{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T15:03:07Z","timestamp":1790780587756,"version":"4.1.0"},"reference-count":211,"publisher":"Portland Press Ltd.","issue":"5","license":[{"start":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T00:00:00Z","timestamp":1776384000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM149229"],"award-info":[{"award-number":["GM149229"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Blood Cancer United","award":["NA"],"award-info":[{"award-number":["NA"]}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Charles King Trust","award":["NA"],"award-info":[{"award-number":["NA"]}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,5,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Chromatin function emerges from combinatorial patterns of histone post-translational modifications (PTMs) that are read, written, and erased by dedicated enzymes. Over the past 30\u00a0years, increasing evidence suggests that specific histone PTMs or combinations of PTMs influence one another, constituting epigenetic cross-talk that shapes chromatin structure, protein\u2013protein interactions, and catalytic efficiency of nucleosome-targeting enzymes. Here, we summarize mechanistic and methodological advances that enable rigorous interrogation of histone PTM interplay. We highlight selected nucleosome engineering strategies that build precisely modified substrates to test in vitro, proteomic pipelines that preserve combinatorial information, and omics technology that can globally profile integrated chromatin regulatory events in cells and tissues. Furthermore, we survey multivalent reader modules and engineered biosensors that report combinatorial marks in nucleosomes and living cells. Representative case studies illustrate how defined PTMs modulate catalytic parameters of writer and eraser complexes, including lysine methyltransferases, demethylases, acetyltransferases, and deacetylases, focusing on cross-talk with histone H3 N-terminal tail marks. These include the role of H3K9me2\/3 and K14ac in directing propagation of H3K9me3, the role of H3K4me1\/2 and K14ac in slowing H3K4 demethylation, the role of H3K4me2\/3 in directing H3K9 acetylation, and the role of H3K36 methylation in directing deacetylation of H3 and H4. The substrates for these case studies include both mononucleosomes and nucleosome arrays. These examples illustrate the principle of epigenetic cross-talk, namely, that specific combinatorial PTMs can affect enzymes and alter local biochemistry.<\/jats:p>","DOI":"10.1042\/bcj20250115","type":"journal-article","created":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T10:01:57Z","timestamp":1776420117000},"page":"713-740","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Histone modification cross-talk: analytical tools and molecular mechanisms"],"prefix":"10.1042","volume":"483","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5186-5838","authenticated-orcid":false,"given":"Jennifer","family":"Jiang","sequence":"first","affiliation":[{"name":"1Division of Genetics, Department of Medicine, Brigham and Women\u2019s Hospital, Boston, MA 02115, U.S.A."},{"name":"2Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5143-099X","authenticated-orcid":false,"given":"Sarah","family":"DuBois-Coyne","sequence":"additional","affiliation":[{"name":"1Division of Genetics, Department of Medicine, Brigham and Women\u2019s Hospital, Boston, MA 02115, U.S.A."},{"name":"2Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0801-9331","authenticated-orcid":false,"given":"Eunju","family":"Nam","sequence":"additional","affiliation":[{"name":"1Division of Genetics, Department of Medicine, Brigham and Women\u2019s Hospital, Boston, MA 02115, U.S.A."},{"name":"2Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, U.S.A."},{"name":"3Department of Physics and Chemistry, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 42988, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3745-5645","authenticated-orcid":false,"given":"Samuel\u00a0D.","family":"Whedon","sequence":"additional","affiliation":[{"name":"1Division of Genetics, Department of Medicine, Brigham and Women\u2019s Hospital, Boston, MA 02115, U.S.A."},{"name":"2Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2021-5186","authenticated-orcid":false,"given":"Kwangwoon","family":"Lee","sequence":"additional","affiliation":[{"name":"1Division of Genetics, Department of Medicine, Brigham and Women\u2019s Hospital, Boston, MA 02115, U.S.A."},{"name":"2Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, U.S.A."},{"name":"4Division of Medicinal Chemistry and Pharmacognosy, The Ohio State University, Columbus, Ohio 43210, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6873-7824","authenticated-orcid":false,"given":"Philip\u00a0A.","family":"Cole","sequence":"additional","affiliation":[{"name":"1Division of Genetics, Department of Medicine, Brigham and Women\u2019s Hospital, Boston, MA 02115, U.S.A."},{"name":"2Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,4,17]]},"reference":[{"key":"2026041706015387100_B1","first-page":"106","article-title":"Emil Heitz and the concept of heterochromatin: longitudinal chromosome differentiation was recognized fifty years ago","volume":"31","author":"Passarge","year":"1979","journal-title":"Am. J. Hum. Genet."},{"key":"2026041706015387100_B2","doi-asserted-by":"publisher","first-page":"854","DOI":"10.1038\/286854a0","article-title":"The 5\u2032 ends of Drosophila heat shock genes in chromatin are hypersensitive to DNase I","volume":"286","author":"Wu","year":"1980","journal-title":"Nature"},{"key":"2026041706015387100_B3","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1038\/38444","article-title":"Crystal structure of the nucleosome core particle at 2.8 A resolution","volume":"389","author":"Luger","year":"1997","journal-title":"Nature"},{"key":"2026041706015387100_B4","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/0092-8674(94)90180-5","article-title":"Position effect variegation at fission yeast centromeres","volume":"76","author":"Allshire","year":"1994","journal-title":"Cell"},{"key":"2026041706015387100_B5","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1083\/jcb.93.2.285","article-title":"Participation of core histone \u201ctails\u201d in the stabilization of the chromatin solenoid","volume":"93","author":"Allan","year":"1982","journal-title":"J. Cell Biol."},{"key":"2026041706015387100_B6","doi-asserted-by":"publisher","first-page":"693","DOI":"10.1016\/j.cell.2007.02.005","article-title":"Chromatin modifications and their function","volume":"128","author":"Kouzarides","year":"2007","journal-title":"Cell"},{"key":"2026041706015387100_B7","doi-asserted-by":"publisher","first-page":"1016","DOI":"10.1016\/j.cell.2011.08.008","article-title":"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification","volume":"146","author":"Tan","year":"2011","journal-title":"Cell"},{"key":"2026041706015387100_B8","doi-asserted-by":"publisher","first-page":"2382","DOI":"10.1074\/mcp.M113.035659","article-title":"Lysine propionylation is a prevalent post-translational modification in Thermus thermophilus","volume":"13","author":"Okanishi","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"2026041706015387100_B9","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1038\/s41589-024-01680-8","article-title":"Lysine L-lactylation is the dominant lactylation isomer induced by glycolysis","volume":"21","author":"Zhang","year":"2025","journal-title":"Nat. Chem. Biol."},{"key":"2026041706015387100_B10","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1016\/j.molcel.2016.03.036","article-title":"Metabolic regulation of gene expression by histone lysine beta-hydroxybutyrylation","volume":"62","author":"Xie","year":"2016","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B11","doi-asserted-by":"publisher","first-page":"7163","DOI":"10.1111\/jcmm.14650","article-title":"Functions and mechanisms of lysine crotonylation","volume":"23","author":"Wan","year":"2019","journal-title":"J. Cell. Mol. Med."