{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T13:50:21Z","timestamp":1790862621836,"version":"4.1.0"},"reference-count":97,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,7,22]],"date-time":"2025-07-22T00:00:00Z","timestamp":1753142400000},"content-version":"am","delay-in-days":629,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100013349","name":"LABoratoires d\u2019EXcellence ARCANE","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013349","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-17-EURE-0003"],"award-info":[{"award-number":["ANR-17-EURE-0003"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-19-CE44-0002"],"award-info":[{"award-number":["ANR-19-CE44-0002"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2023,11]]},"DOI":"10.1016\/j.ejmech.2023.115672","type":"journal-article","created":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T23:58:15Z","timestamp":1689811095000},"page":"115672","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"special_numbering":"C","title":["Catechol-mimicking transition-state analogues as non-oxidizable inhibitors of tyrosinases"],"prefix":"10.1016","volume":"259","author":[{"given":"Morane","family":"Beaumet","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leticia M.","family":"Lazinski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc","family":"Maresca","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6271-4717","authenticated-orcid":false,"given":"Romain","family":"Haudecoeur","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2023.115672_bib1","series-title":"Ser. Chem. Energy Environ.","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1142\/9789813274440_0007","article-title":"enzymes, models and related applications","author":"Bijelic","year":"2019"},{"key":"10.1016\/j.ejmech.2023.115672_bib2","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1034\/j.1600-0749.2003.00037.x","article-title":"A chemist's view of melanogenesis","volume":"16","author":"Ito","year":"2003","journal-title":"Pigm. Cell Res."},{"key":"10.1016\/j.ejmech.2023.115672_bib3","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1021\/jf020826f","article-title":"Mushroom tyrosinase: recent prospects","volume":"51","author":"Seo","year":"2003","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib4","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1016\/j.procbio.2012.08.018","article-title":"Bacterial tyrosinases and their applications","volume":"47","author":"Faccio","year":"2012","journal-title":"Process Biochem."},{"key":"10.1016\/j.ejmech.2023.115672_bib5","doi-asserted-by":"crossref","first-page":"82","DOI":"10.3390\/cosmetics8030082","article-title":"Melanogenesis and melasma treatment","volume":"8","author":"Maddaleno","year":"2021","journal-title":"Cosmetics"},{"key":"10.1016\/j.ejmech.2023.115672_bib6","doi-asserted-by":"crossref","first-page":"3033","DOI":"10.2174\/1568026616666160216160112","article-title":"Are human tyrosinase and related proteins suitable targets for melanoma therapy?","volume":"16","author":"Buitrago","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib7","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/s41467-019-08858-y","article-title":"Brain tyrosinase overexpression implicates age-dependent neuromelanin production in Parkinson's disease pathogenesis","volume":"10","author":"Carballo-Carbajal","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2023.115672_bib8","doi-asserted-by":"crossref","first-page":"13428","DOI":"10.1021\/acs.jmedchem.0c00994","article-title":"Advances in the design of genuine human tyrosinase inhibitors for targeting melanogenesis and related pigmentations","volume":"63","author":"Roulier","year":"2020","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib9","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1111\/j.1541-4337.2012.00191.x","article-title":"Natural and synthetic tyrosinase inhibitors as antibrowning agents: an update","volume":"11","author":"Loizzo","year":"2012","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"10.1016\/j.ejmech.2023.115672_bib10","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1021\/ja01183a090","article-title":"The oxidation of catechol-type substrates by tyrosinase","volume":"70","author":"Cushing","year":"1948","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2023.115672_bib11","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1042\/bj0440442","article-title":"The action of tyrosinase on monophenols","volume":"44","author":"Kendal","year":"1949","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2023.115672_bib12","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1046\/j.1432-1327.2000.01013.x","article-title":"Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase","volume":"267","author":"Espin","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ejmech.2023.115672_bib13","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0187845","article-title":"Structural and kinetic considerations on the catalysis of deoxyarbutin by tyrosinase","volume":"12","author":"Garcia-Jimenez","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2023.115672_bib14","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.bbrc.2012.06.074","volume":"424","author":"Munoz-Munoz","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ejmech.2023.115672_bib15","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1002\/bab.1998","article-title":"Study of tyrosine and dopa enantiomers as tyrosinase substrates initiating l- and d-melanogenesis pathways","volume":"68","author":"Fernandez-Julia","year":"2021","journal-title":"Biotechnol. Appl. Biochem."