{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T04:12:37Z","timestamp":1778904757107,"version":"3.51.4"},"reference-count":74,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T00:00:00Z","timestamp":1770076800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM144091"],"award-info":[{"award-number":["R35GM144091"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM152031"],"award-info":[{"award-number":["R35GM152031"]}],"id":[{"id":"10.13039\/100000057","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":[[2026,3]]},"DOI":"10.1016\/j.jbc.2026.111247","type":"journal-article","created":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T00:48:56Z","timestamp":1770252536000},"page":"111247","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Unusual and atypical cyclooxygenase reactions"],"prefix":"10.1016","volume":"302","author":[{"given":"Claus","family":"Schneider","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-2639-5848","authenticated-orcid":false,"given":"Alan R.","family":"Brash","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.111247_bib1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0005-2760(91)90119-3","article-title":"Prostaglandin endoperoxide synthase: structure and catalysis","volume":"1083","author":"Smith","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.111247_bib2","first-page":"3555","article-title":"Prostaglandins and related factors. 15. The structures of prostaglandin E1, F1-Alpha, and F1-Beta","volume":"238","author":"Bergstroem","year":"1963","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib3","doi-asserted-by":"crossref","first-page":"3229","DOI":"10.1016\/S0021-9258(18)48651-6","article-title":"Isolation and identification of prostaglandins from human seminal plasma .18. Prostaglandins and related factors","volume":"238","author":"Samuelsson","year":"1963","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib4","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1038\/250665a0","article-title":"19-Hydroxylated-E prostaglandins as major prostaglandins of human semen","volume":"250","author":"Taylor","year":"1974","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111247_bib5","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1038\/260544a0","article-title":"19-Hydroxyprostaglandin-E1 as a major component of semen of primates","volume":"260","author":"Kelly","year":"1976","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111247_bib6","doi-asserted-by":"crossref","first-page":"21844","DOI":"10.1074\/jbc.M001712200","article-title":"Identification of CYP4F8 in human seminal vesicles as a prominent 19-hydroxylase of prostaglandin endoperoxides","volume":"275","author":"Bylund","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib7","doi-asserted-by":"crossref","first-page":"5344","DOI":"10.1016\/S0021-9258(18)99434-2","article-title":"Oxygenation of unsaturated fatty acids by the vesicular gland of sheep","volume":"242","author":"Hamberg","year":"1967","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib8","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1006\/abbi.1997.0443","article-title":"Stereochemistry of oxygenation of linoleic acid catalyzed by prostaglandin-endoperoxide H synthase-2","volume":"349","author":"Hamberg","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2026.111247_bib9","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1111\/j.1432-1033.1987.tb13587.x","article-title":"Identification of novel arachidonic acid metabolites formed by prostaglandin H synthase","volume":"169","author":"Hecker","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2026.111247_bib10","doi-asserted-by":"crossref","first-page":"1836","DOI":"10.1021\/bi962476u","article-title":"Analysis of hydroperoxide-induced tyrosyl radicals and lipoxygenase activity in aspirin-treated human prostaglandin H synthase-2","volume":"36","author":"Xiao","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.111247_bib11","doi-asserted-by":"crossref","first-page":"8501","DOI":"10.1074\/jbc.275.12.8501","article-title":"Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products","volume":"275","author":"Thuresson","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib12","doi-asserted-by":"crossref","first-page":"19330","DOI":"10.1074\/jbc.270.33.19330","article-title":"Fatty acid specificities of human prostaglandin-endoperoxide H synthase-1 and -2. Formation of 12-hydroxy-(9Z,13E\/Z,15Z)-octadecatrienoic acids from \u03b1-linolenic acid","volume":"270","author":"Laneuville","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib13","doi-asserted-by":"crossref","first-page":"24619","DOI":"10.1074\/jbc.M112.372243","article-title":"Investigating substrate promiscuity in cyclooxygenase-2: the role of Arg-120 and residues lining the hydrophobic groove","volume":"287","author":"Vecchio","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib14","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/S0021-9258(18)65729-1","article-title":"Metabolism