},{"key":"2026041706015387100_B12","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/j.molcel.2015.12.015","article-title":"Modulations of DNA contacts by linker histones and post-translational modifications determine the mobility and modifiability of nucleosomal H3 tails","volume":"61","author":"Stutzer","year":"2016","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B13","doi-asserted-by":"publisher","first-page":"844","DOI":"10.1126\/science.1124000","article-title":"Histone H4-K16 acetylation controls chromatin structure and protein interactions","volume":"311","author":"Shogren-Knaak","year":"2006","journal-title":"Science"},{"key":"2026041706015387100_B14","doi-asserted-by":"publisher","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":"2026041706015387100_B15","doi-asserted-by":"publisher","first-page":"1795","DOI":"10.1101\/gad.269977.115","article-title":"Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response","volume":"29","author":"Shanle","year":"2015","journal-title":"Genes Dev."},{"key":"2026041706015387100_B16","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1016\/j.tibs.2013.08.002","article-title":"Tudor: a versatile family of histone methylation \u2018readers\u2019","volume":"38","author":"Lu","year":"2013","journal-title":"Trends Biochem. Sci."},{"key":"2026041706015387100_B17","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1038\/cr.2011.22","article-title":"Regulation of chromatin by histone modifications","volume":"21","author":"Bannister","year":"2011","journal-title":"Cell Res."},{"key":"2026041706015387100_B18","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1016\/j.molcel.2005.08.032","article-title":"Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3","volume":"20","author":"Macdonald","year":"2005","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B19","doi-asserted-by":"publisher","first-page":"194627","DOI":"10.1016\/j.bbagrm.2020.194627","article-title":"Catalysis by protein acetyltransferase Gcn5","volume":"1864","author":"Albaugh","year":"2021","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"2026041706015387100_B20","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1016\/0076-6879(89)70065-3","article-title":"Assembly of nucleosomes and chromatin in vitro","volume":"170","author":"Rhodes","year":"1989","journal-title":"Methods Enzymol."},{"key":"2026041706015387100_B21","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1006\/jmbi.1997.1494","article-title":"New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning","volume":"276","author":"Lowary","year":"1998","journal-title":"J. Mol. Biol."},{"key":"2026041706015387100_B22","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1006\/jmbi.1997.1235","article-title":"Characterization of nucleosome core particles containing histone proteins made in bacteria","volume":"272","author":"Luger","year":"1997","journal-title":"J. Mol. Biol."},{"key":"2026041706015387100_B23","doi-asserted-by":"publisher","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":"2026041706015387100_B24","doi-asserted-by":"publisher","first-page":"e3367","DOI":"10.1002\/psc.3367","article-title":"Chemical approaches for the preparation of ubiquitinated proteins via natural linkages","volume":"28","author":"Zhou","year":"2022","journal-title":"J. Pept. Sci."},{"key":"2026041706015387100_B25","doi-asserted-by":"publisher","first-page":"6705","DOI":"10.1073\/pnas.95.12.6705","article-title":"Expressed protein ligation: a general method for protein engineering","volume":"95","author":"Muir","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B26","doi-asserted-by":"publisher","first-page":"776","DOI":"10.1126\/science.7973629","article-title":"Synthesis of proteins by native chemical ligation","volume":"266","author":"Dawson","year":"1994","journal-title":"Science"},{"key":"2026041706015387100_B27","doi-asserted-by":"publisher","first-page":"2483","DOI":"10.1038\/nprot.2013.152","article-title":"Chemical synthesis of proteins using peptide hydrazides as thioester surrogates","volume":"8","author":"Zheng","year":"2013","journal-title":"Nat. Protoc."},{"key":"2026041706015387100_B28","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1002\/psc.2747","article-title":"Efficient generation of peptide hydrazides via direct hydrazinolysis of Peptidyl-Wang-TentaGel resins","volume":"21","author":"Bello","year":"2015","journal-title":"J. Pept. Sci."},{"key":"2026041706015387100_B29","doi-asserted-by":"publisher","first-page":"7197","DOI":"10.1021\/jacs.5b03504","article-title":"Chemical protein synthesis using a second-generation N-acylurea linker for the preparation of peptide-thioester precursors","volume":"137","author":"Blanco-Canosa","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B30","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/978-1-0716-0434-2_1","article-title":"Methods and applications of expressed protein ligation","volume":"2133","author":"Wang","year":"2020","journal-title":"Methods Mol. Biol."},{"key":"2026041706015387100_B31","doi-asserted-by":"publisher","first-page":"10025","DOI":"10.1039\/D3SC03664B","article-title":"Synthesis of ubiquitinated proteins for biochemical and functional analysis","volume":"14","author":"Kriegesmann","year":"2023","journal-title":"Chem. Sci."},{"key":"2026041706015387100_B32","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/j.chembiol.2021.03.009","article-title":"Decoding the messaging of the ubiquitin system using chemical and protein probes","volume":"28","author":"Henneberg","year":"2021","journal-title":"Cell Chem. Biol."},{"key":"2026041706015387100_B33","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/bs.mie.2019.01.003","article-title":"Semisynthesis of ubiquitinated histone H2B with a native or nonhydrolyzable linkage","volume":"618","author":"Morgan","year":"2019","journal-title":"Methods Enzymol."},{"key":"2026041706015387100_B34","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1146\/annurev-biochem-060614-034429","article-title":"Application of the protein semisynthesis strategy to the generation of modified chromatin","volume":"84","author":"Holt","year":"2015","journal-title":"Annu. Rev. Biochem."},{"key":"2026041706015387100_B35","doi-asserted-by":"publisher","first-page":"1003","DOI":"10.1016\/j.cell.2006.12.041","article-title":"The site-specific installation of methyl-lysine analogs into recombinant histones","volume":"128","author":"Simon","year":"2007","journal-title":"Cell"},{"key":"2026041706015387100_B36","doi-asserted-by":"publisher","first-page":"33827","DOI":"10.1074\/jbc.M114.591644","article-title":"Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions","volume":"289","author":"Dhall","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B37","doi-asserted-by":"publisher","first-page":"13613","DOI":"10.1039\/D1SC02973H","article-title":"Recent developments in chemical conjugation strategies targeting native amino acids in proteins and their applications in antibody-drug conjugates","volume":"12","author":"Kang","year":"2021","journal-title":"Chem. Sci."},{"key":"2026041706015387100_B38","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1039\/D0CB00174K","article-title":"Dehydroamino acid chemical biology: an example of functional group interconversion on proteins","volume":"1","author":"Jones","year":"2020","journal-title":"RSC Chem. Biol."},{"key":"2026041706015387100_B39","doi-asserted-by":"publisher","first-page":"10001","DOI":"10.1021\/bi0007019","article-title":"Nonhydrolyzable diubiquitin analogues are inhibitors of ubiquitin conjugation and deconjugation","volume":"39","author":"Yin","year":"2000","journal-title":"Biochemistry"},{"key":"2026041706015387100_B40","doi-asserted-by":"publisher","first-page":"13496","DOI":"10.1002\/anie.202002974","article-title":"An E1-catalyzed chemoenzymatic strategy to isopeptide-N-ethylated deubiquitylase-resistant ubiquitin probes","volume":"59","author":"Zheng","year":"2020","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026041706015387100_B41","doi-asserted-by":"publisher","first-page":"9478","DOI":"10.1021\/jacs.8b03572","article-title":"Hydrazide mimics for protein lysine acylation to assess nucleosome dynamics and deubiquitinase action","volume":"140","author":"Bhat","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B42","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1124\/pr.118.015651","article-title":"Protein engineering in the ubiquitin system: tools for discovery and beyond","volume":"72","author":"Zhao","year":"2020","journal-title":"Pharmacol. Rev."