{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T16:03:00Z","timestamp":1790352180983,"version":"4.1.0"},"reference-count":48,"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":[[2026,6,24]],"date-time":"2026-06-24T00:00:00Z","timestamp":1782259200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100008783","name":"National Research Council of Science and Technology","doi-asserted-by":"publisher","award":["CRC22021-100"],"award-info":[{"award-number":["CRC22021-100"]}],"id":[{"id":"10.13039\/501100008783","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2022-NR068428"],"award-info":[{"award-number":["RS-2022-NR068428"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003716","name":"Korea Basic Science Institute","doi-asserted-by":"publisher","award":["S610000"],"award-info":[{"award-number":["S610000"]}],"id":[{"id":"10.13039\/501100003716","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003716","name":"Korea Basic Science Institute","doi-asserted-by":"publisher","award":["C623200"],"award-info":[{"award-number":["C623200"]}],"id":[{"id":"10.13039\/501100003716","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011705","name":"Korea Institute of Marine Science and Technology Promotion","doi-asserted-by":"publisher","award":["RS-2024-00405273"],"award-info":[{"award-number":["RS-2024-00405273"]}],"id":[{"id":"10.13039\/501100011705","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.2026.101611","type":"journal-article","created":{"date-parts":[[2026,6,25]],"date-time":"2026-06-25T16:28:03Z","timestamp":1782404883000},"page":"101611","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Depletion-free Automated Enrichment of Serum Glycopeptides for High-Throughput Clinical Glycoproteomics"],"prefix":"10.1016","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-6402-8915","authenticated-orcid":false,"given":"Jung Hoon","family":"Choi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geul","family":"Bang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jong Hyun","family":"Seol","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seong Woo","family":"Choi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Su-Min","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2786-1938","authenticated-orcid":false,"given":"Bao Tan","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5159-2048","authenticated-orcid":false,"given":"Seungjin","family":"Na","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cheol-Jung","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heeyoun","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinsoo","family":"Chung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sang-Jae","family":"Park","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sang Myoung","family":"Woo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hye Gwang","family":"Jeong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0656-1269","authenticated-orcid":false,"given":"Jin Young","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mcpro.2026.101611_bib1","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1042\/BCJ20170111","article-title":"Role of glycosylation in nucleating protein folding and stability","volume":"474","author":"Jayaprakash","year":"2017","journal-title":"Biochem. J."},{"key":"10.1016\/j.mcpro.2026.101611_bib2","doi-asserted-by":"crossref","first-page":"12827","DOI":"10.1074\/jbc.M313173200","article-title":"N-Glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I","volume":"279","author":"Wujek","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib3","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1111\/j.1432-1033.1997.00243.x","article-title":"Domain-Specific n-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding","volume":"246","author":"Fan","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.mcpro.2026.101611_bib4","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1042\/BST0390399","article-title":"Glycobiomarkers by glycoproteomics and glycan profiling (glycomics): emergence of functionality","volume":"39","author":"Gabius","year":"2011","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.mcpro.2026.101611_bib5","doi-asserted-by":"crossref","DOI":"10.1002\/jcla.23711","article-title":"Serum N -glycan profiling as a diagnostic biomarker for the identification and assessment of psoriasis","volume":"35","author":"Zou","year":"2021","journal-title":"J. Clin. Lab. Anal."