of essential fatty acids .3. isolation of 5,8,11-eicosatrienoic acid from fat-deficient rats","volume":"219","author":"Mead","year":"1956","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib15","doi-asserted-by":"crossref","first-page":"6719","DOI":"10.1016\/S0021-9258(19)62675-X","article-title":"Calcium-dependent oxidation of 5,8,11-icosatrienoic acid by the cyclooxygenase enzyme system","volume":"261","author":"Elliott","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib16","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1006\/abbi.1993.1425","article-title":"Oxygenation of 5,8,11-eicosatrienoic acid by prostaglandin endoperoxide synthase and by cytochrome P450 monooxygenase: structure and mechanism of formation of major metabolites","volume":"305","author":"Oliw","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2026.111247_bib19","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/S0378-4347(96)00372-6","article-title":"Oxygenation of 5,8,11-eicosatrienoic acid by prostaglandin H synthase-2 of ovine placental cotyledons: isolation of 13-hydroxy-5,8,11-eicosatrienoic and 11-hydroxy-5,8,12-eicosatrienoic acids","volume":"690","author":"Oliw","year":"1997","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"10.1016\/j.jbc.2026.111247_bib17","doi-asserted-by":"crossref","first-page":"4404","DOI":"10.1074\/jbc.M307431200","article-title":"Identification of two cyclooxygenase active site residues, leucine-384 and glycine-526, that control carbon ring cyclization in prostaglandin biosynthesis","volume":"279","author":"Schneider","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib18","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1021\/ja056517y","article-title":"Convergent oxygenation of arachidonic acid by 5-lipoxygenase and cyclooxygenase-2","volume":"128","author":"Schneider","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2026.111247_bib20","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/0005-2760(85)90274-7","article-title":"Metabolism of eicosapentaenoic acid by aorta - Formation of a novel 13-hydroxylated prostaglandin","volume":"835","author":"Powell","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.111247_bib21","doi-asserted-by":"crossref","first-page":"5655","DOI":"10.1016\/S0040-4039(00)96805-9","article-title":"Synthesis of novel prostaglandin-F2-alpha isomers and structure of an enzymatically formed 13-hydroxyprostaglandin endoperoxide","volume":"28","author":"Hofmann","year":"1987","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.jbc.2026.111247_bib22","doi-asserted-by":"crossref","first-page":"3581","DOI":"10.1073\/pnas.80.12.3581","article-title":"Docosahexaenoic acid is a strong inhibitor of prostaglandin but not leukotriene biosynthesis","volume":"80","author":"Corey","year":"1983","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111247_bib23","doi-asserted-by":"crossref","first-page":"9339","DOI":"10.1016\/S0021-9258(17)44672-2","article-title":"Synthesis of hydroxy fatty acids from 4,7,10,13,16,19-[1-C-14] docosahexaenoic acid by human platelets","volume":"258","author":"Aveldano","year":"1983","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib24","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1124\/mol.109.063115","article-title":"Asymmetric acetylation of the cyclooxygenase-2 homodimer by aspirin and its effects on the oxygenation of arachidonic, eicosapentaenoic, and docosahexaenoic acids","volume":"77","author":"Sharma","year":"2010","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.jbc.2026.111247_bib25","doi-asserted-by":"crossref","first-page":"10046","DOI":"10.1074\/jbc.M808634200","article-title":"Cyclooxygenase allosterism, fatty acid-mediated cross-talk between monomers of cyclooxygenase homodimers","volume":"284","author":"Yuan","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib26","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/nchembio.367","article-title":"Cyclooxygenase-2 generates anti-inflammatory mediators from omega-3 fatty acids","volume":"6","author":"Groeger","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2026.111247_bib27","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/384644a0","article-title":"Structural basis for the selective inhibition of cyclooxygenase-2 by anti-inflammatory agents","volume":"384","author":"Kurumbail","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111247_bib28","doi-asserted-by":"crossref","first-page":"2716","DOI":"10.1016\/S0021-9258(17)43204-2","article-title":"Metabolism of 5(6)Oxidoeicosatrienoic acid by ram seminal vesicles. Formation of two stereoisomers of 5-hydroxyprostaglandin I1","volume":"259","author":"Oliw","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib29","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/0005-2760(84)90256-X","article-title":"Metabolism of 5(6)-expoxyeicosatrienoic acid by ram seminal