{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T16:45:44Z","timestamp":1792082744861,"version":"4.4.0"},"reference-count":63,"publisher":"American Chemical Society (ACS)","issue":"9","license":[{"start":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T00:00:00Z","timestamp":1787529600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T00:00:00Z","timestamp":1787529600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T00:00:00Z","timestamp":1787529600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM142505"],"award-info":[{"award-number":["R35GM142505"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Assigning causal function to post-translational modifications (PTMs) remains a central challenge in molecular biology, as most modification events cannot be readily interrogated in their native cellular context. Here, we present a generalizable chemical biology strategy for investigating the functional consequences of lysine acetylation through programmable induced proximity. By combining modular effector recruitment with chemically controlled proximity, this approach enables systematic elucidation of how enzyme identity shapes acetylation outcomes on target proteins in living cells. Across multiple substrates, including histone H3 and p53, we find that distinct acetyltransferases generate reproducible and target-dependent site-selective acetylation patterns, indicating that effector identity encodes predictable features of modification outcomes. These observations establish a framework for linking enzyme recruitment to site-specific PTM deposition and provide a route to identify candidate functional modification events. Rather than providing a single mechanistic insight, this work introduces a broadly applicable strategy for interrogating causal relationships between proximity-driven enzyme recruitment and protein modification, as demonstrated by the impact of p53 acetylation on downstream transcripts. This platform is readily extensible to additional effectors and targets and enables systematic discovery of functional PTMs in cellular systems.<\/jats:p>","DOI":"10.1021\/acschembio.6c00510","type":"journal-article","created":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T12:03:12Z","timestamp":1788177792000},"page":"2384-2393","source":"Crossref","is-referenced-by-count":0,"title":["General Strategy for Controlling Functional Lysine Acetylation via Induced Proximity"],"prefix":"10.1021","volume":"21","author":[{"given":"Brianna","family":"Hill-Payne","sequence":"first","affiliation":[{"name":"University of Pennsylvania , ,","place":["PA, 19104"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohd. Younis","family":"Bhat","sequence":"additional","affiliation":[{"name":"University of Pennsylvania , ,","place":["PA, 19104"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2812-983X","authenticated-orcid":true,"given":"George M.","family":"Burslem","sequence":"additional","affiliation":[{"name":"University of Pennsylvania , ,","place":["PA, 19104"]},{"name":"Perelman School of Medicine, University of Pennsylvania , ,","place":["PA, 19104"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,24]]},"reference":[{"issue":"3","key":"2026101511072759100_cit1","doi-asserted-by":"publisher","first-page":"1216","DOI":"10.1021\/acs.chemrev.7b00181","article-title":"Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics","volume":"118","author":"Ali","year":"2018","journal-title":"Chem Rev"},{"issue":"10","key":"2026101511072759100_cit2","doi-asserted-by":"publisher","first-page":"1372","DOI":"10.1016\/j.bbapap.2016.06.007","article-title":"The world of protein acetylation","volume":"1864","author":"Drazic","year":"2016","journal-title":"Biochim. Biophys. Acta."},{"key":"2026101511072759100_cit3","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2023.115519","article-title":"Acetylation in pathogenesis: Revealing emerging mechanisms and therapeutic prospects","volume":"167","author":"Jiang","year":"2023","journal-title":"Biomed. Pharmacother."},{"issue":"19","key":"2026101511072759100_cit4","doi-asserted-by":"publisher","first-page":"4499","DOI":"10.1093\/jxb\/ery295","article-title":"Orchestrating the proteome with post-translational modifications","volume":"69","author":"Spoel","year":"2018","journal-title":"J. Exp. Bot."