{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T10:43:11Z","timestamp":1771065791111,"version":"3.50.1"},"reference-count":61,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,2,24]],"date-time":"2023-02-24T00:00:00Z","timestamp":1677196800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100011045","name":"Minist\u00e8re de l'Enseignement sup\u00e9rieur et de la Recherche","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100011045","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005156","name":"Alexander von Humboldt-Stiftung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005156","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001677","name":"Institut National de la Sant\u00e9 et de la Recherche M\u00e9dicale","doi-asserted-by":"publisher","award":["UMR-1100"],"award-info":[{"award-number":["UMR-1100"]}],"id":[{"id":"10.13039\/501100001677","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2023,4]]},"DOI":"10.1016\/j.jbc.2023.103072","type":"journal-article","created":{"date-parts":[[2023,2,26]],"date-time":"2023-02-26T14:53:22Z","timestamp":1677423202000},"page":"103072","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Constitutive and induced forms of membrane-bound proteinase 3 interact with antineutrophil cytoplasmic antibodies and promote immune activation of neutrophils"],"prefix":"10.1016","volume":"299","author":[{"family":"Carla Guarino","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seda","family":"Seren","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9889-3614","authenticated-orcid":false,"given":"Roxane","family":"Lemoine","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amber M.","family":"Hummel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean-Edouard","family":"Margotin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jamel","family":"El-Benna","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cyrille","family":"Hoarau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ulrich","family":"Specks","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dieter E.","family":"Jenne","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brice","family":"Korkmaz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2023.103072_bib1","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/s41572-020-0204-y","article-title":"ANCA-associated vasculitis","volume":"6","author":"Kitching","year":"2020","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.jbc.2023.103072_bib2","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2021.571933","article-title":"Pathogenicity of proteinase 3-anti-neutrophil cytoplasmic antibody in granulomatosis with polyangiitis: implications as Biomarker and future therapies","volume":"12","author":"Granel","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib3","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1038\/nrneph.2017.69","article-title":"Vasculitis: a clear argument for targeting complement in ANCA vasculitis","volume":"13","author":"Kettritz","year":"2017","journal-title":"Nat. Rev. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib4","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1056\/NEJMoa1213277","article-title":"Efficacy of remission-induction regimens for ANCA-associated vasculitis","volume":"369","author":"Specks","year":"2013","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.jbc.2023.103072_bib5","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1124\/pr.115.012104","article-title":"Inhibitors and antibody fragments as potential anti-inflammatory therapeutics targeting neutrophil proteinase 3 in human disease","volume":"68","author":"Korkmaz","year":"2016","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.jbc.2023.103072_bib6","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.pharmthera.2018.05.011","article-title":"Therapeutic targeting of cathepsin C: from pathophysiology to treatment","volume":"190","author":"Korkmaz","year":"2018","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.jbc.2023.103072_bib7","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1007\/s00281-013-0362-z","article-title":"Neutrophil proteinase 3 and dipeptidyl peptidase I (cathepsin C) as pharmacological targets in granulomatosis with polyangiitis (Wegener granulomatosis)","volume":"35","author":"Korkmaz","year":"2013","journal-title":"Semin. Immunopathol."},{"key":"10.1016\/j.jbc.2023.103072_bib8","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1097\/01.ASN.0000040751.83734.D1","article-title":"Membrane expression of proteinase 3 is genetically determined","volume":"14","author":"Schreiber","year":"2003","journal-title":"J.\u00a0Am. Soc. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib9","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0014-5793(95)01073-N","article-title":"Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool","volume":"374","author":"Halbwachs-Mecarelli","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2023.103072_bib10","doi-asserted-by":"crossref","first-page":"19896","DOI":"10.1074\/jbc.M901471200","article-title":"Catalytic activity and inhibition of wegener antigen proteinase 3 on the cell surface of human polymorphonuclear neutrophils","volume":"284","author":"Korkmaz","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib11","doi-asserted-by":"crossref","first-page":"31777","DOI":"10.1074\/jbc.M114.591339","article-title":"New selective peptidyl di(chlorophenyl) phosphonate esters for visualizing and blocking neutrophil proteinase 3 in human diseases","volume":"289","author":"Guarino","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib12","doi-asserted-by":"crossref","first-page":"35976","DOI":"10.1074\/jbc.M806754200","article-title":"A\u00a0hydrophobic patch on proteinase 3, the target of autoantibodies in Wegener granulomatosis, mediates membrane binding via NB1 receptors","volume":"283","author":"Korkmaz","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib13","doi-asserted-by":"crossref","first-page":"2232","DOI":"10.1097\/01.ASN.0000028642.26222.00","article-title":"Neutrophil membrane expression of proteinase 3 (PR3) is related to relapse in PR3-ANCA-associated vasculitis","volume":"13","author":"Rarok","year":"2002","journal-title":"J.