},{"key":"10.1016\/j.mcpro.2026.101611_bib6","first-page":"1156","article-title":"Recent advances in N-glycan biomarker discovery among human diseases","volume":"56","author":"Wang","year":"2024","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"10.1016\/j.mcpro.2026.101611_bib7","doi-asserted-by":"crossref","DOI":"10.1084\/jem.20211505","article-title":"Altered glycosylation in pancreatic cancer and beyond","volume":"219","author":"Lumibao","year":"2022","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.mcpro.2026.101611_bib8","doi-asserted-by":"crossref","first-page":"35478","DOI":"10.18632\/oncotarget.8155","article-title":"Hallmarks of glycosylation in cancer","volume":"7","author":"Munkley","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.mcpro.2026.101611_bib9","doi-asserted-by":"crossref","DOI":"10.1002\/eji.202451318","article-title":"Tumor glycosylation: a main player in the modulation of immune responses","volume":"55","author":"Rodriguez","year":"2025","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.mcpro.2026.101611_bib10","doi-asserted-by":"crossref","DOI":"10.21769\/BioProtoc.4059","article-title":"Differential analysis of N-glycopeptide abundance and N-glycosylation site occupancy for studying protein N-glycosylation dysregulation in human disease","volume":"11","author":"Zhang","year":"2021","journal-title":"BIO-Protoc."},{"key":"10.1016\/j.mcpro.2026.101611_bib11","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2023.1170818","article-title":"Editorial: new methods, techniques and applications in clinical glycoproteomics","volume":"10","author":"Zhang","year":"2023","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.mcpro.2026.101611_bib12","doi-asserted-by":"crossref","first-page":"15656","DOI":"10.1021\/acs.analchem.3c02856","article-title":"Parallelized acquisition of orbitrap and astral analyzers enables high-throughput quantitative analysis","volume":"95","author":"Stewart","year":"2023","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib13","doi-asserted-by":"crossref","first-page":"2439","DOI":"10.1042\/BST20240257","article-title":"Tools and techniques for quantitative glycoproteomic analysis","volume":"52","author":"Kong","year":"2024","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.mcpro.2026.101611_bib14","doi-asserted-by":"crossref","first-page":"7473","DOI":"10.1021\/acs.analchem.1c00645","article-title":"Automated intact glycopeptide enrichment method facilitating highly reproducible analysis of serum site-specific N-Glycoproteome","volume":"93","author":"Liu","year":"2021","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib15","doi-asserted-by":"crossref","first-page":"5598","DOI":"10.1021\/ac100530w","article-title":"Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics","volume":"82","author":"Mysling","year":"2010","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib16","doi-asserted-by":"crossref","first-page":"11193","DOI":"10.1021\/acs.analchem.7b03641","article-title":"Comparison of enrichment methods for intact N- and O-Linked glycopeptides using strong anion exchange and hydrophilic interaction liquid chromatography","volume":"89","author":"Yang","year":"2017","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib17","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1002\/jssc.200800094","article-title":"Efficacy of glycoprotein enrichment by microscale lectin affinity chromatography","volume":"31","author":"Madera","year":"2008","journal-title":"J. Sep. Sci."},{"key":"10.1016\/j.mcpro.2026.101611_bib18","doi-asserted-by":"crossref","first-page":"8822","DOI":"10.1021\/acs.analchem.4c01454","article-title":"A fully automated online enrichment and separation System for highly reproducible and In-Depth analysis of intact glycopeptide","volume":"96","author":"Hu","year":"2024","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib19","doi-asserted-by":"crossref","first-page":"A0061","DOI":"10.5702\/massspectrometry.A0061","article-title":"Rapid glycopeptide enrichment using cellulose hydrophilic Interaction\/Reversed-Phase StageTips","volume":"6","author":"Ohta","year":"2017","journal-title":"Mass Spectrom."},{"key":"10.1016\/j.mcpro.2026.101611_bib20","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1074\/mcp.M113.027953","article-title":"The GlycoFilter: a simple and comprehensive sample preparation platform for proteomics, N-Glycomics and glycosylation site assignment","volume":"12","author":"Zhou","year":"2013","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2026.101611_bib21","doi-asserted-by":"crossref","first-page":"5433","DOI":"10.1021\/acs.analchem.9b00776","article-title":"Site-Specific glycosylation quantitation of 50 serum glycoproteins enhanced by predictive glycopeptidomics for improved disease biomarker discovery","volume":"91","author":"Li","year":"2019","journal-title":"Anal. Chem."