vesicles. Formation of novel prostaglandin E1 metabolites","volume":"793","author":"Oliw","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.111247_bib30","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/0005-2760(84)90089-4","article-title":"Biosynthesis of 5,6-dihydroxyprostaglandin E1 and F1 alpha from 5,6-dihydroxyeicosatrienoic acid by ram seminal vesicles","volume":"795","author":"Oliw","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.111247_bib31","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/0006-291X(92)91619-2","article-title":"Regiospecific and enantioselective metabolism of 8,9-epoxyeicosatrienoic acid by cyclooxygenase","volume":"183","author":"Zhang","year":"1992","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2026.111247_bib32","doi-asserted-by":"crossref","first-page":"4370","DOI":"10.1073\/pnas.1616893114","article-title":"Cyclooxygenase-derived proangiogenic metabolites of epoxyeicosatrienoic acids","volume":"114","author":"Rand","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111247_bib33","doi-asserted-by":"crossref","first-page":"15334","DOI":"10.1016\/S0021-9258(18)66872-3","article-title":"Inhibition of cyclooxygenase activity and platelet aggregation by epoxyeicosatrienoic acids. Influence of stereochemistry","volume":"261","author":"Fitzpatrick","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib34","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1007\/s11745-006-0164-3","article-title":"Production of 3R-hydroxy-polyenoic fatty acids by the yeast Dipodascopsis uninucleata","volume":"32","author":"Venter","year":"1997","journal-title":"Lipids"},{"key":"10.1016\/j.jbc.2026.111247_bib35","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1042\/BJ20041995","article-title":"Oxygenation by COX-2 (cyclo-oxygenase-2) of 3-HETE (3-hydroxyeicosatetraenoic acid), a fungal mimetic of arachidonic acid, produces a cascade of novel bioactive 3-hydroxyeicosanoids","volume":"390","author":"Ciccoli","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2026.111247_bib36","doi-asserted-by":"crossref","first-page":"11658","DOI":"10.1016\/S0021-9258(18)80115-6","article-title":"Metabolism of 20-hydroxyeicosatetraenoic acid by cyclooxygenase. Formation and identification of novel endothelium-dependent vasoconstrictor metabolites","volume":"264","author":"Schwartzman","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib37","doi-asserted-by":"crossref","first-page":"23305","DOI":"10.1074\/jbc.274.33.23305","article-title":"The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (COX-2)","volume":"274","author":"Rowlinson","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib38","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1194\/jlr.M900181-JLR200","article-title":"Convergence of the 5-LOX and COX-2 pathways. Heme-catalyzed cleavage of the 5S-HETE-derived di-endoperoxide into aldehyde fragments","volume":"50","author":"Griesser","year":"2009","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.111247_bib39","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1021\/jacsau.1c00177","article-title":"Biosynthetic crossover of 5-lipoxygenase and cyclooxygenase-2 yields 5-hydroxy-PGE2 and 5-hydroxy-PGD2","volume":"1","author":"Nakashima","year":"2021","journal-title":"JACS Au"},{"key":"10.1016\/j.jbc.2026.111247_bib40","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1194\/jlr.M001719","article-title":"Identification and absolute configuration of dihydroxy-arachidonic acids formed by oxygenation of 5S-HETE by native and aspirin-acetylated COX-2","volume":"51","author":"Mulugeta","year":"2010","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.111247_bib41","doi-asserted-by":"crossref","first-page":"6945","DOI":"10.1073\/pnas.1019473108","article-title":"Biosynthesis of hemiketal eicosanoids by cross-over of the 5-lipoxygenase and cyclooxygenase-2 pathways","volume":"108","author":"Griesser","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111247_bib42","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1096\/fj.201601136R","article-title":"Roles of 5-lipoxygenase and cyclooxygenase-2 in the biosynthesis of hemiketals E2 and D2 by activated human leukocytes","volume":"31","author":"Gimenez-Bastida","year":"2017","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2026.111247_bib43","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.prostaglandins.2016.09.001","article-title":"Biomimetic synthesis of hemiketal eicosanoids for biological testing","volume":"132","author":"Gimenez-Bastida","year":"2017","journal-title":"Prostag. Other Lipid Mediat."},{"key":"10.1016\/j.jbc.2026.111247_bib44","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.103050","article-title":"The 5-lipoxygenase\/cyclooxygenase-2 cross-over metabolite, hemiketal E(2), enhances VEGFR2 activation and promotes angiogenesis","volume":"299","author":"Nakashima","year":"2023","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib45","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0090-6980(02)00026-6","article-title":"The structures of prostaglandin endoperoxide H synthases-1 and -2","volume":"68-69","author":"Garavito","year":"2002","journal-title":"Prostag. Other Lipid Mediat."