.1069473","volume":"295","author":"SA Jacobs","year":"2002","unstructured":"Jacobs, S.A. & Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080\u20132083 (2002).","journal-title":"Science"},{"key":"BFnsmb2153_CR33","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1038\/nature722","volume":"416","author":"PR Nielsen","year":"2002","unstructured":"Nielsen, P.R. et al. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature 416, 103\u2013107 (2002).","journal-title":"Nature"},{"key":"BFnsmb2153_CR34","doi-asserted-by":"publisher","first-page":"1823","DOI":"10.1101\/gad.269603","volume":"17","author":"J Min","year":"2003","unstructured":"Min, J., Zhang, Y. & Xu, R.M. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17, 1823\u20131828 (2003).","journal-title":"Genes Dev."},{"key":"BFnsmb2153_CR35","doi-asserted-by":"publisher","first-page":"1181","DOI":"10.1038\/nature04290","volume":"438","author":"JF Flanagan","year":"2005","unstructured":"Flanagan, J.F. et al. Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature 438, 1181\u20131185 (2005).","journal-title":"Nature"},{"key":"BFnsmb2153_CR36","doi-asserted-by":"publisher","first-page":"853","DOI":"10.1016\/j.molcel.2010.05.011","volume":"38","author":"TA Milne","year":"2010","unstructured":"Milne, T.A. et al. Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesis. Mol. Cell 38, 853\u2013863 (2010).","journal-title":"Mol. Cell"},{"key":"BFnsmb2153_CR37","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1038\/ncb1982","volume":"11","author":"Y Sun","year":"2009","unstructured":"Sun, Y. et al. Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60. Nat. Cell Biol. 11, 1376\u20131382 (2009).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb2153_CR38","doi-asserted-by":"publisher","first-page":"4929","DOI":"10.1158\/0008-5472.CAN-05-4461","volume":"66","author":"KM Dreijerink","year":"2006","unstructured":"Dreijerink, K.M. et al. Menin links estrogen receptor activation to histone H3K4 trimethylation. Cancer Res. 66, 4929\u20134935 (2006).","journal-title":"Cancer Res."},{"key":"BFnsmb2153_CR39","doi-asserted-by":"publisher","first-page":"15714","DOI":"10.1074\/jbc.M513245200","volume":"281","author":"R Mo","year":"2006","unstructured":"Mo, R., Rao, S.M. & Zhu, Y.J. Identification of the MLL2 complex as a coactivator for estrogen receptor alpha. J. Biol. Chem. 281, 15714\u201315720 (2006).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2153_CR40","doi-asserted-by":"publisher","first-page":"1119","DOI":"10.1016\/S1097-2765(02)00740-2","volume":"10","author":"T Nakamura","year":"2002","unstructured":"Nakamura, T. et al. ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol. Cell 10, 1119\u20131128 (2002).","journal-title":"Mol. Cell"},{"key":"BFnsmb2153_CR41","doi-asserted-by":"publisher","first-page":"873","DOI":"10.1016\/j.cell.2005.04.031","volume":"121","author":"Y Dou","year":"2005","unstructured":"Dou, Y. et al. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121, 873\u2013885 (2005).","journal-title":"Cell"},{"key":"BFnsmb2153_CR42","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1038\/nature01080","volume":"419","author":"H Santos-Rosa","year":"2002","unstructured":"Santos-Rosa, H. et al. Active genes are tri-methylated at K4 of histone H3. Nature 419, 407\u2013411 (2002).","journal-title":"Nature"},{"key":"BFnsmb2153_CR43","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1016\/S1097-2765(03)00092-3","volume":"11","author":"HH Ng","year":"2003","unstructured":"Ng, H.H., Robert, F., Young, R.A. & Struhl, K. Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell 11, 709\u2013719 (2003).","journal-title":"Mol. Cell"},{"key":"BFnsmb2153_CR44","doi-asserted-by":"publisher","first-page":"5993","DOI":"10.1093\/nar\/gkp660","volume":"37","author":"J Choi","year":"2009","unstructured":"Choi, J., Heo, K. & An, W. Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A. Nucleic Acids Res. 37, 5993\u20136007 (2009).","journal-title":"Nucleic Acids Res."},{"key":"BFnsmb2153_CR45","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/S0092-8674(00)81585-8","volume":"94","author":"E Wolf","year":"1998","unstructured":"Wolf, E. et al. Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell 94, 439\u2013449 (1998).","journal-title":"Cell"},{"key":"BFnsmb2153_CR46","doi-asserted-by":"publisher","first-page":"2750","DOI":"10.1128\/MCB.00804-09","volume":"30","author":"JH Park","year":"2010","unstructured":"Park, J.H., Sun, X.J. & Roeder, R.G. The SANT domain of p400 ATPase represses acetyltransferase activity and coactivator function of TIP60 in basal p21 gene expression. Mol. Cell Biol. 30, 2750\u20132761 (2010).","journal-title":"Mol. Cell Biol."