},{"key":"10.1016\/j.ejmech.2023.115672_bib16","doi-asserted-by":"crossref","first-page":"1594","DOI":"10.1016\/S1357-2725(02)00076-6","article-title":"Kinetic characterisation of the reaction mechanism of mushroom tyrosinase on tyramine\/dopamine and l-tyrosine methyl esther\/l-dopa methyl esther","volume":"34","author":"Fenoll","year":"2002","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.ejmech.2023.115672_bib17","doi-asserted-by":"crossref","first-page":"3360","DOI":"10.1016\/j.bmc.2014.04.048","article-title":"Tyrosinase-catalyzed hydroxylation of hydroquinone, a depigmenting agent, to hydroxyhydroquinone: a kinetic study","volume":"22","author":"Garcia-Molina","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib18","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0177330","article-title":"Action of tyrosinase on alpha and beta-arbutin: a kinetic study","volume":"12","author":"Garcia-Jimenez","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2023.115672_bib19","first-page":"828","article-title":"Kinetic characterization of oxyresveratrol as a tyrosinase substrate","volume":"67","author":"Ortiz-Ruiz","year":"2015","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.ejmech.2023.115672_bib20","doi-asserted-by":"crossref","first-page":"2925","DOI":"10.1021\/acs.jafc.6b00286","article-title":"Recombinant tyrosinase from Polyporus arcularius: overproduction in Escherichia coli, characterization, and use in a study of aurones as tyrosinase effectors","volume":"64","author":"Markova","year":"2016","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib21","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.molcatb.2013.02.003","article-title":"Catalysis and inactivation of tyrosinase in its action on o-diphenols, o-aminophenols and o-phenylendiamines: potential use in industrial applications","volume":"91","author":"Munoz-Munoz","year":"2013","journal-title":"J. Mol. Catal. B Enzym."},{"key":"10.1016\/j.ejmech.2023.115672_bib22","doi-asserted-by":"crossref","first-page":"2650","DOI":"10.1016\/j.ijbiomac.2017.10.151","article-title":"Action of tyrosinase on caffeic acid and its n-nonyl ester. Catalysis and suicide inactivation","volume":"107","author":"Garcia-Jimenez","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ejmech.2023.115672_bib23","doi-asserted-by":"crossref","first-page":"7781","DOI":"10.1021\/jf034656y","article-title":"Kinetic study of the oxidation of quercetin by mushroom tyrosinase","volume":"51","author":"Fenoll","year":"2003","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib24","doi-asserted-by":"crossref","first-page":"619","DOI":"10.3839\/jksabc.2011.093","article-title":"Oxidation of rosmarinic acid catalyzed by mushroom tyrosinase","volume":"54","author":"Ha","year":"2011","journal-title":"J. Korean Soc. Appl. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib25","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1007\/s12033-014-9800-y","article-title":"Human tyrosinase produced in insect cells: a landmark for the screening of new drugs addressing its activity","volume":"57","author":"Fogal","year":"2015","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.ejmech.2023.115672_bib26","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.foodchem.2008.07.076","article-title":"Enzymatic and chemical oxidation of trihydroxylated phenols","volume":"113","author":"Munoz-Munoz","year":"2009","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib27","doi-asserted-by":"crossref","first-page":"4434","DOI":"10.1016\/j.bmc.2016.07.048","article-title":"Characterization of the action of tyrosinase on resorcinols","volume":"24","author":"Garcia-Jimenez","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib28","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1016\/j.jid.2018.01.019","article-title":"Inhibition of human tyrosinase requires molecular motifs distinctively different from mushroom tyrosinase","volume":"138","author":"Mann","year":"2018","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.ejmech.2023.115672_bib29","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.1021\/jf5051816","article-title":"Discrimination between alternative substrates and inhibitors of tyrosinase","volume":"63","author":"Ortiz-Ruiz","year":"2015","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib30","article-title":"Quercetin is a substrate not an inhibitor of tyrosinase - comments on \u201cQuercetin as a tyrosinase inhibitor: inhibitory activity, conformational change and mechanism\u201d published by Fan et al","volume":"153","author":"Wojtasek","year":"2017","journal-title":"Food Res. Int."