{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T18:11:22Z","timestamp":1777659082616,"version":"3.51.4"},"reference-count":44,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22077045"],"award-info":[{"award-number":["22077045"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Analytica Chimica Acta"],"published-print":{"date-parts":[[2026,5]]},"DOI":"10.1016\/j.aca.2026.345308","type":"journal-article","created":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T08:39:48Z","timestamp":1772095188000},"page":"345308","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["\u201cIEDDA\u201d-activated fluorescent sensing for protein cysteine redox modifications profiling"],"prefix":"10.1016","volume":"1399","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2519-8063","authenticated-orcid":false,"given":"Linfeng","family":"Chen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yifu","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ziyi","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tianyang","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xin","family":"Wen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huiling","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9240-0380","authenticated-orcid":false,"given":"Chunrong","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.aca.2026.345308_bib1","doi-asserted-by":"crossref","first-page":"312","DOI":"10.3390\/antiox13030312","article-title":"Reactive oxygen species signaling and oxidative stress: transcriptional regulation and evolution","volume":"13","author":"Hong","year":"2024","journal-title":"Antioxidants"},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib2","article-title":"Protein redox modification as a cellular defense mechanism against tissue ischemic injury, oxid. Med","volume":"2014","author":"Yan","year":"2014","journal-title":"Cell. Longev."},{"key":"10.1016\/j.aca.2026.345308_bib3","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1146\/annurev-physiol-020518-114417","article-title":"Cysteine-based redox sensing and its role in signaling by cyclic nucleotide\u2013dependent kinases in the cardiovascular system","volume":"81","author":"Cuello","year":"2019","journal-title":"Annu. Rev. Physiol."},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib4","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1038\/s41392-024-02095-6","article-title":"Redox regulation: mechanisms, biology and therapeutic targets in diseases","volume":"10","author":"Li","year":"2025","journal-title":"Signal Transduct. Targeted Ther."},{"key":"10.1016\/j.aca.2026.345308_bib5","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.cophys.2019.04.025","article-title":"Cysteine oxidation and redox signaling in dopaminergic neurons physiology and in Parkinson's disease","volume":"9","author":"Milanese","year":"2019","journal-title":"Curr. Opin. Physiol."},{"key":"10.1016\/j.aca.2026.345308_bib6","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2017.00005","article-title":"Cysteine modifications in the pathogenesis of ALS","volume":"10","author":"Valle","year":"2017","journal-title":"Front. Mol. Neurosci."},{"issue":"24","key":"10.1016\/j.aca.2026.345308_bib7","doi-asserted-by":"crossref","first-page":"6035","DOI":"10.1039\/C9SC01652J","article-title":"Fluorescent probes for organelle-targeted bioactive species imaging","volume":"10","author":"Gao","year":"2019","journal-title":"Chem. Sci."},{"issue":"4","key":"10.1016\/j.aca.2026.345308_bib8","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1021\/cbmi.4c00001","article-title":"Sensing mechanism of cysteine specific fluorescence probes and their application of cysteine recognition","volume":"2","author":"Asghar","year":"2024","journal-title":"Chem. Biomed. Imag."},{"issue":"10","key":"10.1016\/j.aca.2026.345308_bib9","doi-asserted-by":"crossref","first-page":"4252","DOI":"10.3390\/molecules28104252","article-title":"Recent progress in the rational design of biothiol-responsive fluorescent probes","volume":"28","author":"Xie","year":"2023","journal-title":"Molecules"},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib10","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1021\/acsomega.2c06218","article-title":"Near-infrared probes for biothiols (Cysteine, homocysteine, and glutathione): a comprehensive review","volume":"8","author":"Kaushik","year":"2023","journal-title":"ACS Omega"},{"issue":"19","key":"10.1016\/j.aca.2026.345308_bib11","doi-asserted-by":"crossref","first-page":"4172","DOI":"10.1002\/chem.201904470","article-title":"BODIPY-based fluorescent probes for biothiols","volume":"26","author":"Zhang","year":"2020","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.aca.2026.345308_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbpa.2024.102435","article-title":"A new era of cysteine proteomics \u2013 technological advances in thiol biology","volume":"79","author":"Burger","year":"2024","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"45","key":"10.1016\/j.aca.2026.345308_bib13","doi-asserted-by":"crossref","first-page":"10262","DOI":"10.1039\/D5OB00905G","article-title":"A perspective on cysteine-reactive activity-based probes","volume":"23","author":"Nuber","year":"2025","journal-title":"Org. Biomol. Chem."