\u00a0Am. Soc. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib14","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1681\/ASN.V1061224","article-title":"A\u00a0large subset of neutrophils expressing membrane proteinase 3 is a risk factor for vasculitis and rheumatoid arthritis","volume":"10","author":"Witko-Sarsat","year":"1999","journal-title":"J.\u00a0Am. Soc. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib15","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.autrev.2008.01.003","article-title":"Membrane-bound proteinase 3 and its receptors: relevance for the pathogenesis of wegener's granulomatosis","volume":"8","author":"Hu","year":"2009","journal-title":"Autoimmun. Rev."},{"key":"10.1016\/j.jbc.2023.103072_bib16","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.jaut.2010.06.021","article-title":"Discrimination and variable impact of ANCA binding to different surface epitopes on proteinase 3, the Wegener's autoantigen","volume":"35","author":"Silva","year":"2010","journal-title":"J.\u00a0Autoimmun."},{"key":"10.1016\/j.jbc.2023.103072_bib17","doi-asserted-by":"crossref","first-page":"387","DOI":"10.4049\/jimmunol.0903887","article-title":"Mapping of conformational epitopes on human proteinase 3, the autoantigen of Wegener's granulomatosis","volume":"185","author":"Kuhl","year":"2010","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib18","doi-asserted-by":"crossref","first-page":"2467","DOI":"10.3389\/fimmu.2019.02467","article-title":"Remote activation of a latent epitope in an autoantigen decoded with simulated B-factors","volume":"10","author":"Pang","year":"2019","journal-title":"Front. Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib19","doi-asserted-by":"crossref","first-page":"26635","DOI":"10.1074\/jbc.M113.495770","article-title":"A\u00a0monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism","volume":"288","author":"Hinkofer","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib20","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/978-1-4757-9182-2_7","article-title":"Proteinase 3: substrate specificity and possible pathogenetic effect of wegener's granulomatosis autoantibodies (c-ANCA) by dysregulation of the enzyme","volume":"336","author":"Dolman","year":"1993","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jbc.2023.103072_bib21","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1046\/j.1365-2249.2002.01926.x","article-title":"Interference of PR3-ANCA with the enzymatic activity of PR3: differences in patients during active disease or remission of wegener's granulomatosis","volume":"129","author":"van der Geld","year":"2002","journal-title":"Clin. Exp. Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib22","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.jaut.2015.02.002","article-title":"Allosteric modulation of proteinase 3 activity by anti-neutrophil cytoplasmic antibodies in granulomatosis with polyangiitis","volume":"59","author":"Hinkofer","year":"2015","journal-title":"J.\u00a0Autoimmun."},{"key":"10.1016\/j.jbc.2023.103072_bib23","doi-asserted-by":"crossref","first-page":"4115","DOI":"10.1073\/pnas.87.11.4115","article-title":"Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in\u00a0vitro","volume":"87","author":"Falk","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2023.103072_bib24","doi-asserted-by":"crossref","first-page":"7070","DOI":"10.1074\/jbc.M110.171256","article-title":"Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA neutrophil activation","volume":"286","author":"Jerke","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib25","doi-asserted-by":"crossref","first-page":"2172","DOI":"10.1111\/j.1523-1755.2004.00640.x","article-title":"Membrane proteinase 3 expression and ANCA-induced neutrophil activation","volume":"65","author":"Schreiber","year":"2004","journal-title":"Kidney Int."},{"key":"10.1016\/j.jbc.2023.103072_bib26","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1124\/pr.110.002733","article-title":"Neutrophil elastase, proteinase 3 and cathepsin G as therapeutic targets in human diseases","volume":"62","author":"Korkmaz","year":"2010","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.jbc.2023.103072_bib27","doi-asserted-by":"crossref","first-page":"12415","DOI":"10.1074\/jbc.RA118.001922","article-title":"Consequences of cathepsin C inactivation for membrane exposure of proteinase 3, the target antigen in autoimmune vasculitis","volume":"293","author":"Seren","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib28","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2020.573040","article-title":"4C3 human monoclonal antibody: a proof of concept for non-pathogenic proteinase 3 anti-neutrophil cytoplasmic antibodies in granulomatosis with polyangiitis","volume":"11","author":"Granel","year":"2020","journal-title":"Front. Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib29","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1165\/ajrcmb.24.6.4147","article-title":"Anti-proteinase 3 antibody activation of neutrophils can be inhibited by alpha1-antitrypsin","volume":"24","author":"Rooney","year":"2001","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"10.1016\/j.jbc.2023.103072_bib30","doi-asserted-by":"crossref","first-page":"2033","DOI":"10.1172\/JCI27544","article-title":"A\u00a0specific p47phox -serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites","volume":"116","author":"Dang","year":"2006","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2023.103072_bib31","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1016\/j.micinf.2003.09.008","article-title":"Neutrophil granules and secretory vesicles in inflammation","volume":"5","author":"Faurschou","year":"2003","journal-title":"Microbes Infect."},{"key":"10.1016\/j.jbc.2023.103072_bib32","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1681\/ASN.2021081112","article-title":"Targeting cathepsin C in PR3-ANCA vasculitis","volume":"33","author":"Jerke","year":"2022","journal-title":"J.\u00a0Am. Soc. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib33","doi-asserted-by":"crossref","first-page":"2216","DOI":"10.1681\/ASN.2004070609","article-title":"Membrane proteinase 3 expression in patients with wegener's granulomatosis and in human hematopoietic stem cell-derived neutrophils","volume":"16","author":"Schreiber","year":"2005","journal-title":"J.\u00a0Am. Soc. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib34","doi-asserted-by":"crossref","first-page":"4487","DOI":"10.1182\/blood-2006-10-055327","article-title":"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils","volume":"109","author":"von Vietinghoff","year":"2007","journal-title":"Blood"},{"key":"10.1016\/j.jbc.2023.103072_bib35","doi-asserted-by":"crossref","DOI":"10.1172\/JCI160089","article-title":"Protective alpha1-antitrypsin effects in autoimmune vasculitis are compromised by methionine oxidation","volume":"132","author":"Ebert","year":"2022","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2023.103072_bib36","doi-asserted-by":"crossref","first-page":"3019","DOI":"10.1096\/fj.10-176552","article-title":"A\u00a0substrate-based approach to convert SerpinB1 into a specific inhibitor of proteinase 3, the Wegener's granulomatosis autoantigen","volume":"25","author":"Jegot","year":"2011","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2023.103072_bib37","first-page":"S94","article-title":"Risk factors for relapse in anti-neutrophil cytoplasmic antibody (ANCA)-associated vasculitis: tools for treatment decisions?","volume":"22","author":"Sanders","year":"2004","journal-title":"Clin. Exp. Rheumatol."},{"key":"10.1016\/j.jbc.2023.103072_bib38","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1002\/art.39637","article-title":"Factors determining the clinical utility of serial measurements of antineutrophil cytoplasmic antibodies targeting proteinase 3","volume":"68","author":"Fussner","year":"2016","journal-title":"Arthritis Rheumatol."},{"key":"10.1016\/j.jbc.2023.103072_bib39","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1681\/ASN.2013111233","article-title":"ANCA as a predictor of relapse: useful in patients with renal involvement but not in patients with nonrenal disease","volume":"26","author":"Kemna","year":"2015","journal-title":"J.\u00a0Am. Soc. Nephrol."},{"key":"10.1016\/j.jbc.2023.103072_bib40","doi-asserted-by":"crossref","first-page":"611","DOI":"10.7326\/0003-4819-147-9-200711060-00005","article-title":"Antiproteinase 3 antineutrophil cytoplasmic antibodies and disease activity in Wegener granulomatosis","volume":"147","author":"Finkielman","year":"2007","journal-title":"Ann. Intern. Med."},{"key":"10.1016\/j.jbc.2023.103072_bib41","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1038\/ki.1995.216","article-title":"Inhibition of proteinase 3 by ANCA and its correlation with disease activity in Wegener's granulomatosis","volume":"47","author":"Daouk","year":"1995","journal-title":"Kidney Int."},{"key":"10.1016\/j.jbc.2023.103072_bib42","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1165\/rcmb.2003-0139OC","article-title":"Design and use of highly specific substrates of neutrophil elastase and proteinase 3","volume":"30","author":"Korkmaz","year":"2004","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"10.1016\/j.jbc.2023.103072_bib43","doi-asserted-by":"crossref","first-page":"1989","DOI":"10.1074\/jbc.M608700200","article-title":"Influence of charge distribution at the active site surface on the substrate specificity of human neutrophil protease 3 and elastase. A kinetic and molecular modeling analysis","volume":"282","author":"Korkmaz","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib44","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1038\/ki.1992.52","article-title":"Anti-myeloperoxidase antibodies stimulate neutrophils to damage human endothelial cells","volume":"41","author":"Ewert","year":"1992","journal-title":"Kidney Int."},{"key":"10.1016\/j.jbc.2023.103072_bib45","doi-asserted-by":"crossref","first-page":"3189","DOI":"10.1182\/blood.V86.8.3189.3189","article-title":"Effect of tumor necrosis factor-induced integrin activation on Fc gamma receptor II-mediated signal transduction: relevance for activation of neutrophils by anti-proteinase 3 or anti-myeloperoxidase antibodies","volume":"86","author":"Reumaux","year":"1995","journal-title":"Blood"},{"key":"10.1016\/j.jbc.2023.103072_bib46","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1038\/nm.1959","article-title":"Netting neutrophils in autoimmune small-vessel vasculitis","volume":"15","author":"Kessenbrock","year":"2009","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2023.103072_bib47","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1038\/ncprheum0355","article-title":"Mechanisms of disease: pathogenesis and treatment of ANCA-associated vasculitides","volume":"2","author":"Kallenberg","year":"2006","journal-title":"Nat. Clin. Pract. Rheumatol."