},{"issue":"9","key":"2026101511072759100_cit5","doi-asserted-by":"publisher","first-page":"1868","DOI":"10.1016\/j.molcel.2025.04.002","article-title":"Pooled tagging and hydrophobic targeting of endogenous proteins for unbiased mapping of unfolded protein responses","volume":"85","author":"Sansbury","year":"2025","journal-title":"Mol. Cell."},{"issue":"10","key":"2026101511072759100_cit6","doi-asserted-by":"publisher","DOI":"10.1016\/j.xgen.2024.100651","article-title":"Pooled endogenous protein tagging and recruitment for systematic profiling of protein function","volume":"4","author":"Serebrenik","year":"2024","journal-title":"Cell Genomics."},{"issue":"15","key":"2026101511072759100_cit7","doi-asserted-by":"publisher","first-page":"8554","DOI":"10.1073\/pnas.141230798","article-title":"Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation","volume":"98","author":"Sakamoto","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"33","key":"2026101511072759100_cit8","doi-asserted-by":"publisher","first-page":"14052","DOI":"10.1021\/jacs.0c05537","article-title":"Phosphorylation-Inducing Chimeric Small Molecules","volume":"142","author":"Siriwardena","year":"2020","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026101511072759100_cit9","doi-asserted-by":"publisher","first-page":"904","DOI":"10.1038\/s41467-022-28520-4","article-title":"The AUTOTAC chemical biology platform for targeted protein degradation via the autophagy-lysosome system","volume":"13","author":"Ji","year":"2022","journal-title":"Nat. Commun."},{"key":"2026101511072759100_cit10","doi-asserted-by":"publisher","DOI":"10.1093\/database\/baab012","article-title":"Posttranslational modifications in proteins: resources, tools and prediction methods","volume":"2021","author":"Ramazi","year":"2021","journal-title":"Database (Oxford)"},{"issue":"8","key":"2026101511072759100_cit11","doi-asserted-by":"publisher","first-page":"953","DOI":"10.1016\/j.chembiol.2020.07.002","article-title":"The Chemical Biology of Reversible Lysine Post-translational Modifications","volume":"27","author":"Wang","year":"2020","journal-title":"Cell Chem. Biol."},{"issue":"9","key":"2026101511072759100_cit12","doi-asserted-by":"publisher","first-page":"1918","DOI":"10.1021\/acschembio.4c00438","article-title":"Functional Investigations of p53 Acetylation Enabled by Heterobifunctional Molecules","volume":"19","author":"Chen","year":"2024","journal-title":"ACS Chem. Biol."},{"issue":"4","key":"2026101511072759100_cit13","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1038\/s41589-022-00971-2","article-title":"Deubiquitinase-targeting chimeras for targeted protein stabilization","volume":"18","author":"Henning","year":"2022","journal-title":"Nat. Chem. Biol."},{"issue":"6380","key":"2026101511072759100_cit14","doi-asserted-by":"publisher","DOI":"10.1126\/science.aao5902","article-title":"Chemically induced proximity in biology and medicine","volume":"359","author":"Stanton","year":"2018","journal-title":"Science"},{"issue":"1","key":"2026101511072759100_cit15","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1002\/cbic.202000459","article-title":"Advances and Opportunities in Epigenetic Chemical Biology","volume":"22","author":"Beyer","year":"2021","journal-title":"Chembiochem."},{"issue":"1","key":"2026101511072759100_cit16","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1016\/j.cell.2019.11.031","article-title":"Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery","volume":"181","author":"Burslem","year":"2020","journal-title":"Cell"},{"issue":"17","key":"2026101511072759100_cit17","doi-asserted-by":"publisher","first-page":"2695","DOI":"10.1021\/acs.accounts.5c00326","article-title":"Targeted Protein Acetylation Through Chemically Induced Proximity","volume":"58","author":"Wang","year":"2025","journal-title":"Acc. Chem. Res."},{"issue":"20","key":"2026101511072759100_cit18","doi-asserted-by":"publisher","first-page":"12928","DOI":"10.1093\/nar\/gku962","article-title":"A nanobody modulates the p53 transcriptional program without perturbing its functional architecture","volume":"42","author":"Bethuyne","year":"2014","journal-title":"Nucleic Acids Res."},{"issue":"3","key":"2026101511072759100_cit19","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1038\/s41573-021-00371-6","article-title":"PROTAC targeted protein degraders: the past is prologue","volume":"21","author":"Bekes","year":"2022","journal-title":"Nat. Rev. Drug Discov."