},{"key":"2026041706015387100_B43","doi-asserted-by":"publisher","first-page":"17536","DOI":"10.1021\/ja205630g","article-title":"Directed evolution of sortase A mutants with altered substrate selectivity profiles","volume":"133","author":"Piotukh","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B44","doi-asserted-by":"publisher","first-page":"e37231","DOI":"10.7554\/eLife.37231","article-title":"Lysine-14 acetylation of histone H3 in chromatin confers resistance to the deacetylase and demethylase activities of an epigenetic silencing complex","volume":"7","author":"Wu","year":"2018","journal-title":"Elife"},{"key":"2026041706015387100_B45","doi-asserted-by":"publisher","first-page":"9377","DOI":"10.1002\/anie.201204538","article-title":"Efficient N-terminal labeling of proteins by use of sortase","volume":"51","author":"Williamson","year":"2012","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026041706015387100_B46","doi-asserted-by":"publisher","first-page":"3360","DOI":"10.1021\/jacs.1c13555","article-title":"Histone H2B deacylation selectivity: exploring chromatin's dark matter with an engineered sortase","volume":"144","author":"Wang","year":"2022","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B47","doi-asserted-by":"crossref","first-page":"101638","DOI":"10.1016\/j.xcrp.2023.101638","article-title":"Deciphering histone H4 lysine acetylation and methylation via sortase-mediated semisynthesis","volume":"4","author":"Xiao","year":"2023","journal-title":"Cell Rep. Phys. Sci."},{"key":"2026041706015387100_B48","doi-asserted-by":"publisher","first-page":"e202401961","DOI":"10.1002\/chem.202401961","article-title":"Robust and irreversible sortase-mediated ligation by employment of sarkosyl","volume":"30","author":"Xiao","year":"2024","journal-title":"Chem. Eur. J."},{"key":"2026041706015387100_B49","doi-asserted-by":"publisher","first-page":"33914","DOI":"10.1021\/jacs.4c12585","article-title":"Circular engineered sortase for interrogating histone H3 in chromatin","volume":"146","author":"Whedon","year":"2024","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B50","doi-asserted-by":"publisher","first-page":"e202109032","DOI":"10.1002\/anie.202109032","article-title":"Sortase-mediated multi-fragment assemblies by ligation site switching","volume":"61","author":"Bierlmeier","year":"2022","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026041706015387100_B51","doi-asserted-by":"publisher","first-page":"e202209945","DOI":"10.1002\/anie.202209945","article-title":"A general method to edit histone H3 modifications on chromatin Via sortase-mediated metathesis","volume":"61","author":"Yang","year":"2022","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026041706015387100_B52","doi-asserted-by":"publisher","first-page":"9218","DOI":"10.1039\/D0SC03407J","article-title":"Examining histone modification crosstalk using immobilized libraries established from ligation-ready nucleosomes","volume":"11","author":"Aparicio Pelaz","year":"2020","journal-title":"Chem. Sci."},{"key":"2026041706015387100_B53","article-title":"Flexible and site-specific manipulation of histones in live animals","author":"Finkin-Groner","year":"2023","journal-title":"bioRxiv"},{"key":"2026041706015387100_B54","doi-asserted-by":"publisher","first-page":"118049","DOI":"10.1016\/j.bmc.2024.118049","article-title":"Expanding horizons: genetic code expansion technology in the study of PTM functions","volume":"118","author":"Chen","year":"2025","journal-title":"Bioorg. Med. Chem."},{"key":"2026041706015387100_B55","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.molcel.2009.07.027","article-title":"A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation","volume":"36","author":"Neumann","year":"2009","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B56","doi-asserted-by":"publisher","first-page":"14194","DOI":"10.1021\/ja906603s","article-title":"Genetically encoding N(epsilon)-methyl-L-lysine in recombinant histones","volume":"131","author":"Nguyen","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B57","doi-asserted-by":"publisher","first-page":"15","DOI":"10.3389\/fchem.2014.00015","article-title":"Unnatural amino acid incorporation in E. coli: current and future applications in the design of therapeutic proteins","volume":"2","author":"Wals","year":"2014","journal-title":"Front. Chem."},{"key":"2026041706015387100_B58","doi-asserted-by":"publisher","first-page":"8262","DOI":"10.1002\/anie.201601938","article-title":"Differentially isotope-labeled nucleosomes to study asymmetric histone modification crosstalk by time-resolved NMR spectroscopy","volume":"55","author":"Liokatis","year":"2016","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026041706015387100_B59","doi-asserted-by":"publisher","first-page":"18243","DOI":"10.1073\/pnas.0804530105","article-title":"Cross-talk between histone H3 tails produces cooperative nucleosome acetylation","volume":"105","author":"Li","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B60","doi-asserted-by":"publisher","first-page":"1124","DOI":"10.1002\/cbic.201800744","article-title":"A Modular ligation strategy for asymmetric bivalent nucleosomes trimethylated at K36 and K27","volume":"20","author":"Guidotti","year":"2019","journal-title":"ChemBioChem"},{"key":"2026041706015387100_B61","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1021\/acscentsci.1c01332","article-title":"A genetically encoded approach for breaking chromatin symmetry","volume":"8","author":"Lukasak","year":"2022","journal-title":"ACS Cent. Sci."},{"key":"2026041706015387100_B62","doi-asserted-by":"publisher","first-page":"762571","DOI":"10.3389\/fcell.2021.762571","article-title":"Nucleosome assembly and disassembly in vitro are governed by chemical kinetic principles","volume":"9","author":"Zhao","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"2026041706015387100_B63","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1016\/j.ab.2012.05.006","article-title":"Polycistronic coexpression and nondenaturing purification of histone octamers","volume":"427","author":"Shim","year":"2012","journal-title":"Anal. Biochem."},{"key":"2026041706015387100_B64","doi-asserted-by":"publisher","first-page":"eabc3393","DOI":"10.1126\/science.abc3393","article-title":"JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications","volume":"371","author":"Kasinath","year":"2021","journal-title":"Science"},{"key":"2026041706015387100_B65","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1038\/s41467-025-61482-x","article-title":"Nucleosome spacing can fine-tune higher order chromatin assembly","volume":"2025","author":"Chen","year":"2025","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B66","doi-asserted-by":"publisher","first-page":"7011","DOI":"10.1038\/s41467-021-27285-6","article-title":"The biogenesis and function of nucleosome arrays","volume":"12","author":"Singh","year":"2021","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B67","doi-asserted-by":"publisher","first-page":"34597","DOI":"10.1074\/jbc.M110.140061","article-title":"Nucleosome interactions and stability in an ordered nucleosome array model system","volume":"285","author":"Blacketer","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B68","doi-asserted-by":"publisher","first-page":"e202500162","DOI":"10.1002\/anie.202500162","article-title":"A method for constructing nucleosome arrays with spatially defined histone PTMs and DNA damage","volume":"64","author":"Liu","year":"2025","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026041706015387100_B69","doi-asserted-by":"publisher","first-page":"11726","DOI":"10.1073\/pnas.92.25.11726","article-title":"Assembly of regularly spaced nucleosome arrays by Drosophila chromatin assembly factor 1 and a 56-kDa histone-binding protein","volume":"92","author":"Bulger","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B70","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1016\/j.cell.2016.09.045","article-title":"Genomic nucleosome