{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T16:00:55Z","timestamp":1790352055563,"version":"4.1.0"},"reference-count":79,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,15]],"date-time":"2026-08-15T00:00:00Z","timestamp":1786752000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001825","name":"Danish Agency for Higher Education and Science","doi-asserted-by":"publisher","award":["5229-00012B"],"award-info":[{"award-number":["5229-00012B"]}],"id":[{"id":"10.13039\/501100001825","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Foundation","doi-asserted-by":"publisher","award":["NNF20OC0061575"],"award-info":[{"award-number":["NNF20OC0061575"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Foundation","doi-asserted-by":"publisher","award":["NNF23OC0083407"],"award-info":[{"award-number":["NNF23OC0083407"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["mcponline.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular & Cellular Proteomics"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.mcpro.2026.101640","type":"journal-article","created":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T23:12:29Z","timestamp":1787008349000},"page":"101640","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Top-Down Sequencing of Intact Proteoforms Using the timsOmni Mass Spectrometer: Accurate Determination of Co-Occurring Histone Modifications"],"prefix":"10.1016","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5178-8967","authenticated-orcid":false,"given":"Francis","family":"Berthias","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7097-7218","authenticated-orcid":false,"given":"Nurg\u00fcl","family":"Bilgin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1677-4214","authenticated-orcid":false,"given":"Athanasios","family":"Smyrnakis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7339-4280","authenticated-orcid":false,"given":"Elisa","family":"Le Boiteux","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8454-5398","authenticated-orcid":false,"given":"Mariangela","family":"Kosmopoulou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Albers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1859-2492","authenticated-orcid":false,"given":"Detlev","family":"Suckau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5559-3822","authenticated-orcid":false,"given":"Jasmin","family":"Mecinovi\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2299-9479","authenticated-orcid":false,"given":"Dimitris","family":"Papanastasiou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1862-8528","authenticated-orcid":false,"given":"Ole N.","family":"Jensen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mcpro.2026.101640_bib1","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1038\/nchembio.2576","article-title":"How many human proteoforms are there?","volume":"14","author":"Aebersold","year":"2018","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib2","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nmeth.2369","article-title":"Proteoform: a single term describing protein complexity","volume":"10","author":"Smith","year":"2013","journal-title":"Nat. Methods"},{"key":"10.1016\/j.mcpro.2026.101640_bib3","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/nrm1939","article-title":"Interpreting the protein language using proteomics","volume":"7","author":"Jensen","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib4","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1004049","article-title":"The roles of post-translational modifications in the context of protein interaction networks","volume":"11","author":"Duan","year":"2015","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib5","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/nsmb.1842","article-title":"Post-translational modifications in signal integration","volume":"17","author":"Deribe","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib6","article-title":"Protein posttranslational modifications in health and diseases: functions, regulatory mechanisms, and therapeutic implications","volume":"4","author":"Zhong","year":"2023","journal-title":"MedComm (2020)"},{"key":"10.1016\/j.mcpro.2026.101640_bib7","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/srep00090","article-title":"Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database","volume":"1","author":"Khoury","year":"2011","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mcpro.2026.101640_bib8","doi-asserted-by":"crossref","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)"},{"key":"10.1016\/j.mcpro.2026.101640_bib9","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1016\/j.molcel.2021.03.015","article-title":"Discovering the landscape of protein modifications","volume":"81","author":"Keenan","year":"2021","journal-title":"Mol. Cell"},{"key":"10.1016\/j.mcpro.2026.101640_bib10","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/47412","article-title":"The language of covalent histone modifications","volume":"403","author":"Strahl","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.mcpro.2026.101640_bib11","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1126\/science.1063127","article-title":"Translating the histone code","volume":"293","author":"Jenuwein","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.mcpro.2026.101640_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.mcpro.2024.100897","article-title":"Development of a high-throughput platform for quantitation of histone modifications on a new QTOF instrument","volume":"24","author":"Zahn","year":"2025","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib13","doi-asserted-by":"crossref","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":"10.1016\/j.mcpro.2026.101640_bib14","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/s42003-020-0898-0","article-title":"Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha","volume":"3","author":"Gao","year":"2020","journal-title":"Commun. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib15","doi-asserted-by":"crossref","first-page":"14456","DOI":"10.1074\/jbc.M117.802074","article-title":"Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation","volume":"292","author":"Gates","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib16","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1186\/1471-2164-11-257","article-title":"Core promoter structure and genomic context reflect histone 3 lysine 9 acetylation patterns","volume":"11","author":"Kratz","year":"2010","journal-title":"BMC Genomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib17","doi-asserted-by":"crossref","first-page":"21931","DOI":"10.1073\/pnas.1016071107","article-title":"Histone H3K27ac separates active from poised enhancers and predicts developmental state","volume":"107","author":"Creyghton","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.mcpro.2026.101640_bib18","doi-asserted-by":"crossref","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":"10.1016\/j.mcpro.2026.101640_bib19","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.cell.2012.06.013","article-title":"Cancer epigenetics: from mechanism to therapy","volume":"150","author":"Dawson","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2026.101640_bib20","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1038\/nrg.2016.93","article-title":"Targeting the cancer epigenome for therapy","volume":"17","author":"Jones","year":"2016","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.mcpro.2026.101640_bib21","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1002\/jcb.20615","article-title":"Histone modifying enzymes and cancer: going beyond histones","volume":"96","author":"Zhang","year":"2005","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.mcpro.2026.101640_bib22","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1038\/nature10849","article-title":"An epigenetic blockade of cognitive functions in the neurodegenerating brain","volume":"483","author":"Gr\u00e4ff","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.mcpro.2026.101640_bib23","doi-asserted-by":"crossref","first-page":"29","DOI":"10.3390\/proteomes6030029","article-title":"Proteomic analysis of histone variants and their PTMs: strategies and pitfalls","volume":"6","author":"El Kennani","year":"2018","journal-title":"Proteomes"},{"key":"10.1016\/j.mcpro.2026.101640_bib24","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/nsmb.1972","article-title":"An assessment of histone-modification antibody quality","volume":"18","author":"Egelhofer","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib25","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1182\/blood-2018-99-115347","article-title":"Epiproteomic landscape and histone code of cutaneous T-Cell Lymphoma\/S\u00e9zary syndrome","volume":"132","author":"Onder","year":"2018","journal-title":"Blood"},{"key":"10.1016\/j.mcpro.2026.101640_bib26","doi-asserted-by":"crossref","first-page":"33585","DOI":"10.1074\/jbc.M803312200","article-title":"Phosphorylation of H3S10 blocks the access of H3K9 by specific antibodies and histone methyltransferase. Implication in regulating chromatin dynamics and epigenetic inheritance during mitosis","volume":"283","author":"Duan","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib27","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1038\/srep00489","article-title":"Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies","volume":"2","author":"Rothbart","year":"2012","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mcpro.2026.101640_bib28","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1080\/14789450.2017.1345632","article-title":"Middle-down proteomics: a still unexploited resource for chromatin biology","volume":"14","author":"Sidoli","year":"2017","journal-title":"Expert Rev. Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib29","doi-asserted-by":"crossref","first-page":"3129","DOI":"10.1021\/acs.analchem.5b00072","article-title":"Bottom-Up and middle-down proteomics have comparable accuracies in defining histone post-translational modification relative abundance and stoichiometry","volume":"87","author":"Sidoli","year":"2015","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib30","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1074\/mcp.M115.048975","article-title":"Top-down and middle-down protein analysis reveals that intact and clipped human histones differ in post-translational modification patterns","volume":"14","author":"Tvardovskiy","year":"2015","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib31","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1074\/mcp.O114.046573","article-title":"Mass spectrometric quantification of histone post-translational modifications by a hybrid chemical labeling method[S]","volume":"14","author":"Maile","year":"2015","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib32","doi-asserted-by":"crossref","first-page":"3386","DOI":"10.1021\/ja039748i","article-title":"Shotgun annotation of histone modifications: a new approach for streamlined characterization of proteins by top Down mass spectrometry","volume":"126","author":"Pesavento","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mcpro.2026.101640_bib33","doi-asserted-by":"crossref","first-page":"3791","DOI":"10.1021\/acs.jproteome.8b00458","article-title":"Increasing the separation capacity of intact histone proteoforms chromatography coupling online weak cation exchange-HILIC to reversed phase LC UVPD-HRMS","volume":"17","author":"Gargano","year":"2018","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.mcpro.2026.101640_bib34","doi-asserted-by":"crossref","first-page":"2200","DOI":"10.1002\/pmic.201400084","article-title":"Middle-down hybrid chromatography\/tandem mass spectrometry workflow for characterization of combinatorial post-translational modifications in histones","volume":"14","author":"Sidoli","year":"2014","journal-title":"Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib35","doi-asserted-by":"crossref","first-page":"2266","DOI":"10.1074\/mcp.M900238-MCP200","article-title":"High throughput characterization of combinatorial histone codes","volume":"8","author":"Young","year":"2009","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib36","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cbpa.2017.10.026","article-title":"The application of ion-mobility mass spectrometry for structure\/function investigation of protein complexes","volume":"42","author":"Ben-Nissan","year":"2018","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib37","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/nchem.1889","article-title":"The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics","volume":"6","author":"Lanucara","year":"2014","journal-title":"Nat. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib38","doi-asserted-by":"crossref","first-page":"2185","DOI":"10.1007\/s13361-019-02288-2","article-title":"Ion mobility spectrometry: fundamental concepts, instrumentation, applications, and the road ahead","volume":"30","author":"Dodds","year":"2019","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101640_bib39","doi-asserted-by":"crossref","first-page":"2318","DOI":"10.1021\/acs.analchem.3c03079","article-title":"Multiplatform high-definition ion mobility separations of the largest epimeric peptides","volume":"96","author":"Thurman","year":"2024","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib40","doi-asserted-by":"crossref","first-page":"2364","DOI":"10.1021\/acs.analchem.9b05011","article-title":"Middle-down proteomic analyses with ion mobility separations of endogenous isomeric proteoforms","volume":"92","author":"Shliaha","year":"2020","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib41","doi-asserted-by":"crossref","first-page":"2918","DOI":"10.1021\/acs.analchem.7b05224","article-title":"Linear and differential ion mobility separations of middle-down proteoforms","volume":"90","author":"Garabedian","year":"2018","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib42","doi-asserted-by":"crossref","first-page":"5461","DOI":"10.1021\/acs.analchem.7b00379","article-title":"Characterization of complete histone tail proteoforms using differential ion mobility spectrometry","volume":"89","author":"Shliaha","year":"2017","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib43","doi-asserted-by":"crossref","DOI":"10.1002\/pmic.202200471","article-title":"Top-down ion mobility\/mass spectrometry reveals enzyme specificity: separation and sequencing of isomeric proteoforms","volume":"24","author":"Berthias","year":"2024","journal-title":"Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib44","first-page":"784","article-title":"Top-down ion mobility separations of isomeric proteoforms","volume":"95","author":"Berthias","year":"2023","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib45","doi-asserted-by":"crossref","first-page":"3265","DOI":"10.1021\/ja973478k","article-title":"Electron capture dissociation of multiply charged protein cations. A nonergodic process","volume":"120","author":"Zubarev","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.mcpro.2026.101640_bib46","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1002\/pmic.201100517","article-title":"Electron transfer dissociation mass spectrometry in proteomics","volume":"12","author":"Kim","year":"2012","journal-title":"Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib47","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/j.bbrc.2014.02.041","article-title":"Top Down proteomics: facts and perspectives","volume":"445","author":"Catherman","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mcpro.2026.101640_bib48","doi-asserted-by":"crossref","first-page":"12519","DOI":"10.1021\/acs.analchem.8b02344","article-title":"Maximizing