},{"key":"10.1016\/j.mcpro.2026.101611_bib22","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1074\/mcp.M116.065250","article-title":"Human plasma N-glycosylation as analyzed by matrix-assisted laser Desorption\/Ionization-Fourier transform ion Cyclotron Resonance-MS associates with markers of inflammation and metabolic health","volume":"16","author":"Reiding","year":"2017","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2026.101611_bib23","doi-asserted-by":"crossref","first-page":"4952","DOI":"10.1021\/pr100202a","article-title":"Human serum processing and analysis methods for rapid and reproducible N-Glycan mass profiling","volume":"9","author":"Kronewitter","year":"2010","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib24","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1002\/jssc.201100060","article-title":"Characterization of the human serum depletome by label-free shotgun proteomics","volume":"34","author":"Koutroukides","year":"2011","journal-title":"J. Sep. Sci."},{"key":"10.1016\/j.mcpro.2026.101611_bib25","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1021\/pr0501721","article-title":"Effect of immunoaffinity depletion of human serum during proteomic investigations","volume":"4","author":"Yocum","year":"2005","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib26","doi-asserted-by":"crossref","first-page":"4316","DOI":"10.1002\/elps.200800211","article-title":"Quantitative assessment of human serum high-abundance protein depletion","volume":"29","author":"Stempfer","year":"2008","journal-title":"Electrophoresis"},{"key":"10.1016\/j.mcpro.2026.101611_bib27","doi-asserted-by":"crossref","first-page":"17","DOI":"10.12688\/hrbopenres.12846.1","article-title":"Chemical crosslinking analysis of \u03b2-dystroglycan in dystrophin-deficient skeletal muscle","volume":"1","author":"Murphy","year":"2018","journal-title":"HRB Open Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib28","article-title":"pGlyco: a pipeline for the identification of intact N-glycopeptides by using HCD- and CID-MS\/MS and MS3","volume":"6","author":"Zeng","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mcpro.2026.101611_bib29","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1038\/s41467-017-00535-2","article-title":"pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification","volume":"8","author":"Liu","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mcpro.2026.101611_bib30","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1038\/s41592-021-01306-0","article-title":"Precise, fast and comprehensive analysis of intact glycopeptides and modified glycans with pGlyco3","volume":"18","author":"Zeng","year":"2021","journal-title":"Nat. Methods"},{"key":"10.1016\/j.mcpro.2026.101611_bib31","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1038\/s41592-020-0967-9","article-title":"Fast and comprehensive N- and O-glycoproteomics analysis with MSFragger-Glyco","volume":"17","author":"Polasky","year":"2020","journal-title":"Nat. Methods"},{"key":"10.1016\/j.mcpro.2026.101611_bib32","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/nmeth.3901","article-title":"The Perseus computational platform for comprehensive analysis of (prote)omics data","volume":"13","author":"Tyanova","year":"2016","journal-title":"Nat. Methods"},{"key":"10.1016\/j.mcpro.2026.101611_bib33","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1002\/pro.4218","article-title":"Panther : making genome-scale phylogenetics accessible to all","volume":"31","author":"Thomas","year":"2022","journal-title":"Protein Sci."},{"key":"10.1016\/j.mcpro.2026.101611_bib34","doi-asserted-by":"crossref","first-page":"1523","DOI":"10.1038\/s41467-019-09234-6","article-title":"Metascape provides a biologist-oriented resource for the analysis of systems-level datasets","volume":"10","author":"Zhou","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mcpro.2026.101611_bib35","article-title":"A fucosylated glycopeptide as a candidate biomarker for early diagnosis of NASH hepatocellular carcinoma using a stepped HCD method and PRM evaluation","volume":"12","author":"Lin","year":"2022","journal-title":"Front. Oncol."},{"key":"10.1016\/j.mcpro.2026.101611_bib36","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1186\/s12964-024-01569-y","article-title":"Integrating transcriptomics, glycomics and glycoproteomics to characterize hepatitis B virus-associated hepatocellular carcinoma","volume":"22","author":"Li","year":"2024","journal-title":"Cell Commun. Signal."