organization reconstituted with pure proteins","volume":"167","author":"Krietenstein","year":"2016","journal-title":"Cell"},{"key":"2026041706015387100_B71","doi-asserted-by":"publisher","first-page":"3232","DOI":"10.1038\/s41467-021-23015-0","article-title":"Ruler elements in chromatin remodelers set nucleosome array spacing and phasing","volume":"12","author":"Oberbeckmann","year":"2021","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B72","doi-asserted-by":"publisher","first-page":"607","DOI":"10.1038\/nature23671","article-title":"ISWI chromatin remodellers sense nucleosome modifications to determine substrate preference","volume":"548","author":"Dann","year":"2017","journal-title":"Nature"},{"key":"2026041706015387100_B73","doi-asserted-by":"publisher","first-page":"15029","DOI":"10.1021\/jacs.9b02321","article-title":"Nucleation and propagation of heterochromatin by the histone methyltransferase PRC2: Geometric constraints and impact of the regulatory subunit JARID2","volume":"141","author":"Ge","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B74","doi-asserted-by":"publisher","first-page":"9903","DOI":"10.1038\/s41598-020-66259-4","article-title":"Constructing arrays of nucleosome positioning sequences using Gibson Assembly for single-molecule studies","volume":"10","author":"Spakman","year":"2020","journal-title":"Sci. Rep."},{"key":"2026041706015387100_B75","doi-asserted-by":"publisher","first-page":"2449","DOI":"10.1007\/s13361-019-02303-6","article-title":"Quantitation of single and combinatorial histone modifications by integrated chromatography of bottom-up peptides and middle-down polypeptide tails","volume":"30","author":"Janssen","year":"2019","journal-title":"J. Am. Soc. Mass. Spectrom."},{"key":"2026041706015387100_B76","doi-asserted-by":"publisher","first-page":"953","DOI":"10.1038\/nbt.3652","article-title":"Co-ChIP enables genome-wide mapping of histone mark co-occurrence at single-molecule resolution","volume":"34","author":"Weiner","year":"2016","journal-title":"Nat. Biotechnol."},{"key":"2026041706015387100_B77","doi-asserted-by":"publisher","first-page":"4736","DOI":"10.1016\/j.molcel.2021.09.019","article-title":"Simultaneous profiling of multiple chromatin proteins in the same cells","volume":"81","author":"Gopalan","year":"2021","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B78","article-title":"Global mapping of combinatorial chromatin regulatory events using Hi-Plex CUT&Tag","author":"Liao","year":"2025","journal-title":"bioRxiv"},{"key":"2026041706015387100_B79","doi-asserted-by":"publisher","first-page":"206","DOI":"10.1016\/j.molcel.2019.07.015","article-title":"CoBATCH for high-throughput single-cell epigenomic profiling","volume":"76","author":"Wang","year":"2019","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B80","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1038\/s41592-023-02090-9","article-title":"Combinatorial single-cell profiling of major chromatin types with MAbID","volume":"21","author":"Lochs","year":"2024","journal-title":"Nat. Methods"},{"key":"2026041706015387100_B81","doi-asserted-by":"publisher","first-page":"4446","DOI":"10.1038\/s41596-021-00585-3","article-title":"Genome-wide and sister chromatid-resolved profiling of protein occupancy in replicated chromatin with ChOR-seq and SCAR-seq","volume":"16","author":"Petryk","year":"2021","journal-title":"Nat. Protoc."},{"key":"2026041706015387100_B82","doi-asserted-by":"publisher","first-page":"692","DOI":"10.1016\/j.cell.2011.03.053","article-title":"Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions","volume":"145","author":"Ruthenburg","year":"2011","journal-title":"Cell"},{"key":"2026041706015387100_B83","doi-asserted-by":"publisher","first-page":"e78866","DOI":"10.7554\/eLife.78866","article-title":"Nucleosome conformation dictates the histone code","volume":"13","author":"Marunde","year":"2024","journal-title":"Elife"},{"key":"2026041706015387100_B84","doi-asserted-by":"publisher","first-page":"6218","DOI":"10.1021\/acs.analchem.9b05394","article-title":"An integrated approach for combinatorial readout of dual histone modifications by epigenetic tandem domains","volume":"92","author":"Chen","year":"2020","journal-title":"Anal. Chem."},{"key":"2026041706015387100_B85","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.chembiol.2017.10.008","article-title":"Engineered multivalent sensors to detect coexisting histone modifications in living stem cells","volume":"25","author":"Delachat","year":"2018","journal-title":"Cell Chem. Biol."},{"key":"2026041706015387100_B86","doi-asserted-by":"publisher","first-page":"1288","DOI":"10.1101\/gad.220467.113","article-title":"Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation","volume":"27","author":"Rothbart","year":"2013","journal-title":"Genes Dev."},{"key":"2026041706015387100_B87","doi-asserted-by":"publisher","first-page":"1067","DOI":"10.1038\/nature09504","article-title":"Selective inhibition of BET bromodomains","volume":"468","author":"Filippakopoulos","year":"2010","journal-title":"Nature"},{"key":"2026041706015387100_B88","doi-asserted-by":"publisher","first-page":"9103","DOI":"10.1073\/pnas.1408293111","article-title":"Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D","volume":"111","author":"Bhattacharya","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B89","doi-asserted-by":"publisher","first-page":"2753","DOI":"10.1021\/acschembio.2c00266","article-title":"Identification of histone peptide binding specificity and small-molecule ligands for the TRIM33alpha and TRIM33beta bromodomains","volume":"17","author":"Sekirnik","year":"2022","journal-title":"ACS Chem. Biol."},{"key":"2026041706015387100_B90","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1042\/BCJ20230011","article-title":"Novel insights into the recognition of acetylated histone H4 tail by the TRIM24 PHD-Bromo module","volume":"480","author":"Bardhan","year":"2023","journal-title":"Biochem. J."},{"key":"2026041706015387100_B91","doi-asserted-by":"publisher","first-page":"1489","DOI":"10.1038\/s41467-017-01598-x","article-title":"Accessibility of the histone H3 tail in the nucleosome for binding of paired readers","volume":"8","author":"Gatchalian","year":"2017","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B92","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1016\/j.molcel.2016.06.035","article-title":"ZMYND8 reads the dual histone mark H3K4me1-H3K14ac to antagonize the expression of metastasis-linked genes","volume":"63","author":"Li","year":"2016","journal-title":"Mol. Cell."},{"key":"2026041706015387100_B93","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1038\/nature13045","article-title":"ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression","volume":"508","author":"Wen","year":"2014","journal-title":"Nature"},{"key":"2026041706015387100_B94","doi-asserted-by":"publisher","first-page":"852","DOI":"10.1038\/s41586-020-2533-0","article-title":"Histone H3.3 phosphorylation amplifies stimulation-induced transcription","volume":"583","author":"Armache","year":"2020","journal-title":"Nature"},{"key":"2026041706015387100_B95","doi-asserted-by":"publisher","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":"2026041706015387100_B96","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/j.molcel.2005.06.010","article-title":"Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1","volume":"19","author":"Shahbazian","year":"2005","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B97","doi-asserted-by":"publisher","first-page":"27365","DOI":"10.1073\/pnas.2001075117","article-title":"DOT1L-controlled cell-fate determination and transcription elongation are independent of H3K79 methylation","volume":"117","author":"Cao","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B98","doi-asserted-by":"publisher","first-page":"100897","DOI":"10.1016\/j.mcpro.2024.100897","article-title":"Development of a high-throughput platform for quantitation of histone modifications on a new QTOF I-instrument","volume":"24","author":"Zahn","year":"2025","journal-title":"Mol. Cell. Proteomics"},{"key":"2026041706015387100_B99","doi-asserted-by":"publisher","first-page":"1345","DOI":"10.1101\/gad.2057811","article-title":"The diverse functions of Dot1 and H3K79 methylation","volume":"25","author":"Nguyen","year":"2011","journal-title":"Genes Dev."