},{"issue":"1","key":"2026101511072759100_cit20","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1186\/s13045-020-00885-3","article-title":"Proteolysis-targeting chimera (PROTAC) for targeted protein degradation and cancer therapy","volume":"13","author":"Li","year":"2020","journal-title":"J. Hematol. Oncolo."},{"key":"2026101511072759100_cit21","first-page":"215","volume-title":"Methods Enzymol.","author":"Hill-Payne","year":"2023"},{"issue":"8","key":"2026101511072759100_cit22","doi-asserted-by":"publisher","first-page":"1831","DOI":"10.1021\/acschembio.5b00442","article-title":"HaloPROTACS: Use of Small Molecule PROTACs to Induce Degradation of HaloTag Fusion Proteins","volume":"10","author":"Buckley","year":"2015","journal-title":"ACS Chem. Biol."},{"issue":"40","key":"2026101511072759100_cit23","doi-asserted-by":"publisher","first-page":"16700","DOI":"10.1021\/jacs.1c07850","article-title":"Targeted Protein Acetylation in Cells Using Heterobifunctional Molecules","volume":"143","author":"Wang","year":"2021","journal-title":"J. Am. Chem. Soc."},{"issue":"7","key":"2026101511072759100_cit24","doi-asserted-by":"publisher","first-page":"6897","DOI":"10.1021\/acs.jmedchem.4c02975","article-title":"Deubiquitinase-Targeting Chimeras (DUBTACs) as a Potential Paradigm-Shifting Drug Discovery Approach","volume":"68","author":"Ma","year":"2025","journal-title":"J. Med. Chem."},{"issue":"16","key":"2026101511072759100_cit25","doi-asserted-by":"publisher","first-page":"13754","DOI":"10.1021\/jacs.5c01889","article-title":"USP28-Based Deubiquitinase-Targeting Chimeras for Cancer Treatment","volume":"147","author":"Wang","year":"2025","journal-title":"J. Am. Chem. Soc."},{"issue":"12","key":"2026101511072759100_cit26","doi-asserted-by":"publisher","first-page":"2808","DOI":"10.1021\/acschembio.1c00693","article-title":"Modulation of Phosphoprotein Activity by Phosphorylation Targeting Chimeras (PhosTACs)","volume":"16","author":"Chen","year":"2021","journal-title":"ACS Chem. Biol."},{"issue":"7","key":"2026101511072759100_cit27","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202413377","article-title":"Harnessing the TAF1 Acetyltransferase for Targeted Acetylation of the Tumor Suppressor p53","volume":"12","author":"Kabir","year":"2025","journal-title":"Adv. Sci."},{"issue":"27","key":"2026101511072759100_cit28","doi-asserted-by":"publisher","first-page":"14932","DOI":"10.1021\/jacs.3c04640","article-title":"Acetylation Targeting Chimera Enables Acetylation of the Tumor Suppressor p53","volume":"145","author":"Kabir","year":"2023","journal-title":"J. Am. Chem. Soc."},{"issue":"8009","key":"2026101511072759100_cit29","doi-asserted-by":"publisher","first-page":"878","DOI":"10.1038\/s41586-024-07224-3","article-title":"Proteome-scale discovery of protein degradation and stabilization effectors","volume":"628","author":"Poirson","year":"2024","journal-title":"Nature"},{"issue":"4","key":"2026101511072759100_cit30","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1016\/j.trecan.2025.01.013","article-title":"Acetylation: a new target for protein degradation in cancer","volume":"11","author":"Crawford","year":"2025","journal-title":"Trends Cancer"},{"issue":"4","key":"2026101511072759100_cit31","doi-asserted-by":"publisher","first-page":"2923","DOI":"10.3892\/etm.2020.9073","article-title":"Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review)","volume":"20","author":"Xia","year":"2020","journal-title":"Exp. Ther. Med."},{"issue":"6","key":"2026101511072759100_cit32","doi-asserted-by":"publisher","first-page":"1641","DOI":"10.1038\/s44318-025-00369-5","article-title":"SLC25A1 and ACLY maintain cytosolic acetyl-CoA and regulate ferroptosis susceptibility via FSP1 acetylation","volume":"44","author":"Li","year":"2025","journal-title":"EMBO J."},{"issue":"7243","key":"2026101511072759100_cit33","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1038\/nature07829","article-title":"Histone modifications at human enhancers reflect global cell-type-specific gene expression","volume":"459","author":"Heintzman","year":"2009","journal-title":"Nature"},{"issue":"6","key":"2026101511072759100_cit34","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1021\/cb800025k","article-title":"HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis","volume":"3","author":"Los","year":"2008","journal-title":"ACS Chem. Biol."