},{"issue":"6","key":"10.1016\/j.aca.2026.345308_bib14","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/j.chembiol.2023.04.004","article-title":"CysDB: a human cysteine database based on experimental quantitative chemoproteomics","volume":"30","author":"Boatner","year":"2023","journal-title":"Cell Chem. Biol."},{"issue":"6","key":"10.1016\/j.aca.2026.345308_bib15","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.cbpa.2008.07.028","article-title":"Expanding the functional diversity of proteins through cysteine oxidation","volume":"12","author":"Reddie","year":"2008","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.aca.2026.345308_bib16","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1146\/annurev.pharmtox.44.101802.121735","article-title":"Protein sulfenic acids in redox signaling","volume":"44","author":"Poole","year":"2004","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"issue":"7","key":"10.1016\/j.aca.2026.345308_bib17","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1021\/cr300163e","article-title":"Cysteine-mediated Redox signaling: chemistry, biology, and tools for discovery","volume":"113","author":"Paulsen","year":"2013","journal-title":"Chem. Rev."},{"key":"10.1016\/j.aca.2026.345308_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2019.101282","article-title":"Cysteine-based regulation of redox-sensitive ras small GTPases","volume":"26","author":"Messina","year":"2019","journal-title":"Redox Biol."},{"key":"10.1016\/j.aca.2026.345308_bib19","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.freeradbiomed.2014.11.013","article-title":"The basics of thiols and cysteines in redox biology and chemistry","volume":"80","author":"Poole","year":"2015","journal-title":"Free Radical Biol. Med."},{"issue":"6","key":"10.1016\/j.aca.2026.345308_bib20","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1039\/B719986D","article-title":"A chemical approach for detecting sulfenic acid-modified proteins in living cells","volume":"4","author":"Reddie","year":"2008","journal-title":"Mol. Biosyst."},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib21","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1039\/C7CS00607A","article-title":"Chemical methods for mapping cysteine oxidation","volume":"47","author":"Alcock","year":"2018","journal-title":"Chem. Soc. Rev."},{"issue":"19","key":"10.1016\/j.aca.2026.345308_bib22","doi-asserted-by":"crossref","first-page":"6234","DOI":"10.1016\/S0021-9258(19)42244-8","article-title":"The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins","volume":"249","author":"Benitez","year":"1974","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib23","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1039\/C5SC02569A","article-title":"Profiling the reactivity of cyclic C-nucleophiles towards electrophilic sulfur in cysteine sulfenic acid","volume":"7","author":"Gupta","year":"2016","journal-title":"Chem. Sci."},{"issue":"34","key":"10.1016\/j.aca.2026.345308_bib24","doi-asserted-by":"crossref","first-page":"4091","DOI":"10.1039\/c2cc17868k","article-title":"A simple and effective strategy for labeling cysteine sulfenic acid in proteins by utilization of \u03b2-ketoesters as cleavable probes","volume":"48","author":"Qian","year":"2012","journal-title":"Chem. Commun."},{"issue":"2","key":"10.1016\/j.aca.2026.345308_bib25","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.bmcl.2008.11.073","article-title":"Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins","volume":"19","author":"Seo","year":"2009","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"9","key":"10.1016\/j.aca.2026.345308_bib26","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1021\/cb900105q","article-title":"Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells","volume":"4","author":"Leonard","year":"2009","journal-title":"ACS Chem. Biol."},{"issue":"48","key":"10.1016\/j.aca.2026.345308_bib27","doi-asserted-by":"crossref","first-page":"15013","DOI":"10.1021\/bi972191x","article-title":"Novel application of 7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase","volume":"36","author":"Ellis","year":"1997","journal-title":"Biochemistry"},{"issue":"39","key":"10.1016\/j.aca.2026.345308_bib28","doi-asserted-by":"crossref","first-page":"14544","DOI":"10.1021\/ja407628a","article-title":"Capturing a sulfenic acid with arylboronic acids and benzoxaborole","volume":"135","author":"Liu","year":"2013","journal-title":"J. Am. Chem. Soc."},{"issue":"11","key":"10.1016\/j.aca.2026.345308_bib29","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1038\/s41557-021-00767-2","article-title":"Wittig reagents for chemoselective sulfenic acid ligation enables global site stoichiometry analysis and redox-controlled mitochondrial targeting","volume":"13","author":"Shi","year":"2021","journal-title":"Nat. Chem."},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib30","doi-asserted-by":"crossref","first-page":"4776","DOI":"10.1038\/ncomms5776","article-title":"Site-specific mapping and quantification of protein S-sulphenylation in cells","volume":"5","author":"Yang","year":"2014","journal-title":"Nat. Commun."