},{"key":"2026041706015387100_B100","doi-asserted-by":"publisher","first-page":"eadt8765","DOI":"10.1126\/sciadv.adt8765","article-title":"H3K79 methylation and H3K36 trimethylation synergistically regulate gene expression in pluripotent stem cells","volume":"11","author":"Cooke","year":"2025","journal-title":"Sci. Adv."},{"key":"2026041706015387100_B101","doi-asserted-by":"publisher","first-page":"881","DOI":"10.1038\/nsmb.1454","article-title":"A comprehensive library of histone mutants identifies nucleosomal residues required for H3K4 methylation","volume":"15","author":"Nakanishi","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026041706015387100_B102","doi-asserted-by":"publisher","first-page":"558","DOI":"10.1016\/j.cell.2014.09.049","article-title":"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation","volume":"159","author":"Li","year":"2014","journal-title":"Cell"},{"key":"2026041706015387100_B103","doi-asserted-by":"publisher","first-page":"812","DOI":"10.1038\/nature06906","article-title":"Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation","volume":"453","author":"McGinty","year":"2008","journal-title":"Nature"},{"key":"2026041706015387100_B104","doi-asserted-by":"publisher","first-page":"eabc663","DOI":"10.1126\/science.abc6663","article-title":"Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation","volume":"371","author":"Valencia-Sanchez","year":"2021","journal-title":"Science"},{"key":"2026041706015387100_B105","doi-asserted-by":"publisher","first-page":"110369","DOI":"10.1016\/j.celrep.2022.110369","article-title":"DOT1L activity in leukemia cells requires interaction with ubiquitylated H2B that promotes productive nucleosome binding","volume":"38","author":"Spangler","year":"2022","journal-title":"Cell Rep."},{"key":"2026041706015387100_B106","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1101\/gad.323790.118","article-title":"Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase","volume":"33","author":"Jang","year":"2019","journal-title":"Genes Dev."},{"key":"2026041706015387100_B107","doi-asserted-by":"publisher","first-page":"1490","DOI":"10.1016\/j.cell.2019.02.002","article-title":"Mechanism of cross-talk between H2B ubiquitination and H3 methylation by Dot1L","volume":"176","author":"Worden","year":"2019","journal-title":"Cell"},{"key":"2026041706015387100_B108","doi-asserted-by":"publisher","first-page":"4574","DOI":"10.1038\/s41467-018-07072-6","article-title":"Structural insights into the pi-pi-pi stacking mechanism and DNA-binding activity of the YEATS domain","volume":"9","author":"Klein","year":"2018","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B109","doi-asserted-by":"publisher","first-page":"1233","DOI":"10.1016\/j.str.2025.04.010","article-title":"The YEATS domain is a selective reader of histone methacrylation","volume":"33","author":"Becht","year":"2025","journal-title":"Structure"},{"key":"2026041706015387100_B110","doi-asserted-by":"publisher","first-page":"194560","DOI":"10.1016\/j.bbagrm.2020.194560","article-title":"The complex activities of the SET1\/MLL complex core subunits in development and disease","volume":"1863","author":"Jiang","year":"2020","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"2026041706015387100_B111","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1016\/j.cell.2007.05.009","article-title":"High-resolution profiling of histone methylations in the human genome","volume":"129","author":"Barski","year":"2007","journal-title":"Cell"},{"key":"2026041706015387100_B112","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1016\/j.molcel.2017.10.013","article-title":"Determinants of histone H3K4 methylation patterns","volume":"68","author":"Soares","year":"2017","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B113","doi-asserted-by":"publisher","first-page":"e53199","DOI":"10.7554\/eLife.53199","article-title":"Structural basis for COMPASS recognition of an H2B-ubiquitinated nucleosome","volume":"9","author":"Worden","year":"2020","journal-title":"Elife"},{"key":"2026041706015387100_B114","doi-asserted-by":"publisher","first-page":"e82596","DOI":"10.7554\/eLife.82596","article-title":"An acetylation-mediated chromatin switch governs H3K4 methylation read-write capability","volume":"12","author":"Jain","year":"2023","journal-title":"Elife"},{"key":"2026041706015387100_B115","doi-asserted-by":"publisher","first-page":"107527","DOI":"10.1016\/j.jbc.2024.107527","article-title":"Histone H3K18 & H3K23 acetylation directs establishment of MLL-mediated H3K4 methylation","volume":"300","author":"Fox","year":"2024","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B116","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.molcel.2019.03.011","article-title":"Molecular mechanisms directing PRC2 recruitment and H3K27 methylation","volume":"74","author":"Laugesen","year":"2019","journal-title":"Mol. Cell"},{"key":"2026041706015387100_B117","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1038\/nm.4036","article-title":"Targeting EZH2 in cancer","volume":"22","author":"Kim","year":"2016","journal-title":"Nat. Med."},{"key":"2026041706015387100_B118","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1038\/s41416-019-0615-2","article-title":"Engaging chromatin: PRC2 structure meets function","volume":"122","author":"Chammas","year":"2020","journal-title":"Br. J. Cancer"},{"key":"2026041706015387100_B119","doi-asserted-by":"publisher","first-page":"4592","DOI":"10.1038\/s41467-021-24866-3","article-title":"PALI1 facilitates DNA and nucleosome binding by PRC2 and triggers an allosteric activation of catalysis","volume":"12","author":"Zhang","year":"2021","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B120","doi-asserted-by":"publisher","first-page":"e51989","DOI":"10.15252\/embr.202051989","article-title":"H4K20me1 and H3K27me3 are concurrently loaded onto the inactive X chromosome but dispensable for inducing gene silencing","volume":"22","author":"Tjalsma","year":"2021","journal-title":"EMBO Rep."},{"key":"2026041706015387100_B121","doi-asserted-by":"publisher","first-page":"e61964","DOI":"10.7554\/eLife.61964","article-title":"Structural basis for PRC2 decoding of active histone methylation marks H3K36me2\/3","volume":"9","author":"Finogenova","year":"2020","journal-title":"Elife"},{"key":"2026041706015387100_B122","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1038\/s41594-024-01452-x","article-title":"Structural basis for the inhibition of PRC2 by active transcription histone posttranslational modifications","volume":"32","author":"Cookis","year":"2025","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026041706015387100_B123","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1016\/j.molcel.2018.03.019","article-title":"Distinct stimulatory mechanisms regulate the catalytic activity of polycomb repressive complex 2","volume":"70","author":"Lee","year":"2018","journal-title":"Mol. Cell."},{"key":"2026041706015387100_B124","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1016\/j.molcel.2011.03.025","article-title":"Histone methylation by PRC2 is inhibited by active chromatin marks","volume":"42","author":"Schmitges","year":"2011","journal-title":"Mol. Cell."},{"key":"2026041706015387100_B125","doi-asserted-by":"publisher","first-page":"940","DOI":"10.1126\/science.aar5700","article-title":"Structures of human PRC2 with its cofactors AEBP2 and JARID2","volume":"359","author":"Kasinath","year":"2018","journal-title":"Science"},{"key":"2026041706015387100_B126","doi-asserted-by":"publisher","first-page":"8295","DOI":"10.1073\/pnas.1819029116","article-title":"Histone H3 tail binds a unique sensing pocket in EZH2 to activate the PRC2 methyltransferase","volume":"116","author":"Jani","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B127","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1016\/j.molcel.2024.11.009","article-title":"DNA hypomethylation promotes UHRF1-and SUV39H1\/H2-dependent crosstalk between H3K18ub and H3K9me3 to reinforce heterochromatin states","volume":"85","author":"Liu","year":"2025","journal-title":"Mol. Cell."