},{"key":"2026101511072759100_cit35","doi-asserted-by":"publisher","DOI":"10.1101\/2023.07.13.548611","article-title":"Pooled tagging and hydrophobic targeting of endogenous proteins for unbiased mapping of unfolded protein responses","author":"Sansbury","year":"2023","journal-title":"bioRxiv"},{"issue":"8","key":"2026101511072759100_cit36","doi-asserted-by":"publisher","first-page":"1831","DOI":"10.1021\/acschembio.5b00442","article-title":"HaloPROTACS: Use of Small Molecule PROTACs to Induce Degradation of HaloTag Fusion Proteins","volume":"10","author":"Buckley","year":"2015","journal-title":"ACS Chem. Biol."},{"issue":"1","key":"2026101511072759100_cit37","doi-asserted-by":"publisher","first-page":"2073","DOI":"10.1038\/s41467-022-29670-1","article-title":"Development of NanoLuc-targeting protein degraders and a universal reporter system to benchmark tag-targeted degradation platforms","volume":"13","author":"Grohmann","year":"2022","journal-title":"Nat. Commun."},{"issue":"18","key":"2026101511072759100_cit38","doi-asserted-by":"publisher","first-page":"10437","DOI":"10.1073\/pnas.95.18.10437","article-title":"Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity","volume":"95","author":"Clackson","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"8","key":"2026101511072759100_cit39","doi-asserted-by":"publisher","first-page":"1309","DOI":"10.1016\/s0968-0896(98)00125-4","article-title":"Synthesis and activity of bivalent FKBP12 ligands for the regulated dimerization of proteins","volume":"6","author":"Keenan","year":"1998","journal-title":"Bioorg. Med. Chem."},{"issue":"5","key":"2026101511072759100_cit40","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1038\/nmeth.1318","article-title":"Enzymatic assembly of DNA molecules up to several hundred kilobases","volume":"6","author":"Gibson","year":"2009","journal-title":"Nat. Methods."},{"issue":"12","key":"2026101511072759100_cit41","doi-asserted-by":"publisher","first-page":"2389","DOI":"10.1002\/pro.519","article-title":"Structural and thermodynamic analysis of the GFP:GFP-nanobody complex","volume":"19","author":"Kubala","year":"2010","journal-title":"Protein Sci."},{"issue":"7","key":"2026101511072759100_cit42","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0040410","article-title":"A study on the effect of surface lysine to arginine mutagenesis on protein stability and structure using green fluorescent protein","volume":"7","author":"Sokalingam","year":"2012","journal-title":"PLoS ONE"},{"issue":"14","key":"2026101511072759100_cit43","doi-asserted-by":"publisher","first-page":"R546","DOI":"10.1016\/j.cub.2004.07.007","article-title":"Histones and histone modifications","volume":"14","author":"Peterson","year":"2004","journal-title":"Curr. Biol."},{"issue":"10","key":"2026101511072759100_cit44","doi-asserted-by":"publisher","first-page":"2183","DOI":"10.1016\/j.molcel.2021.04.015","article-title":"Targeting histone acetylation dynamics and oncogenic transcription by catalytic P300\/CBP inhibition","volume":"81","author":"Hogg","year":"2021","journal-title":"Mol. Cell"},{"issue":"2","key":"2026101511072759100_cit45","doi-asserted-by":"publisher","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":"2026101511072759100_cit46","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2021.672447","article-title":"The Role of Histone Protein Acetylation in Regulating Endothelial Function","volume":"9","author":"Fang","year":"2021","journal-title":"Front. Cell. Dev. Biol."},{"issue":"2","key":"2026101511072759100_cit47","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1016\/j.molcel.2009.01.007","article-title":"HBO1 HAT complexes target chromatin throughout gene coding regions via multiple PHD finger interactions with histone H3 tail","volume":"33","author":"Saksouk","year":"2009","journal-title":"Mol. Cell."},{"issue":"11","key":"2026101511072759100_cit48","doi-asserted-by":"publisher","first-page":"3537","DOI":"10.7150\/jca.118273","article-title":"H3K14: A histone site closely related to diseases","volume":"16","author":"Fan","year":"2025","journal-title":"J. Cancer"},{"issue":"12","key":"2026101511072759100_cit49","doi-asserted-by":"publisher","first-page":"789","DOI":"10.1046\/j.1365-2443.1998.00229.x","article-title":"Tip60 acetylates six lysines of a specific class in core histones in vitro","volume":"3","author":"Kimura","year":"1998","journal-title":"Genes Cells."