},{"key":"BFnsmb2153_CR47","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1038\/ncb1343","volume":"8","author":"R Murr","year":"2006","unstructured":"Murr, R. et al. Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat. Cell Biol. 8, 91\u201399 (2006).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb2153_CR48","doi-asserted-by":"publisher","first-page":"8502","DOI":"10.1128\/MCB.01382-07","volume":"27","author":"Y Sun","year":"2007","unstructured":"Sun, Y., Xu, Y., Roy, K. & Price, B.D. DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity. Mol. Cell Biol. 27, 8502\u20138509 (2007).","journal-title":"Mol. Cell Biol."},{"key":"BFnsmb2153_CR49","doi-asserted-by":"publisher","first-page":"2466","DOI":"10.1038\/sj.onc.1206342","volume":"22","author":"K Halkidou","year":"2003","unstructured":"Halkidou, K. et al. Expression of Tip60, an androgen receptor coactivator, and its role in prostate cancer development. Oncogene 22, 2466\u20132477 (2003).","journal-title":"Oncogene"},{"key":"BFnsmb2153_CR50","doi-asserted-by":"publisher","first-page":"1063","DOI":"10.1038\/nature06055","volume":"448","author":"C Gorrini","year":"2007","unstructured":"Gorrini, C. et al. Tip60 is a haplo-insufficient tumour suppressor required for an oncogene-induced DNA damage response. Nature 448, 1063\u20131067 (2007).","journal-title":"Nature"},{"key":"BFnsmb2153_CR51","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1073\/pnas.88.1.263","volume":"88","author":"R Paro","year":"1991","unstructured":"Paro, R. & Hogness, D.S. The Polycomb protein shares a homologous domain with a heterochromatin-associated protein of Drosophila. Proc. Natl. Acad. Sci. USA 88, 263\u2013267 (1991).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2153_CR52","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1016\/j.immuni.2010.02.008","volume":"32","author":"S Ghisletti","year":"2010","unstructured":"Ghisletti, S. et al. Identification and characterization of enhancers controlling the inflammatory gene expression program in macrophages. Immunity 32, 317\u2013328 (2010).","journal-title":"Immunity"},{"key":"BFnsmb2153_CR53","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1101\/gad.967202","volume":"16","author":"K Nishioka","year":"2002","unstructured":"Nishioka, K. et al. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16, 479\u2013489 (2002).","journal-title":"Genes Dev."},{"key":"BFnsmb2153_CR54","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1186\/gb-2005-6-8-227","volume":"6","author":"SC Dillon","year":"2005","unstructured":"Dillon, S.C., Zhang, X., Trievel, R.C. & Cheng, X. The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol. 6, 227 (2005).","journal-title":"Genome Biol."},{"key":"BFnsmb2153_CR55","doi-asserted-by":"publisher","first-page":"4152","DOI":"10.1073\/pnas.95.8.4152","volume":"95","author":"O Rozenblatt-Rosen","year":"1998","unstructured":"Rozenblatt-Rosen, O. et al. The C-terminal SET domains of ALL-1 and TRITHORAX interact with the INI1 and SNR1 proteins, components of the SWI\/SNF complex. Proc. Natl. Acad. Sci. USA 95, 4152\u20134157 (1998).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2153_CR56","doi-asserted-by":"publisher","first-page":"610","DOI":"10.1210\/me.2008-0455","volume":"23","author":"S Lee","year":"2009","unstructured":"Lee, S. et al. Crucial roles for interactions between MLL3\/4 and INI1 in nuclear receptor transactivation. Mol. Endocrinol. 23, 610\u2013619 (2009).","journal-title":"Mol. Endocrinol."},{"key":"BFnsmb2153_CR57","doi-asserted-by":"publisher","first-page":"713","DOI":"10.1038\/nsmb1128","volume":"13","author":"Y Dou","year":"2006","unstructured":"Dou, Y. et al. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Nat. Struct. Mol. Biol. 13, 713\u2013719 (2006).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFnsmb2153_CR58","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1038\/nsmb.1384","volume":"15","author":"RE Collins","year":"2008","unstructured":"Collins, R.E. et al. The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules. Nat. Struct. Mol. Biol. 15, 245\u2013250 (2008).","journal-title":"Nat. Struct. Mol. Biol."}],"container-title":["Nature Structural &amp; Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2153.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2153","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2153.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,19]],"date-time":"2023-05-19T04:30:11Z","timestamp":1684470611000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsmb.2153"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,11,13]]},"references-count":58,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2011,12]]}},"alternative-id":["BFnsmb2153"],"URL":"https:\/\/doi.org\/10.1038\/nsmb.2153","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,11,13]]}}}