},{"key":"2026041706015387100_B128","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.17101","article-title":"Hemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1","volume":"5","author":"Harrison","year":"2016","journal-title":"Elife"},{"key":"2026041706015387100_B129","doi-asserted-by":"publisher","first-page":"2057","DOI":"10.1038\/s41467-017-02259-9","article-title":"H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1","volume":"8","author":"Jurkowska","year":"2017","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B130","first-page":"1803","article-title":"SETDB1 in cancer: overexpression and its therapeutic implications","volume":"11","author":"Lazaro-Camp","year":"2021","journal-title":"Am. J. Cancer Res."},{"key":"2026041706015387100_B131","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1016\/j.str.2023.12.001","article-title":"Structural evidence for protein-protein interaction between the non-canonical methyl-CpG-binding domain of SETDB proteins and C11orf46","volume":"32","author":"Mahana","year":"2024","journal-title":"Structure"},{"key":"2026041706015387100_B132","doi-asserted-by":"publisher","first-page":"13690","DOI":"10.1093\/nar\/gkae1053","article-title":"SETDB1 activity is globally directed by H3K14 acetylation via its Triple Tudor Domain","volume":"52","author":"Chandrasekaran","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"2026041706015387100_B133","doi-asserted-by":"publisher","first-page":"e2321859121","DOI":"10.1073\/pnas.2321859121","article-title":"H3K14ac facilitates the reinstallation of constitutive heterochromatin in Drosophila early embryos by engaging Eggless\/SetDB1","volume":"121","author":"Tang","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B134","doi-asserted-by":"publisher","first-page":"919","DOI":"10.1101\/gad.973302","article-title":"SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase t hat contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins","volume":"16","author":"Schultz","year":"2002","journal-title":"Genes Dev."},{"key":"2026041706015387100_B135","doi-asserted-by":"publisher","first-page":"2041","DOI":"10.1101\/gad.244848.114","article-title":"Setdb1 is required for germline development and silencing of H3K9me3-marked endogenous retroviruses in primordial germ cells","volume":"28","author":"Liu","year":"2014","journal-title":"Genes Dev."},{"key":"2026041706015387100_B136","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1038\/s41420-023-01489-9","article-title":"Histone demethylases in the regulation of immunity and inflammation","volume":"9","author":"Qu","year":"2023","journal-title":"Cell Death Discov."},{"key":"2026041706015387100_B137","doi-asserted-by":"publisher","first-page":"4896","DOI":"10.1038\/onc.2010.234","article-title":"Requirement of the histone demethylase LSD1 in Snai1-mediated transcriptional repression during epithelial-mesenchymal transition","volume":"29","author":"Lin","year":"2010","journal-title":"Oncogene"},{"key":"2026041706015387100_B138","doi-asserted-by":"publisher","first-page":"508","DOI":"10.1038\/nature09272","article-title":"PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression","volume":"466","author":"Liu","year":"2010","journal-title":"Nature"},{"key":"2026041706015387100_B139","doi-asserted-by":"publisher","first-page":"804","DOI":"10.1016\/j.tibs.2024.06.009","article-title":"Versatile JMJD proteins: juggling histones and much more","volume":"49","author":"Oh","year":"2024","journal-title":"Trends Biochem. Sci."},{"key":"2026041706015387100_B140","doi-asserted-by":"publisher","first-page":"941","DOI":"10.1016\/j.cell.2004.12.012","article-title":"Histone demethylation mediated by the nuclear amine oxidase homolog LSD1","volume":"119","author":"Shi","year":"2004","journal-title":"Cell"},{"key":"2026041706015387100_B141","doi-asserted-by":"publisher","first-page":"561","DOI":"10.1016\/j.cbpa.2007.07.014","article-title":"LSD1 and the chemistry of histone demethylation","volume":"11","author":"Culhane","year":"2007","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2026041706015387100_B142","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1016\/j.celrep.2019.03.061","article-title":"A tail-based mechanism drives nucleosome demethylation by the LSD2\/NPAC multimeric complex","volume":"27","author":"Marabelli","year":"2019","journal-title":"Cell Rep."},{"key":"2026041706015387100_B143","doi-asserted-by":"publisher","first-page":"5440","DOI":"10.1021\/bi900499w","article-title":"Use of pH and kinetic isotope effects to establish chemistry as rate-limiting in oxidation of a peptide substrate by LSD1","volume":"48","author":"Gaweska","year":"2009","journal-title":"Biochemistry"},{"key":"2026041706015387100_B144","doi-asserted-by":"publisher","first-page":"e25444","DOI":"10.1371\/journal.pone.0025444","article-title":"Catalytic mechanism investigation of lysine-specific demethylase 1 (LSD1): a computational study","volume":"6","author":"Kong","year":"2011","journal-title":"PloS ONE"},{"key":"2026041706015387100_B145","doi-asserted-by":"publisher","first-page":"6811","DOI":"10.1021\/jacs.2c13512","article-title":"Structural basis of sirtuin 6-catalyzed nucleosome deacetylation","volume":"145","author":"Wang","year":"2023","journal-title":"J. Am. Chem. Soc."},{"key":"2026041706015387100_B146","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1038\/s41467-018-07829-z","article-title":"Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling","volume":"10","author":"Longbotham","year":"2019","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B147","doi-asserted-by":"publisher","first-page":"6102","DOI":"10.1093\/nar\/gkw193","article-title":"Chromatin condensation and recruitment of PHD finger proteins to histone H3K4me3 are mutually exclusive","volume":"44","author":"Gatchalian","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"2026041706015387100_B148","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1038\/s41589-024-01671-9","article-title":"Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1","volume":"21","author":"Lee","year":"2025","journal-title":"Nat. Chem. Biol."},{"key":"2026041706015387100_B149","doi-asserted-by":"publisher","first-page":"20070","DOI":"10.1074\/jbc.C700100200","article-title":"Structural basis of LSD1-CoREST selectivity in histone H3 recognition","volume":"282","author":"Forneris","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B150","doi-asserted-by":"publisher","first-page":"8058","DOI":"10.1021\/bi700664y","article-title":"Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine","volume":"46","author":"Yang","year":"2007","journal-title":"Biochemistry"},{"key":"2026041706015387100_B151","doi-asserted-by":"publisher","first-page":"12509","DOI":"10.1073\/pnas.1207892109","article-title":"LSD1\/CoREST is an allosteric nanoscale clamp regulated by H3-histone-tail molecular recognition","volume":"109","author":"Baron","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B152","doi-asserted-by":"publisher","first-page":"41360","DOI":"10.1074\/jbc.M509549200","article-title":"Human histone demethylase LSD1 reads the histone code","volume":"280","author":"Forneris","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B153","doi-asserted-by":"publisher","first-page":"792","DOI":"10.1038\/nature08839","article-title":"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4","volume":"464","author":"Metzger","year":"2010","journal-title":"Nature"},{"key":"2026041706015387100_B154","doi-asserted-by":"publisher","first-page":"e57663","DOI":"10.7554\/eLife.57663","article-title":"Diverse nucleosome Site-Selectivity among histone deacetylase complexes","volume":"9","author":"Wang","year":"2020","journal-title":"Elife"},{"key":"2026041706015387100_B155","doi-asserted-by":"publisher","first-page":"18505","DOI":"10.1073\/pnas.1202070109","article-title":"Histone H3K4 demethylation is negatively regulated by histone H3 acetylation in Saccharomyces