},{"key":"10.1016\/j.jbc.2026.111247_bib46","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1074\/jbc.271.4.2179","article-title":"Involvement of arginine 120, glutamate 524, and tyrosine 355 in the binding of arachidonate and 2-phenylpropionic acid inhibitors to the cyclooxygenase active site of ovine prostaglandin endoperoxide H synthase-1","volume":"271","author":"Bhattacharyya","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib47","doi-asserted-by":"crossref","first-page":"17109","DOI":"10.1074\/jbc.274.24.17109","article-title":"The role of arginine 120 of human prostaglandin endoperoxide H synthase-2 in the interaction with fatty acid substrates and inhibitors","volume":"274","author":"Rieke","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib48","doi-asserted-by":"crossref","first-page":"21181","DOI":"10.1074\/jbc.272.34.21181","article-title":"Synthesis of prostaglandin E2 ethanolamide from anandamide by cyclooxygenase-2","volume":"272","author":"Yu","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib49","doi-asserted-by":"crossref","first-page":"33744","DOI":"10.1074\/jbc.M007088200","article-title":"Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2","volume":"275","author":"Kozak","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib50","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2025.110870","article-title":"Endocannabinoid oxygenation by prostaglandin H synthase-2: chemistry and biology","volume":"301","author":"Rouzer","year":"2025","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib51","doi-asserted-by":"crossref","first-page":"20736","DOI":"10.1074\/jbc.M111.230367","article-title":"The structural basis of endocannabinoid oxygenation by cyclooxygenase-2","volume":"286","author":"Vecchio","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib52","doi-asserted-by":"crossref","first-page":"9280","DOI":"10.1074\/jbc.272.14.9280","article-title":"Conversion of prostaglandin G\/H synthase-1 into an enzyme sensitive to PGHS-2-selective inhibitors by a double His513 --> Arg and Ile523 --> val mutation","volume":"272","author":"Wong","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib53","doi-asserted-by":"crossref","first-page":"7592","DOI":"10.1021\/acs.chemrev.0c00215","article-title":"Structural and chemical biology of the interaction of cyclooxygenase with substrates and non-steroidal anti-inflammatory drugs","volume":"120","author":"Rouzer","year":"2020","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2026.111247_bib54","doi-asserted-by":"crossref","first-page":"33157","DOI":"10.1074\/jbc.271.52.33157","article-title":"Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2","volume":"271","author":"Smith","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib55","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/367243a0","article-title":"The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1","volume":"367","author":"Picot","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111247_bib56","doi-asserted-by":"crossref","first-page":"1933","DOI":"10.1126\/science.289.5486.1933","article-title":"The productive conformation of arachidonic acid bound to prostaglandin synthase","volume":"289","author":"Malkowski","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111247_bib57","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/nsb0895-637","article-title":"The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase","volume":"2","author":"Loll","year":"1995","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.111247_bib58","doi-asserted-by":"crossref","first-page":"13207","DOI":"10.1016\/S0021-9258(17)36820-5","article-title":"Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin","volume":"269","author":"Lecomte","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib59","doi-asserted-by":"crossref","first-page":"4743","DOI":"10.1074\/jbc.275.7.4743","article-title":"Stereospecificity of hydrogen abstraction in the conversion of arachidonic acid to 15R-HETE by aspirin-treated cyclooxygenase-2","volume":"275","author":"Schneider","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib60","doi-asserted-by":"crossref","first-page":"6586","DOI":"10.1074\/jbc.275.9.6586","article-title":"Spatial requirements for 15-(R)-hydroxy-5Z,8Z,11Z,13E-eicosatetraenoic acid synthesis within the cyclooxygenase active site of murine COX-2. Why acetylated COX-1 does not synthesize 15-(R)-HETE","volume":"275","author":"Rowlinson","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib61","doi-asserted-by":"crossref","first-page":"3206","DOI":"10.1021\/bi052338h","article-title":"Molecular dynamics simulations of arachidonic acid-derived pentadienyl