},{"key":"10.1016\/j.mcpro.2026.101611_bib37","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1093\/glycob\/cws110","article-title":"Site-specific glycoproteomics confirms that protein structure dictates formation of N-glycan type, core fucosylation and branching","volume":"22","author":"Thaysen-Andersen","year":"2012","journal-title":"Glycobiology"},{"key":"10.1016\/j.mcpro.2026.101611_bib38","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1093\/glycob\/cwab084","article-title":"Functional analysis of Ost3p and Ost6p containing yeast oligosaccharyltransferases","volume":"31","author":"Neuhaus","year":"2021","journal-title":"Glycobiology"},{"key":"10.1016\/j.mcpro.2026.101611_bib39","doi-asserted-by":"crossref","first-page":"4261","DOI":"10.1007\/s00436-014-4104-5","article-title":"Evaluation of protective immune response in mice by vaccination the recombinant adenovirus for expressing Schistosoma japonicum inhibitor apoptosis protein","volume":"113","author":"Hu","year":"2014","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib40","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0145-305X(99)00018-X","article-title":"\u03b1 2 -macroglobulin: an evolutionarily conserved arm of the innate immune system","volume":"23","author":"Armstrong","year":"1999","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.mcpro.2026.101611_bib41","doi-asserted-by":"crossref","first-page":"1885","DOI":"10.1038\/s41467-026-68579-x","article-title":"Large-scale serum N-glycomics tracks N-glycosylation dynamics in hepatocellular carcinoma progression and enables early diagnosis","volume":"17","author":"Fu","year":"2026","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mcpro.2026.101611_bib42","doi-asserted-by":"crossref","DOI":"10.1038\/srep16007","article-title":"Specific N-glycans of hepatocellular carcinoma cell surface and the abnormal increase of Core-\u03b1-1, 6-fucosylated triantennary glycan via N-acetylglucosaminyltransferases-IVa regulation","volume":"5","author":"Nie","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mcpro.2026.101611_bib43","doi-asserted-by":"crossref","first-page":"3454","DOI":"10.1021\/acs.jproteome.8b00323","article-title":"N-Linked glycan branching and fucosylation are increased directly in Hcc tissue as determined through in Situ glycan Imaging","volume":"17","author":"West","year":"2018","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib44","doi-asserted-by":"crossref","first-page":"2314","DOI":"10.1002\/hep.26262","article-title":"Identification of novel serum biomarkers of hepatocellular carcinoma using glycomic analysis","volume":"57","author":"Kamiyama","year":"2013","journal-title":"Hepatology"},{"key":"10.1016\/j.mcpro.2026.101611_bib45","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.cca.2022.12.015","article-title":"Diagnostic potential of site-specific serotransferrin N-glycosylation in discriminating different liver diseases","volume":"539","author":"Zhang","year":"2023","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.mcpro.2026.101611_bib46","doi-asserted-by":"crossref","first-page":"D543","DOI":"10.1093\/nar\/gkab1038","article-title":"The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences","volume":"50","author":"Perez-Riverol","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib47","doi-asserted-by":"crossref","first-page":"D447","DOI":"10.1093\/nar\/gkv1145","article-title":"2016 update of the PRIDE database and its related tools","volume":"44","author":"Vizca\u00edno","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.mcpro.2026.101611_bib48","doi-asserted-by":"crossref","first-page":"D1100","DOI":"10.1093\/nar\/gkw936","article-title":"The ProteomeXchange consortium in 2017: supporting the cultural change in proteomics public data deposition","volume":"45","author":"Deutsch","year":"2017","journal-title":"Nucleic Acids Res."}],"container-title":["Molecular & Cellular Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947626001076?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947626001076?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T15:09:19Z","timestamp":1790348959000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1535947626001076"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":48,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["S1535947626001076"],"URL":"https:\/\/doi.org\/10.1016\/j.mcpro.2026.101611","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":"Depletion-free Automated Enrichment of Serum Glycopeptides for High-Throughput Clinical Glycoproteomics","name":"articletitle","label":"Article Title"},{"value":"Molecular & Cellular Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mcpro.2026.101611","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":"101611"}}