cerevisiae","volume":"109","author":"Maltby","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B156","doi-asserted-by":"publisher","first-page":"959","DOI":"10.1093\/nar\/gkh252","article-title":"The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases","volume":"32","author":"Yang","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"2026041706015387100_B157","doi-asserted-by":"publisher","first-page":"14065","DOI":"10.1073\/pnas.222373899","article-title":"Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor","volume":"99","author":"Poux","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026041706015387100_B158","doi-asserted-by":"publisher","first-page":"2896","DOI":"10.1074\/mcp.M114.038174","article-title":"The bromodomain of Gcn5 regulates site specificity of lysine acetylation on histone H3","volume":"13","author":"Cieniewicz","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"2026041706015387100_B159","doi-asserted-by":"publisher","first-page":"E5461","DOI":"10.1073\/pnas.1508449112","article-title":"Nucleosome competition reveals processive acetylation by the SAGA HAT module","volume":"112","author":"Ringel","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026041706015387100_B160","doi-asserted-by":"publisher","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":"2026041706015387100_B161","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1038\/s41467-023-36063-5","article-title":"Structural mechanism of BRD4-NUT and p300 bipartite interaction in propagating aberrant gene transcription in chromatin in NUT carcinoma","volume":"14","author":"Yu","year":"2023","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B162","doi-asserted-by":"publisher","first-page":"33721","DOI":"10.1074\/jbc.M104736200","article-title":"Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity","volume":"276","author":"Thompson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B163","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1038\/emboj.2010.318","article-title":"Distinct roles of GCN5\/PCAF-mediated H3K9ac and CBP\/p300-mediated H3K18\/27ac in nuclear receptor transactivation","volume":"30","author":"Jin","year":"2011","journal-title":"EMBO J."},{"key":"2026041706015387100_B164","doi-asserted-by":"publisher","first-page":"7759","DOI":"10.1038\/s41467-022-35375-2","article-title":"Structural insights into p300 regulation and acetylation-dependent genome organisation","volume":"13","author":"Ibrahim","year":"2022","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B165","doi-asserted-by":"publisher","first-page":"15912","DOI":"10.1038\/s41598-021-95398-5","article-title":"Investigating crosstalk between H3K27 acetylation and H3K4 trimethylation in CRISPR\/dCas-based epigenome editing and gene activation","volume":"11","author":"Zhao","year":"2021","journal-title":"Sci. Rep."},{"key":"2026041706015387100_B166","doi-asserted-by":"publisher","first-page":"1147","DOI":"10.1007\/s00018-010-0599-9","article-title":"MYST-family histone acetyltransferases: beyond chromatin","volume":"68","author":"Sapountzi","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"2026041706015387100_B167","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1007\/978-3-642-55747-7_8","article-title":"The MYST family of histone acetyltransferases","volume":"274","author":"Utley","year":"2003","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"2026041706015387100_B168","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1021\/bi602513x","article-title":"Catalytic mechanism of a MYST family histone acetyltransferase","volume":"46","author":"Berndsen","year":"2007","journal-title":"Biochemistry"},{"key":"2026041706015387100_B169","doi-asserted-by":"publisher","first-page":"186","DOI":"10.4161\/epi.26792","article-title":"Crosstalk between epigenetic readers regulates the MOZ\/MORF HAT complexes","volume":"9","author":"Klein","year":"2014","journal-title":"Epigenetics"},{"key":"2026041706015387100_B170","doi-asserted-by":"publisher","first-page":"930","DOI":"10.4161\/cc.9.5.10931","article-title":"Tip60: connecting chromatin to DNA damage signaling","volume":"9","author":"Sun","year":"2010","journal-title":"Cell Cycle"},{"key":"2026041706015387100_B171","doi-asserted-by":"publisher","first-page":"176","DOI":"10.15252\/embj.201591293","article-title":"BRPF3-HBO1 regulates replication origin activation and histone H3K14 acetylation","volume":"35","author":"Feng","year":"2016","journal-title":"EMBO J."},{"key":"2026041706015387100_B172","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1210\/me.2016-1024","article-title":"KAT8 regulates androgen signaling in prostate cancer cells","volume":"30","author":"Kim","year":"2016","journal-title":"Mol. Endocrinol."},{"key":"2026041706015387100_B173","doi-asserted-by":"publisher","first-page":"843","DOI":"10.1038\/embor.2009.168","article-title":"Insights into SAGA function during gene expression","volume":"10","author":"Rodriguez-Navarro","year":"2009","journal-title":"EMBO Rep."},{"key":"2026041706015387100_B174","doi-asserted-by":"publisher","first-page":"194600","DOI":"10.1016\/j.bbagrm.2020.194600","article-title":"The SAGA continues: the rise of cis- and trans-histone crosstalk pathways","volume":"1864","author":"Strahl","year":"2021","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"2026041706015387100_B175","doi-asserted-by":"publisher","first-page":"989","DOI":"10.1038\/s41594-021-00682-7","article-title":"Structure of the human SAGA coactivator complex","volume":"28","author":"Herbst","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026041706015387100_B176","doi-asserted-by":"publisher","first-page":"1999","DOI":"10.1101\/gad.250225.114","article-title":"The SAGA coactivator complex acts on the whole transcribed genome and is required for RNA polymerase II transcription","volume":"28","author":"Bonnet","year":"2014","journal-title":"Genes Dev."},{"key":"2026041706015387100_B177","doi-asserted-by":"publisher","first-page":"2829","DOI":"10.1038\/emboj.2011.193","article-title":"Sgf29 binds histone H3K4me2\/3 and is required for SAGA complex recruitment and histone H3 acetylation","volume":"30","author":"Bian","year":"2011","journal-title":"EMBO J."},{"key":"2026041706015387100_B178","doi-asserted-by":"publisher","first-page":"9411","DOI":"10.1074\/jbc.M809617200","article-title":"The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes","volume":"284","author":"Li","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B179","doi-asserted-by":"publisher","first-page":"2766","DOI":"10.1101\/gad.1979710","article-title":"Gcn5 regulates the dissociation of SWI\/SNF from chromatin by acetylation of Swi2\/Snf2","volume":"24","author":"Kim","year":"2010","journal-title":"Genes Dev."},{"key":"2026041706015387100_B180","doi-asserted-by":"publisher","first-page":"2419","DOI":"10.1021\/cr500452k","article-title":"Protein lysine acetylation by p300\/CBP","volume":"115","author":"Dancy","year":"2015","journal-title":"Chem. Rev."},{"key":"2026041706015387100_B181","doi-asserted-by":"publisher","DOI":"10.3390\/molecules29194524","article-title":"Targeting CBP and p300: emerging anticancer agents","volume":"29","author":"Masci","year":"2024","journal-title":"Molecules"},{"key":"2026041706015387100_B182","doi-asserted-by":"publisher","first-page":"e63512","DOI":"10.7554\/eLife.63512","article-title":"Promoter-specific changes in initiation, elongation, and homeostasis of histone H3 acetylation during CBP\/p300 inhibition","volume":"10","author":"Hsu","year":"2021","journal-title":"Elife"},{"key":"2026041706015387100_B183","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.cell.2018.04.033","article-title":"Time-resolved analysis reveals rapid dynamics and broad scope of the CBP\/p300 acetylome","volume":"174","author":"Weinert","year":"2018","journal-title":"Cell"},{"key":"2026041706015387100_B184","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1038\/s41586-018-0621-1","article-title":"Transcription factor dimerization activates the p300 acetyltransferase","volume":"562","author":"Ortega","year":"2018","journal-title":"Nature"},{"key":"2026041706015387100_B185","doi-asserted-by":"publisher","first-page":"2133","DOI":"10.1021\/acs.biochem.9b00160","article-title":"Combination targeting of the bromodomain and acetyltransferase active site of p300\/CBP","volume":"58","author":"Zucconi","year":"2019","journal-title":"Biochemistry"},{"key":"2026041706015387100_B186","doi-asserted-by":"publisher","first-page":"4103","DOI":"10.1038\/s41467-023-39735-4","article-title":"Epigenetic mechanisms to propagate histone acetylation by p300\/CBP","volume":"14","author":"Kikuchi","year":"2023","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B187","doi-asserted-by":"publisher","first-page":"650","DOI":"10.1016\/j.str.2017.02.003","article-title":"Recognition of histone H3K14 acylation by MORF","volume":"25","author":"Klein","year":"2017","journal-title":"Structure"},{"key":"2026041706015387100_B188","doi-asserted-by":"publisher","first-page":"1191","DOI":"10.1016\/j.chembiol.2023.07.005","article-title":"Discovery of a highly potent, selective, orally bioavailable inhibitor of KAT6A\/B histone acetyltransferases with efficacy against KAT6A-high ER+ breast cancer","volume":"30","author":"Sharma","year":"2023","journal-title":"Cell Chem. Biol."