},{"key":"10.1016\/j.jbc.2023.103072_bib48","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1111\/j.1365-2249.1992.tb07934.x","article-title":"Activation of normal neutrophils by anti-neutrophil cytoplasm antibodies","volume":"90","author":"Keogan","year":"1992","journal-title":"Clin. Exp. Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib49","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.4049\/jimmunol.153.3.1271","article-title":"Anti-neutrophil cytoplasmic antibodies engage and activate human neutrophils via Fc gamma RIIa","volume":"153","author":"Porges","year":"1994","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib50","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1056\/NEJMoa2023386","article-title":"Avacopan for the treatment of ANCA-associated vasculitis","volume":"384","author":"Jayne","year":"2021","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.jbc.2023.103072_bib51","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/70525","article-title":"Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis","volume":"23","author":"Toomes","year":"1999","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jbc.2023.103072_bib52","doi-asserted-by":"crossref","first-page":"7277","DOI":"10.4049\/jimmunol.173.12.7277","article-title":"Papillon-lefevre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C\/dipeptidyl peptidase I deficiency in humans","volume":"173","author":"Pham","year":"2004","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.jbc.2023.103072_bib53","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.1056\/NEJMoa2021713","article-title":"Phase 2 trial of the DPP-1 inhibitor brensocatib in bronchiectasis","volume":"383","author":"Chalmers","year":"2020","journal-title":"New Engl. J. Med."},{"key":"10.1016\/j.jbc.2023.103072_bib54","doi-asserted-by":"crossref","first-page":"13258","DOI":"10.1021\/acs.jmedchem.0c00776","article-title":"Lung protection by cathepsin C inhibition: a new hope for COVID-19 and ARDS?","volume":"63","author":"Korkmaz","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib55","doi-asserted-by":"crossref","DOI":"10.1016\/j.bcp.2021.114803","article-title":"Cathepsin C inhibition as a potential treatment strategy in cancer","volume":"194","author":"Korkmaz","year":"2021","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.jbc.2023.103072_bib56","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.ccell.2020.12.012","article-title":"Cathepsin C promotes breast cancer lung metastasis by modulating neutrophil infiltration and neutrophil extracellular trap formation","volume":"39","author":"Xiao","year":"2021","journal-title":"Cancer Cell"},{"key":"10.1016\/j.jbc.2023.103072_bib57","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1038\/nprot.2008.63","article-title":"Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates","volume":"3","author":"Korkmaz","year":"2008","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.jbc.2023.103072_bib58","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.ab.2013.07.028","article-title":"A\u00a0new proteinase 3 substrate with improved selectivity over human neutrophil elastase","volume":"442","author":"Popow-Stellmaszyk","year":"2013","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2023.103072_bib59","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0022-1759(81)90138-1","article-title":"Rapid microassays for the measurement of superoxide and hydrogen peroxide production by macrophages in culture using an automatic enzyme immunoassay reader","volume":"46","author":"Pick","year":"1981","journal-title":"J.\u00a0Immunol. Met."},{"key":"10.1016\/j.jbc.2023.103072_bib60","doi-asserted-by":"crossref","first-page":"34084","DOI":"10.1074\/jbc.M109.042903","article-title":"Structural characterization of mouse neutrophil serine proteases and identification of their substrate specificities: relevance to mouse models of human inflammatory diseases","volume":"284","author":"Kalupov","year":"2009","journal-title":"J\u00a0.Biol. Chem."},{"key":"10.1016\/j.jbc.2023.103072_bib61","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1046\/j.1365-2249.1998.00730.x","article-title":"A\u00a0proportion of proteinase 3 (PR3)-specific anti-neutrophil cytoplasmic antibodies (ANCA) only react with PR3 after cleavage of its N-terminal activation dipeptide","volume":"114","author":"Sun","year":"1998","journal-title":"Clin. Exp. Immunol."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925823002041?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925823002041?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T16:35:09Z","timestamp":1762187709000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925823002041"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,4]]},"references-count":61,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2023,4]]}},"alternative-id":["S0021925823002041"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2023.103072","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2023,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Constitutive and induced forms of membrane-bound proteinase 3 interact with antineutrophil cytoplasmic antibodies and promote immune activation of neutrophils","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2023.103072","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"name":"copyright","label":"Copyright"}],"article-number":"103072"}}