},{"issue":"22","key":"2026101511072759100_cit50","doi-asserted-by":"publisher","first-page":"3039","DOI":"10.1038\/s41388-022-02331-9","article-title":"Deciphering the acetylation code of p53 in transcription regulation and tumor suppression","volume":"41","author":"Xia","year":"2022","journal-title":"Oncogene"},{"issue":"4","key":"2026101511072759100_cit51","doi-asserted-by":"publisher","first-page":"612","DOI":"10.1016\/j.cell.2008.03.025","article-title":"Acetylation is indispensable for p53 activation","volume":"133","author":"Tang","year":"2008","journal-title":"Cell"},{"issue":"15","key":"2026101511072759100_cit52","doi-asserted-by":"publisher","DOI":"10.3390\/cancers16152677","article-title":"Evaluating the Cellular Roles of the Lysine Acetyltransferase Tip60 in Cancer: A Multi-Action Molecular Target for Precision Oncology","volume":"16","author":"Zohourian","year":"2024","journal-title":"Cancers"},{"issue":"28","key":"2026101511072759100_cit53","doi-asserted-by":"crossref","first-page":"25568","DOI":"10.1074\/jbc.M212574200","article-title":"Identification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305","volume":"278","author":"Wang","year":"2003","journal-title":"Journal of Biological Chemistry"},{"issue":"29","key":"2026101511072759100_cit54","doi-asserted-by":"publisher","first-page":"19412","DOI":"10.1074\/jbc.M109.014951","article-title":"Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus","volume":"284","author":"Brent","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"1","key":"2026101511072759100_cit55","doi-asserted-by":"publisher","first-page":"30","DOI":"10.3390\/cancers7010030","article-title":"p53 Acetylation: Regulation and Consequences","volume":"7","author":"Reed","year":"2014","journal-title":"Cancers"},{"issue":"6","key":"2026101511072759100_cit56","doi-asserted-by":"publisher","first-page":"1331","DOI":"10.1093\/emboj\/20.6.1331","article-title":"p300\/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2","volume":"20","author":"Ito","year":"2001","journal-title":"EMBO J."},{"issue":"1","key":"2026101511072759100_cit57","doi-asserted-by":"publisher","first-page":"2947","DOI":"10.1038\/s41467-019-10846-1","article-title":"A genetically encoded probe for imaging nascent and mature HA-tagged proteins in vivo","volume":"10","author":"Zhao","year":"2019","journal-title":"Nat. Commun."},{"issue":"6","key":"2026101511072759100_cit58","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."},{"issue":"9","key":"2026101511072759100_cit59","doi-asserted-by":"publisher","first-page":"1040","DOI":"10.1038\/nsmb.2642","article-title":"Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation","volume":"20","author":"Delvecchio","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"1","key":"2026101511072759100_cit60","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."},{"issue":"3","key":"2026101511072759100_cit61","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1007\/s11515-018-1502-6","article-title":"CBP\/p300: intramolecular and intermolecular regulations","volume":"13","author":"Xue","year":"2018","journal-title":"Front. Biol."},{"issue":"4","key":"2026101511072759100_cit62","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1038\/nsmb740","article-title":"Regulation of the p300 HAT domain via a novel activation loop","volume":"11","author":"Thompson","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"6","key":"2026101511072759100_cit63","doi-asserted-by":"publisher","first-page":"696","DOI":"10.4161\/cc.6.6.4013","article-title":"The diverse biological roles of MYST histone acetyltransferase family proteins","volume":"6","author":"Thomas","year":"2007","journal-title":"Cell Cycle"}],"container-title":["ACS Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acschembio.6c00510","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/acbcct\/article-pdf\/21\/9\/2384\/67362012\/cb-2026-00510c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/acbcct\/article-pdf\/21\/9\/2384\/67362012\/cb-2026-00510c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T15:49:33Z","timestamp":1792079373000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/acbcct\/article\/21\/9\/2384\/5325151\/General-Strategy-for-Controlling-Functional-Lysine"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,24]]},"references-count":63,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2026,8,24]]},"published-print":{"date-parts":[[2026,9,18]]}},"URL":"https:\/\/doi.org\/10.1021\/acschembio.6c00510","relation":{},"ISSN":["1554-8929","1554-8937"],"issn-type":[{"value":"1554-8929","type":"print"},{"value":"1554-8937","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,24]]}}}