},{"key":"2026041706015387100_B189","doi-asserted-by":"publisher","first-page":"4724","DOI":"10.1038\/s41467-019-12551-5","article-title":"Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation","volume":"10","author":"Klein","year":"2019","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B190","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1101\/gad.188359.112","article-title":"Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription","volume":"26","author":"Qiu","year":"2012","journal-title":"Genes Dev."},{"key":"2026041706015387100_B191","doi-asserted-by":"publisher","first-page":"a026831","DOI":"10.1101\/cshperspect.a026831","article-title":"HDACs and HDAC inhibitors in cancer development and therapy","volume":"6","author":"Li","year":"2016","journal-title":"Cold Spring Harb. Perspect Med."},{"key":"2026041706015387100_B192","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1042\/bj20021321","article-title":"Histone deacetylases (HDACs): characterization of the classical HDAC family","volume":"370","author":"de Ruijter","year":"2003","journal-title":"Biochem. J."},{"key":"2026041706015387100_B193","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.molonc.2007.01.001","article-title":"The role of histone deacetylases (HDACs) in human cancer","volume":"1","author":"Ropero","year":"2007","journal-title":"Mol. Oncol."},{"key":"2026041706015387100_B194","doi-asserted-by":"publisher","first-page":"2699","DOI":"10.1016\/j.celrep.2020.01.091","article-title":"Mechanism of crosstalk between the LSD1 demethylase and HDAC1 deacetylase in the CoREST complex","volume":"30","author":"Song","year":"2020","journal-title":"Cell Rep."},{"key":"2026041706015387100_B195","doi-asserted-by":"publisher","first-page":"11621","DOI":"10.1074\/jbc.C200045200","article-title":"Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex","volume":"277","author":"Zegerman","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B196","doi-asserted-by":"publisher","first-page":"e13941","DOI":"10.7554\/eLife.13941","article-title":"The structure of the core NuRD repression complex provides insights into its interaction with chromatin","volume":"5","author":"Millard","year":"2016","journal-title":"Elife"},{"key":"2026041706015387100_B197","doi-asserted-by":"publisher","first-page":"11779","DOI":"10.1074\/jbc.M110.208207","article-title":"Plant homeodomain (PHD) fingers of CHD4 are histone H3-binding modules with preference for unmodified H3K4 and methylated H3K9","volume":"286","author":"Mansfield","year":"2011","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B198","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1038\/s41586-023-06349-1","article-title":"Diverse modes of H3K36me3-guided nucleosomal deacetylation by Rpd3S","volume":"620","author":"Guan","year":"2023","journal-title":"Nature"},{"key":"2026041706015387100_B199","doi-asserted-by":"publisher","first-page":"1050","DOI":"10.1126\/science.1139004","article-title":"Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin","volume":"316","author":"Li","year":"2007","journal-title":"Science"},{"key":"2026041706015387100_B200","doi-asserted-by":"publisher","first-page":"3564","DOI":"10.1038\/emboj.2012.221","article-title":"Multivalent di-nucleosome recognition enables the Rpd3S histone deacetylase complex to tolerate decreased H3K36 methylation levels","volume":"31","author":"Huh","year":"2012","journal-title":"EMBO J."},{"key":"2026041706015387100_B201","doi-asserted-by":"publisher","first-page":"1893","DOI":"10.1038\/s41594-023-01121-5","article-title":"Structure of histone deacetylase complex Rpd3S bound to nucleosome","volume":"30","author":"Li","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026041706015387100_B202","doi-asserted-by":"publisher","first-page":"8128","DOI":"10.1038\/s41467-023-43968-8","article-title":"Structure of the complete Saccharomyces cerevisiae Rpd3S-nucleosome complex","volume":"14","author":"Markert","year":"2023","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B203","doi-asserted-by":"publisher","first-page":"790","DOI":"10.1038\/s41422-023-00869-1","article-title":"Structural basis of nucleosome deacetylation and DNA linker tightening by Rpd3S histone deacetylase complex","volume":"33","author":"Dong","year":"2023","journal-title":"Cell Res."},{"key":"2026041706015387100_B204","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1016\/j.cell.2005.10.023","article-title":"Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription","volume":"123","author":"Carrozza","year":"2005","journal-title":"Cell"},{"key":"2026041706015387100_B205","doi-asserted-by":"publisher","first-page":"14796","DOI":"10.1074\/jbc.M116.720193","article-title":"Combinatorial histone readout by the dual plant homeodomain (PHD) fingers of Rco1 mediates Rpd3S chromatin recruitment and the maintenance of transcriptional fidelity","volume":"291","author":"McDaniel","year":"2016","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B206","doi-asserted-by":"publisher","first-page":"eadk7678","DOI":"10.1126\/sciadv.adk7678","article-title":"Structures and dynamics of Rpd3S complex bound to nucleosome","volume":"10","author":"Wang","year":"2024","journal-title":"Sci. Adv."},{"key":"2026041706015387100_B207","doi-asserted-by":"publisher","first-page":"3252","DOI":"10.1038\/s41467-020-17078-8","article-title":"The MiDAC histone deacetylase complex is essential for embryonic development and has a unique multivalent structure","volume":"11","author":"Turnbull","year":"2020","journal-title":"Nat. Commun."},{"key":"2026041706015387100_B208","doi-asserted-by":"publisher","first-page":"eadf7586","DOI":"10.1126\/sciadv.adf7586","article-title":"Cryo-EM structure of the human Sirtuin 6-nucleosome complex","volume":"9","author":"Chio","year":"2023","journal-title":"Sci. Adv."},{"key":"2026041706015387100_B209","doi-asserted-by":"publisher","first-page":"108446","DOI":"10.1016\/j.jbc.2025.108446","article-title":"Structural and enzymatic plasticity of SIRT6 deacylase activity","volume":"301","author":"Wang","year":"2025","journal-title":"J. Biol. Chem."},{"key":"2026041706015387100_B210","doi-asserted-by":"publisher","first-page":"440","DOI":"10.1038\/nature06268","article-title":"SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation","volume":"450","author":"Vaquero","year":"2007","journal-title":"Nature"},{"key":"2026041706015387100_B211","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1038\/nsmb.2990","article-title":"NAD(+)-SIRT1 control of H3K4 trimethylation through circadian deacetylation of MLL1","volume":"22","author":"Aguilar-Arnal","year":"2015","journal-title":"Nat. Struct. Mol. Biol."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/483\/5\/713\/987043\/bcj-2025-0115c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/483\/5\/713\/987043\/bcj-2025-0115c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T10:02:00Z","timestamp":1776420120000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/483\/5\/713\/237440\/Histone-modification-cross-talk-analytical-tools"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4,17]]},"references-count":211,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,5,6]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20250115","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,5]]},"published":{"date-parts":[[2026,4,17]]}}}