radical intermediate complexes with COX-1 and COX-2: insights into oxygenation regio- and stereoselectivity","volume":"45","author":"Furse","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.111247_bib62","doi-asserted-by":"crossref","first-page":"1226","DOI":"10.1021\/acs.biochem.5b01378","article-title":"Crystal structure of aspirin-acetylated human cyclooxygenase-2: insight into the formation of products with reversed stereochemistry","volume":"55","author":"Lucido","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.111247_bib63","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1021\/acscatal.9b04223","article-title":"Understanding the molecular details of the mechanism that governs the oxidation of rrachidonic acid catalyzed by aspirin-acetylated cyclooxygenase-2","volume":"10","author":"Cebri\u00e1n-Prats","year":"2020","journal-title":"ACS Catal."},{"key":"10.1016\/j.jbc.2026.111247_bib64","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.chembiol.2007.04.007","article-title":"Control of oxygenation in lipoxygenase and cyclooxygenase catalysis","volume":"14","author":"Schneider","year":"2007","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2026.111247_bib65","doi-asserted-by":"crossref","first-page":"9041","DOI":"10.1021\/bi034471k","article-title":"Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid anandamide","volume":"42","author":"Kozak","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.111247_bib66","doi-asserted-by":"crossref","first-page":"30072","DOI":"10.1074\/jbc.M104467200","article-title":"Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol","volume":"276","author":"Kozak","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111247_bib67","doi-asserted-by":"crossref","first-page":"7700","DOI":"10.1073\/pnas.131022398","article-title":"The origin of 15R-prostaglandins in the Caribbean coral Plexaura homomalla: molecular cloning and expression of a novel cyclooxygenase","volume":"98","author":"Valmsen","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111247_bib68","doi-asserted-by":"crossref","first-page":"3533","DOI":"10.1111\/j.0014-2956.2004.04289.x","article-title":"Structural and functional comparison of 15S- and 15R-specific cyclooxygenases from the coral Plexaura homomalla","volume":"271","author":"Valmsen","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2026.111247_bib69","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1007\/s11745-004-1339-7","article-title":"Resolvins, docosatrienes, and neuroprotectins, novel omega-3-derived mediators, and their endogenous aspirin-triggered epimers","volume":"39","author":"Serhan","year":"2004","journal-title":"Lipids"},{"key":"10.1016\/j.jbc.2026.111247_bib70","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1016\/j.chembiol.2011.06.008","article-title":"Novel proresolving aspirin-triggered DHA pathway","volume":"18","author":"Serhan","year":"2011","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2026.111247_bib71","doi-asserted-by":"crossref","first-page":"6292","DOI":"10.1073\/pnas.1804000116","article-title":"Aspirin-triggered proresolving mediators stimulate resolution in cancer","volume":"116","author":"Gilligan","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111247_bib72","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1038\/mi.2015.129","article-title":"Aspirin-triggered resolvin D1 is produced during self-resolving gram-negative bacterial pneumonia and regulates host immune responses for the resolution of lung inflammation","volume":"9","author":"Abdulnour","year":"2016","journal-title":"Mucosal Immunol."},{"key":"10.1016\/j.jbc.2026.111247_bib73","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1096\/fj.201801018R","article-title":"Residual cyclooxygenase activity of aspirin-acetylated COX-2 forms 15R-prostaglandins that inhibit platelet aggregation","volume":"33","author":"Gim\u00e9nez-Bastida","year":"2019","journal-title":"FASEB J."},{"key":"10.1016\/j.jbc.2026.111247_bib74","doi-asserted-by":"crossref","first-page":"7353","DOI":"10.1021\/bi900999z","article-title":"Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid","volume":"48","author":"Prusakiewicz","year":"2009","journal-title":"Biochemistry"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826001171?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826001171?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T23:16:30Z","timestamp":1776381390000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826001171"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":74,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2026,3]]}},"alternative-id":["S0021925826001171"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.111247","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Unusual and atypical cyclooxygenase reactions","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.111247","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":"111247"}}