},{"key":"10.1016\/j.ejmech.2023.115672_bib31","article-title":"Letter to the Editor: evaluation of inhibitory effects of some novel phenolic derivatives on the mushroom tyrosinase activity","volume":"398","author":"Garcia-Molina","year":"2023","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib32","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1080\/14756366.2018.1545767","article-title":"A comprehensive review on tyrosinase inhibitors","volume":"34","author":"Zolghadri","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib33","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113744","article-title":"Recent advances in the design and discovery of synthetic tyrosinase inhibitors","volume":"224","author":"Li","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib34","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114525","article-title":"Azole inhibitors of mushroom and human tyrosinases: current advances and prospects of drug development for melanogenic dermatological disorders","volume":"239","author":"Ghani","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib35","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1039\/C8MD00372F","article-title":"The transition to magic bullets \u2013 transition state analogue drug design","volume":"9","author":"Evans","year":"2018","journal-title":"Med. Chem. Commun."},{"key":"10.1016\/j.ejmech.2023.115672_bib36","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1039\/b416256k","article-title":"Metal complexes of maltol and close analogues in medicinal inorganic chemistry","volume":"35","author":"Thompson","year":"2006","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.ejmech.2023.115672_bib37","doi-asserted-by":"crossref","first-page":"10206","DOI":"10.1021\/acs.jmedchem.8b01363","article-title":"Structure\u2013activity relationships in metal-binding pharmacophores for influenza endonuclease","volume":"61","author":"Credille","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib38","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1021\/ml500502d","article-title":"Synthesis and evaluation of heterocyclic catechol mimics as inhibitors of catechol-O-methyltransferase (COMT)","volume":"6","author":"Harrison","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib39","doi-asserted-by":"crossref","first-page":"10052","DOI":"10.1021\/bi970469f","article-title":"Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding","volume":"36","author":"Orville","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2023.115672_bib40","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1007\/s00775-017-1454-3","article-title":"Effect of donor atom identity on metal-binding pharmacophore coordination","volume":"22","author":"Dick","year":"2017","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib41","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1002\/ardp.200500213","article-title":"Synthesis of tyrosinase inhibitory kojic acid derivative","volume":"339","author":"Lee","year":"2006","journal-title":"Arch. Pharm. Chem. Life Sci."},{"key":"10.1016\/j.ejmech.2023.115672_bib42","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.bmcl.2008.10.119","article-title":"Synthesis of tyrosinase inhibitory (4-oxo-4H-pyran-2-yl)acrylic acid ester derivatives","volume":"19","author":"Kang","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib43","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1038\/513481a","article-title":"Chemical con artists foil drug discovery","volume":"513","author":"Baell","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2023.115672_bib44","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1021\/acs.jnatprod.5b00947","article-title":"Natural products, natural product drugs, and pan assay interference compounds (PAINS)","volume":"79","author":"Baell","year":"2016","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.ejmech.2023.115672_bib45","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1021\/acs.jmedchem.5b01009","article-title":"Can invalid bioactives undermine natural product-based drug discovery?","volume":"59","author":"Bisson","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib46","doi-asserted-by":"crossref","first-page":"471","DOI":"10.5012\/bkcs.2007.28.3.471","article-title":"New 5-hydroxy-2-(hydroxymethyl)-4H-pyran-4-one derivative has both tyrosinase inhibitory and antioxidant properties","volume":"28","author":"Rho","year":"2007","journal-title":"Bull. Kor. Chem. Soc."},{"key":"10.1016\/j.ejmech.2023.115672_bib47","doi-asserted-by":"crossref","first-page":"4411","DOI":"10.5012\/bkcs.2011.32.12.4411","article-title":"Studies on tyrosinase inhibitory and antioxidant activities of benzoic acid derivatives containing kojic acid moiety","volume":"32","author":"Rho","year":"2011","journal-title":"Bull. Kor. Chem. Soc."},{"key":"10.1016\/j.ejmech.2023.115672_bib48","doi-asserted-by":"crossref","first-page":"7466","DOI":"10.1016\/j.bmcl.2011.09.122","article-title":"Inhibitory activity of novel kojic acid derivative containing trolox moiety on melanogenesis","volume":"21","author":"Ahn","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.crfs.2022.100421","article-title":"Tyrosinase inhibitory mechanism and anti-browning properties of novel kojic acid derivatives bearing aromatic aldehyde moiety","volume":"6","author":"Peng","year":"2023","journal-title":"Curr. Res. Food Sci."