sequence coverage in top-down proteomics by automated multimodal gas-phase protein fragmentation","volume":"90","author":"Shliaha","year":"2018","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib49","doi-asserted-by":"crossref","first-page":"15377","DOI":"10.1021\/acs.analchem.2c03147","article-title":"Top-\u201cDouble-Down\u201d mass spectrometry of histone H4 proteoforms: Tandem ultraviolet-photon and mobility\/mass-selected electron capture dissociations","volume":"94","author":"Jeanne Dit Fouque","year":"2022","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib50","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1021\/jasms.2c00214","article-title":"The omnitrap platform: a versatile segmented linear ion trap for multidimensional multiple-stage Tandem mass spectrometry","volume":"33","author":"Papanastasiou","year":"2022","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101640_bib51","doi-asserted-by":"crossref","DOI":"10.1016\/j.mcpro.2024.100896","article-title":"How to deal with internal fragment ions?","volume":"24","author":"Grimaud","year":"2025","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib52","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1021\/acs.bioconjchem.9b00065","article-title":"Installation of trimethyllysine analogs on intact histones via cysteine alkylation","volume":"30","author":"Pieters","year":"2019","journal-title":"Bioconjug. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib53","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1021\/acs.bioconjchem.0c00012","article-title":"Exploring the histone acylome through incorporation of \u03b3-Thialysine on histone tails","volume":"31","author":"Proietti","year":"2020","journal-title":"Bioconjug. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib54","doi-asserted-by":"crossref","first-page":"4225","DOI":"10.1021\/pr800044q","article-title":"Tissue-specific expression and post-translational modification of histone H3 variants","volume":"7","author":"Garcia","year":"2008","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.mcpro.2026.101640_bib55","article-title":"Activation of oligonucleotide polyanions using collisions, electrons and photons in a timsOmni platform","author":"Rosu","year":"2025","journal-title":"bioRxiv"},{"key":"10.1016\/j.mcpro.2026.101640_bib56","doi-asserted-by":"crossref","first-page":"11070","DOI":"10.1021\/acs.analchem.5c07288","article-title":"A prototype timsOmni platform enables confident annotation of the key hypervariable CDR3 regions of IgG immunoglobulins using Low- and high-energy electron-based fragmentation","volume":"98","author":"Ollivier","year":"2026","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib57","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1002\/bms.1200111109","article-title":"Proposal for a common nomenclature for sequence ions in mass spectra of peptides","volume":"11","author":"Roepstorff","year":"1984","journal-title":"Biomed. Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101640_bib58","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1080\/19420862.2015.1128607","article-title":"Full validation of therapeutic antibody sequences by middle-up mass measurements and middle-down protein sequencing","volume":"8","author":"Resemann","year":"2016","journal-title":"MAbs"},{"key":"10.1016\/j.mcpro.2026.101640_bib59","doi-asserted-by":"crossref","first-page":"4370","DOI":"10.1021\/acs.analchem.5b00140","article-title":"Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles","volume":"87","author":"Marty","year":"2015","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib60","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1021\/jasms.5c00079","article-title":"Evaluation of protein ion relative ratio quantification in top-down electrospray ionization-mass spectrometry using site-specific acetylated recombinant histone H3 proteoforms","volume":"36","author":"Lui","year":"2025","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101640_bib61","doi-asserted-by":"crossref","first-page":"4271","DOI":"10.1021\/ac0600050","article-title":"Quantitative analysis of modified proteins and their positional isomers by Tandem mass spectrometry: human histone H4","volume":"78","author":"Pesavento","year":"2006","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib62","doi-asserted-by":"crossref","DOI":"10.1016\/j.mcpro.2021.100070","article-title":"Quantifying positional isomers (QPI) by top-down mass spectrometry","volume":"20","author":"Brunner","year":"2021","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.mcpro.2026.101640_bib63","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1007\/s13361-014-0903-2","article-title":"Detection of large ions in time-of-flight mass spectrometry: effects of ion mass and acceleration voltage on microchannel plate detector response","volume":"25","author":"Liu","year":"2014","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101640_bib64","article-title":"Characterization of microchannel plate detector response for the detection of native multiply charged high mass single ions in orthogonal-time-of-flight mass spectrometry using a Timepix detector","volume":"57","author":"Mathew","year":"2022","journal-title":"J. Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101640_bib65","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1016\/j.molcel.2025.08.029","article-title":"A needed nomenclature for nucleosomes","volume":"85","author":"Keogh","year":"2025","journal-title":"Mol. Cell"},{"key":"10.1016\/j.mcpro.2026.101640_bib66","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/b2bf9c2e-90a9-4228-9b38-2f1bc977a437","article-title":"Quantitating the specificity and selectivity of Gcn5-Mediated acetylation of histone H3","volume":"8","author":"Kuo","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.mcpro.2026.101640_bib67","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1021\/cb5004527","article-title":"Acetyltransferase p300\/CBP associated Factor (PCAF) regulates crosstalk-dependent acetylation of histone H3 by distal site recognition","volume":"10","author":"Kornacki","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.mcpro.2026.101640_bib68","doi-asserted-by":"crossref","first-page":"3521","DOI":"10.1093\/emboj\/18.13.3521","article-title":"Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A","volume":"18","author":"Clements","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.mcpro.2026.101640_bib69","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1074\/jbc.274.3.1189","article-title":"Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates","volume":"274","author":"Schiltz","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mcpro.2026.101640_bib70","doi-asserted-by":"crossref","first-page":"14366","DOI":"10.1021\/bi035632n","article-title":"Molecular basis for Gcn5\/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates","volume":"42","author":"Poux","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.mcpro.2026.101640_bib71","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.molcel.2020.08.018","article-title":"PCAF-mediated histone acetylation promotes replication fork degradation by MRE11 and EXO1 in BRCA-deficient cells","volume":"80","author":"Kim","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.mcpro.2026.101640_bib72","doi-asserted-by":"crossref","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":"10.1016\/j.mcpro.2026.101640_bib73","doi-asserted-by":"crossref","first-page":"5746","DOI":"10.1021\/bi400684q","article-title":"Differences in specificity and selectivity between CBP and p300 acetylation of histone H3 and H3\/H4","volume":"52","author":"Henry","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.mcpro.2026.101640_bib74","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1002\/prot.26848","article-title":"Probing enzymatic acetylation events in real time with NMR spectroscopy: insights into acyl-cofactor dependent p300 modification of histone H4","volume":"93","author":"Dewing","year":"2025","journal-title":"Proteins"},{"key":"10.1016\/j.mcpro.2026.101640_bib75","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0024713","article-title":"The human N-alpha-acetyltransferase 40 (hNaa40p\/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4","volume":"6","author":"Hole","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.mcpro.2026.101640_bib76","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1003805","article-title":"N-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencing","volume":"9","author":"Schiza","year":"2013","journal-title":"PLoS Genet."},{"key":"10.1016\/j.mcpro.2026.101640_bib77","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1007\/s10577-015-9486-4","article-title":"Distribution of histone H4 modifications as revealed by a panel of specific monoclonal antibodies","volume":"23","author":"Hayashi-Takanaka","year":"2015","journal-title":"Chromosome Res."},{"key":"10.1016\/j.mcpro.2026.101640_bib78","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1101\/gad.476008","article-title":"A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse","volume":"22","author":"Schotta","year":"2008","journal-title":"Genes Dev."},{"key":"10.1016\/j.mcpro.2026.101640_bib79","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1074\/mcp.M200031-MCP200","article-title":"Histone acetylation and deacetylation: identification of acetylation and methylation sites of HeLa histone H4 by mass spectrometry","volume":"1","author":"Zhang","year":"2002","journal-title":"Mol. Cell Proteomics"}],"container-title":["Molecular & Cellular Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947626001362?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947626001362?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T15:09:29Z","timestamp":1790348969000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1535947626001362"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":79,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["S1535947626001362"],"URL":"https:\/\/doi.org\/10.1016\/j.mcpro.2026.101640","relation":{},"ISSN":["1535-9476"],"issn-type":[{"value":"1535-9476","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Top-Down Sequencing of Intact Proteoforms Using the timsOmni Mass Spectrometer: Accurate Determination of Co-Occurring Histone Modifications","name":"articletitle","label":"Article Title"},{"value":"Molecular & Cellular Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mcpro.2026.101640","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101640"}}