},{"issue":"4","key":"10.1016\/j.aca.2026.345308_bib31","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1111\/tpj.14146","article-title":"In vivo detection of protein cysteine sulfenylation in plastids","volume":"97","author":"De Smet","year":"2019","journal-title":"Plant J."},{"issue":"42","key":"10.1016\/j.aca.2026.345308_bib32","doi-asserted-by":"crossref","first-page":"21256","DOI":"10.1073\/pnas.1906768116","article-title":"Mining for protein S-sulfenylation in arabidopsis uncovers redox-sensitive sites","volume":"116","author":"Huang","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib33","doi-asserted-by":"crossref","first-page":"5522","DOI":"10.1038\/s41467-022-33124-z","article-title":"Reaction-based fluorogenic probes for detecting protein cysteine oxidation in living cells","volume":"13","author":"Ferreira","year":"2022","journal-title":"Nat. Commun."},{"issue":"9","key":"10.1016\/j.aca.2026.345308_bib34","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1021\/ar200037t","article-title":"Biomedical applications of tetrazine cycloadditions","volume":"44","author":"Devaraj","year":"2011","journal-title":"Acc. Chem. Res."},{"issue":"23","key":"10.1016\/j.aca.2026.345308_bib35","doi-asserted-by":"crossref","first-page":"5805","DOI":"10.1002\/anie.201400135","article-title":"In situ synthesis of alkenyl tetrazines for highly fluorogenic bioorthogonal live-cell imaging probes","volume":"53","author":"Wu","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"issue":"6","key":"10.1016\/j.aca.2026.345308_bib36","doi-asserted-by":"crossref","first-page":"2984","DOI":"10.1039\/D3CS00520H","article-title":"Design strategies for tetrazine fluorogenic probes for bioorthogonal imaging","volume":"54","author":"Yu","year":"2025","journal-title":"Chem. Soc. Rev."},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib37","doi-asserted-by":"crossref","first-page":"2831","DOI":"10.1038\/s41467-024-47188-6","article-title":"An all-in-one tetrazine reagent for cysteine-selective labeling and bioorthogonal activable prodrug construction","volume":"15","author":"He","year":"2024","journal-title":"Nat. Commun."},{"issue":"5","key":"10.1016\/j.aca.2026.345308_bib38","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.1002\/anie.202011544","article-title":"A general strategy to design highly fluorogenic far-red and near-infrared tetrazine bioorthogonal probes","volume":"60","author":"Mao","year":"2021","journal-title":"Angew. Chem. Int. Ed."},{"issue":"52","key":"10.1016\/j.aca.2026.345308_bib39","article-title":"Ultrafluorogenic Monochromophore-Type BODIPY-tetrazine series for dual-color bioorthogonal imaging with a single probe","volume":"62","author":"Kim","year":"2023","journal-title":"Angew. Chem. Int. Ed."},{"issue":"10","key":"10.1016\/j.aca.2026.345308_bib40","doi-asserted-by":"crossref","first-page":"3770","DOI":"10.1039\/C4SC01348D","article-title":"Conformationally strained trans-cyclooctene with improved stability and excellent reactivity in tetrazine ligation","volume":"5","author":"Darko","year":"2014","journal-title":"Chem. Sci."},{"issue":"58","key":"10.1016\/j.aca.2026.345308_bib41","doi-asserted-by":"crossref","first-page":"36777","DOI":"10.1039\/D1RA07905K","article-title":"Bicyclo[6.1.0]nonyne carboxylic acid for the production of stable molecular probes","volume":"11","author":"Rady","year":"2021","journal-title":"RSC Adv."},{"issue":"1","key":"10.1016\/j.aca.2026.345308_bib42","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1002\/pi.5490","article-title":"Thiol michael addition reaction: a facile tool for introducing peptides into polymer-based gene delivery systems","volume":"67","author":"Sun","year":"2018","journal-title":"Polym. Int."},{"issue":"11","key":"10.1016\/j.aca.2026.345308_bib43","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1038\/s41589-023-01330-5","article-title":"Nucleophilic covalent ligand discovery for the cysteine redoxome","volume":"19","author":"Fu","year":"2023","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.aca.2026.345308_bib44","article-title":"A fast and efficient cysteine-specific bioconjugation enables protein functionalization and rapid quantitative thiol reactivity profiling","author":"Linfeng","year":"2026","journal-title":"Sci. China Chem."}],"container-title":["Analytica Chimica Acta"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003267026002588?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003267026002588?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T07:18:05Z","timestamp":1777447085000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003267026002588"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5]]},"references-count":44,"alternative-id":["S0003267026002588"],"URL":"https:\/\/doi.org\/10.1016\/j.aca.2026.345308","relation":{},"ISSN":["0003-2670"],"issn-type":[{"value":"0003-2670","type":"print"}],"subject":[],"published":{"date-parts":[[2026,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"\u201cIEDDA\u201d-activated fluorescent sensing for protein cysteine redox modifications profiling","name":"articletitle","label":"Article Title"},{"value":"Analytica Chimica Acta","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.aca.2026.345308","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"345308"}}