},{"key":"10.1016\/j.ejmech.2023.115672_bib50","doi-asserted-by":"crossref","first-page":"6569","DOI":"10.1016\/j.bmcl.2010.09.042","article-title":"Kojyl thioether derivatives having both tyrosinase inhibitory and anti-inflammatory properties","volume":"20","author":"Rho","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib51","series-title":"Strukturbasierte Entwicklung von Inhibitoren der humanen Tyrosinase und der Farnesyltransferase","author":"M\u00e4del","year":"2009"},{"key":"10.1016\/j.ejmech.2023.115672_bib52","doi-asserted-by":"crossref","first-page":"4330","DOI":"10.1016\/j.ejmech.2011.07.003","article-title":"Refinement of arylthiosemicarbazone pharmacophore in inhibition of mushroom tyrosinase","volume":"46","author":"Yi","year":"2011","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib53","doi-asserted-by":"crossref","first-page":"4384","DOI":"10.1002\/chem.202004695","article-title":"Ditopic chelators of dicopper centers for enhanced tyrosinases inhibition","volume":"27","author":"Buitrago","year":"2021","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.ejmech.2023.115672_bib54","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2023.136106","article-title":"Anti-browning and antibacterial dual functions of novel hydroxypyranone-thiosemicarbazone derivatives as shrimp preservative agents: synthesis, bio-evaluation, mechanism, and application","volume":"419","author":"Peng","year":"2023","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib55","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.jinorgbio.2015.07.001","article-title":"Metal coordination and tyrosinase inhibition studies with kojic-\u03b2Ala-kojic","volume":"151","author":"Lachowicz","year":"2015","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.ejmech.2023.115672_bib56","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.5012\/bkcs.2008.29.8.1569","article-title":"Synthesis of new anti-melanogenic compounds containing two molecules of kojic acid","volume":"29","author":"Rho","year":"2008","journal-title":"Bull. Kor. Chem. Soc."},{"key":"10.1016\/j.ejmech.2023.115672_bib57","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1002\/bip.20670","article-title":"Kojic acid\u2013tripeptide amide as a new tyrosinase inhibitor","volume":"88","author":"Noh","year":"2007","journal-title":"Biopolymers"},{"key":"10.1016\/j.ejmech.2023.115672_bib58","doi-asserted-by":"crossref","first-page":"5586","DOI":"10.1016\/j.bmcl.2009.08.041","article-title":"Kojic acid\u2013amino acid conjugates as tyrosinase inhibitors","volume":"19","author":"Noh","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib59","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2021.116044","article-title":"The natural-based optimization of kojic acid conjugated to different thio-quinazolinones as potential anti-melanogenesis agents with tyrosinase inhibitory activity","volume":"36","author":"Sepehri","year":"2021","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib60","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2021.130241","article-title":"Design, synthesis, molecular modeling, and biological evaluation of novel kojic acid derivatives containing bioactive heterocycle moiety as inhibitors of tyrosinase and antibrowning agents","volume":"362","author":"He","year":"2021","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib61","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1016\/j.bioorg.2018.10.069","article-title":"1,2,3-Triazole-based kojic acid analogs as potent tyrosinase inhibitors: design, synthesis and biological evaluation","volume":"82","author":"Ashooriha","year":"2019","journal-title":"Bioog. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib62","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112480","article-title":"Kojic acid\u2013natural product conjugates as mushroom tyrosinase inhibitors","volume":"201","author":"Ashooriha","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib63","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1111\/cbdd.12577","article-title":"Synthesis and biological evaluation of kojic acid derivatives containing 1,2,4-triazole as potent tyrosinase inhibitors","volume":"86","author":"Xie","year":"2015","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.ejmech.2023.115672_bib64","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.ijbiomac.2018.11.031","article-title":"Anti-melanogenesis of novel kojic acid derivatives in B16F10 cells and zebrafish","volume":"123","author":"Chen","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ejmech.2023.115672_bib65","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/j.bmcl.2016.12.027","article-title":"Synthesis and biological evaluation of novel hydroxybenzaldehyde-based kojic acid analogues as inhibitors of mushroom tyrosinase","volume":"27","author":"Xie","year":"2017","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib66","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2022.133707","article-title":"Biological evaluation, and molecular docking analysis of novel 1,3,4-thiadiazole-based kojic acid derivatives as tyrosinase inhibitors","volume":"1268","author":"Talebi","year":"2022","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ejmech.2023.115672_bib67","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2022.135275","article-title":"Synthesis and biological evaluation of new kojic acid-1,3,4-oxadiazole hybrids as tyrosinase inhibitors and their application in the anti-browning of fresh-cut mushrooms","volume":"409","author":"Wang","year":"2023","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2023.136047","article-title":"Novel kojic acid-1,2,4-triazine hybrids as anti-tyrosinase agents: synthesis, biological evaluation, mode of action, and anti-browning studies","volume":"419","author":"He","year":"2023","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib69","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1042\/bj2570289","article-title":"The inhibition of tyrosinase by pyridinones","volume":"257","author":"Hider","year":"1989","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2023.115672_bib70","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2022.111879","article-title":"A combined experimental and computational study to discover novel tyrosinase inhibitors","volume":"234","author":"Amaral","year":"2022","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.ejmech.2023.115672_bib71","doi-asserted-by":"crossref","first-page":"14334","DOI":"10.3390\/molecules200814334","article-title":"Mimosine dipeptide enantiomers: improved inhibitors against melanogenesis and cyclooxygenase","volume":"20","author":"Nguyen","year":"2015","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2023.115672_bib72","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1080\/14756366.2020.1801669","article-title":"Functionality study of chalcone-hydroxypyridinone hybrids as tyrosinase inhibitors and influence on anti-tyrosinase activity","volume":"35","author":"Singh","year":"2020","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib73","doi-asserted-by":"crossref","first-page":"3103","DOI":"10.1016\/j.bmcl.2016.05.006","article-title":"Design and synthesis of novel hydroxypyridinone derivatives as potential tyrosinase inhibitors","volume":"26","author":"Zhao","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib74","doi-asserted-by":"crossref","first-page":"2146","DOI":"10.1007\/s11947-017-1976-2","article-title":"A novel inhibitor against mushroom tyrosinase with a double action mode and its application in controlling the browning of potato","volume":"10","author":"Chen","year":"2017","journal-title":"Food Bioprocess Technol."},{"key":"10.1016\/j.ejmech.2023.115672_bib75","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.foodchem.2017.09.054","article-title":"Novel hydroxypyridinone derivatives containing an oxime ether moiety: synthesis, inhibition on mushroom tyrosinase and application in anti-browning of fresh-cut apples","volume":"242","author":"Shao","year":"2018","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib76","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2022.132730","article-title":"Design and synthesis of novel stilbene-hydroxypyridinone hybrids as tyrosinase inhibitors and their application in the anti-browning of freshly-cut apples","volume":"385","author":"Zhu","year":"2022","journal-title":"Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib77","doi-asserted-by":"crossref","first-page":"6597","DOI":"10.1021\/jf401585f","article-title":"Design and synthesis of hydroxypyridinone-l-phenylalanine conjugates as potential tyrosinase inhibitors","volume":"61","author":"Li","year":"2013","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib78","doi-asserted-by":"crossref","first-page":"10874","DOI":"10.1021\/ic901593x","article-title":"Binding of 2-hydroxypyridine-N-oxide on dicopper(II) centers: insights into tyrosinase inhibition mechanism by transition-state analogs","volume":"48","author":"Peyroux","year":"2009","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib79","doi-asserted-by":"crossref","first-page":"3655","DOI":"10.1002\/chem.201202643","article-title":"Unsymmetrical binding modes of the HOPNO inhibitor of tyrosinase: from model complexes to the enzyme","volume":"19","author":"Bochot","year":"2013","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.ejmech.2023.115672_bib80","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1021\/acsmedchemlett.6b00369","article-title":"2-Hydroxypyridine-N-oxide-embedded aurones as potent human tyrosinase inhibitors","volume":"8","author":"Haudecoeur","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115672_bib81","doi-asserted-by":"crossref","first-page":"13482","DOI":"10.1002\/chem.201100665","article-title":"The versatile binding mode of transition-state analogue inhibitors of tyrosinase towards dicopper(II) model complexes: experimental and theoretical investigations","volume":"17","author":"Orio","year":"2011","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.ejmech.2023.115672_bib82","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115090","article-title":"Exploiting HOPNO-dicopper center interaction to development of inhibitors for human tyrosinase","volume":"248","author":"Buitrago","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib83","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1002\/cbic.201100716","article-title":"Versatile effects of aurone structure on mushroom tyrosinase activity","volume":"13","author":"Dubois","year":"2012","journal-title":"Chembiochem"},{"key":"10.1016\/j.ejmech.2023.115672_bib84","series-title":"Use of 3-hydroxycoumarin Derivatives","author":"Mujica-Fernaud","year":"2007"},{"key":"10.1016\/j.ejmech.2023.115672_bib85","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1016\/j.colsurfb.2018.08.008","article-title":"3-Hydroxycoumarin loaded vesicles for recombinant human tyrosinase inhibition in topical applications","volume":"171","author":"Schlich","year":"2018","journal-title":"Coll. Surf. B Biointerf."},{"key":"10.1016\/j.ejmech.2023.115672_bib86","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1111\/j.2042-7158.2012.01467.x","article-title":"Tyrosine-like condensed derivatives as tyrosinase inhibitors","volume":"64","author":"Matos","year":"2012","journal-title":"J. Pharm. Pharmacol."},{"key":"10.1016\/j.ejmech.2023.115672_bib87","doi-asserted-by":"crossref","first-page":"8112","DOI":"10.1016\/j.bmc.2010.08.056","article-title":"Structural insights into the hot spot amino acid residues of mushroom tyrosinase for the bindings of thujaplicins","volume":"18","author":"Takahashi","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib88","doi-asserted-by":"crossref","first-page":"6193","DOI":"10.1016\/j.bmc.2014.08.027","article-title":"Structure\u2013activity relationships of the thujaplicins for inhibition of human tyrosinase","volume":"22","author":"Yoshimori","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib89","doi-asserted-by":"crossref","first-page":"4505","DOI":"10.1038\/ncomms5505","article-title":"Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins","volume":"5","author":"Goldfeder","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2023.115672_bib90","doi-asserted-by":"crossref","first-page":"9812","DOI":"10.1002\/anie.201704616","article-title":"Structure of human tyrosinase related protein 1 reveals a binuclear zinc active site important for melanogenesis","volume":"56","author":"Lai","year":"2017","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ejmech.2023.115672_bib91","doi-asserted-by":"crossref","first-page":"5477","DOI":"10.1021\/bi200395t","article-title":"Crystals of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone","volume":"50","author":"Ismaya","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2023.115672_bib92","doi-asserted-by":"crossref","DOI":"10.1038\/srep34993","article-title":"The unravelling of the complex pattern of tyrosinase inhibition","volume":"6","author":"Deri","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2023.115672_bib93","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1039\/C3CC47469K","article-title":"Probing kojic acid binding to tyrosinase enzyme: insights from a model complex and QM\/MM calculations","volume":"50","author":"Bochot","year":"2014","journal-title":"Chem. Commun."},{"key":"10.1016\/j.ejmech.2023.115672_bib94","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.phytochem.2017.06.017","article-title":"Occurrences, biosynthesis and properties of aurones as high-end evolutionary products","volume":"142","author":"Boucherle","year":"2017","journal-title":"Phytochemistry"},{"key":"10.1016\/j.ejmech.2023.115672_bib95","doi-asserted-by":"crossref","first-page":"12594","DOI":"10.1021\/acs.jmedchem.2c01150","article-title":"Bioactive aurones, indanones, and other hemiindigoid scaffolds: medicinal chemistry and photopharmacology perspectives","volume":"65","author":"Lazinski","year":"2022","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115672_bib96","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1002\/cbic.201402003","article-title":"Investigation of binding-site homology between mushroom and bacterial tyrosinases by using aurones as effectors","volume":"15","author":"Haudecoeur","year":"2014","journal-title":"Chembiochem"},{"key":"10.1016\/j.ejmech.2023.115672_bib97","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114972","article-title":"Resorcinol-based hemiindigoid derivatives as human tyrosinase inhibitors and melanogenesis suppressors in human melanoma cells","volume":"246","author":"Roulier","year":"2023","journal-title":"Eur. J. Med. Chem."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423006384?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423006384?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T14:55:59Z","timestamp":1759330559000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523423006384"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,11]]},"references-count":97,"alternative-id":["S0223523423006384"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115672","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2023,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Catechol-mimicking transition-state analogues as non-oxidizable inhibitors of tyrosinases","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115672","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115672"}}