{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T03:15:33Z","timestamp":1789528533500,"version":"build-2803163510"},"reference-count":75,"publisher":"Elsevier","isbn-type":[{"value":"9780443295201","type":"print"}],"license":[{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024]]},"DOI":"10.1016\/bs.enz.2024.06.004","type":"book-chapter","created":{"date-parts":[[2024,8,6]],"date-time":"2024-08-06T19:51:13Z","timestamp":1722973873000},"page":"55-83","source":"Crossref","is-referenced-by-count":6,"title":["Structural characterization of tyrosinases and an update on human enzymes"],"prefix":"10.1016","author":[{"given":"Luigi Franklin","family":"Di Costanzo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/bs.enz.2024.06.004_bib1","doi-asserted-by":"crossref","DOI":"10.1111\/pcmr.12301","article-title":"Skin as a living coloring book: how epithelial cells create patterns of pigmentation","volume":"27","author":"Weiner","year":"2014","journal-title":"Pigment. Cell Melanoma Res."},{"key":"10.1016\/bs.enz.2024.06.004_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(19)67976-7","article-title":"Separation, purification, and properties of two tyrosinases from hamster melanoma","volume":"238","author":"Pomerantz","year":"1963","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib3","doi-asserted-by":"crossref","DOI":"10.1016\/j.ab.2022.114856","article-title":"Kinetic analyses of two-steps oxidation from L-tyrosine to L-dopaquinone with tyrosinase by capillary electrophoresis\/dynamic frontal analysis","volume":"655","author":"Mine","year":"2022","journal-title":"Anal. Biochem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib4","doi-asserted-by":"crossref","DOI":"10.1152\/physrev.1950.30.1.91","article-title":"Biochemistry of melanin formation","volume":"30","author":"Lerner","year":"1950","journal-title":"Physiol. Rev."},{"issue":"7","key":"10.1016\/bs.enz.2024.06.004_bib5","doi-asserted-by":"crossref","DOI":"10.1039\/c0cs00202j","article-title":"Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme","volume":"40","author":"Rolff","year":"2011","journal-title":"Chem. Soc. Rev."},{"issue":"7","key":"10.1016\/bs.enz.2024.06.004_bib6","doi-asserted-by":"crossref","DOI":"10.1021\/cr950046o","article-title":"Multicopper oxidases and oxygenases","volume":"96","author":"Solomon","year":"1996","journal-title":"Chem. Rev."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.004_bib7","doi-asserted-by":"crossref","DOI":"10.1002\/anie.201508534","article-title":"Tyrosinase versus catechol oxidase: one asparagine makes the difference","volume":"55","author":"Solem","year":"2016","journal-title":"Angew. Chem.\u2014Int. Ed."},{"key":"10.1016\/bs.enz.2024.06.004_bib8","doi-asserted-by":"crossref","DOI":"10.1034\/j.1600-0749.2002.02012.x","article-title":"Molecular anatomy of tyrosinase and its related proteins: beyond the histidine-bound metal catalytic center","volume":"15","author":"Garc\u00eda-Borr\u00f3n","year":"2002","journal-title":"Pigment. Cell Res."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib9","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0084494","article-title":"Albinism-causing mutations in recombinant human tyrosinase alter intrinsic enzymatic activity","volume":"9","author":"Dolinska","year":"2014","journal-title":"PLoS One"},{"issue":"5","key":"10.1016\/bs.enz.2024.06.004_bib10","doi-asserted-by":"crossref","DOI":"10.1002\/(SICI)1097-4547(19981201)54:5<691::AID-JNR14>3.0.CO;2-F","article-title":"Dopamine, in the presence of tyrosinase, covalently modifies and inactivates tyrosine hydroxylase","volume":"54","author":"Xu","year":"1998","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/bs.enz.2024.06.004_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/0031-9422(79)80057-6","article-title":"Polyphenol oxidases in plants","volume":"18","author":"Mayer","year":"1979","journal-title":"Phytochemistry"},{"key":"10.1016\/bs.enz.2024.06.004_bib12","doi-asserted-by":"crossref","DOI":"10.3390\/molecules25122754","article-title":"Recent trends in controlling the enzymatic browning of fruit and vegetable products","volume":"25","author":"Moon","year":"2020","journal-title":"Molecules"},{"issue":"10","key":"10.1016\/bs.enz.2024.06.004_bib13","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0025494","article-title":"Morphological and geochemical evidence of eumelanin preservation in the feathers of the Early Cretaceous bird, Gansus yumenensis","volume":"6","author":"Barden","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/bs.enz.2024.06.004_bib14","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20163943","article-title":"From extraction to advanced analytical methods: the challenges of melanin analysis","volume":"20","author":"Pralea","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/bs.enz.2024.06.004_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.tim.2009.06.006","article-title":"Color me bad: microbial pigments as virulence factors","volume":"17","author":"Liu","year":"2009","journal-title":"Trends Microbiol."},{"key":"10.1016\/bs.enz.2024.06.004_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2019.12.252","article-title":"A novel mechanism of inhibition by phenylthiourea on PvdP, a tyrosinase synthesizing pyoverdine of Pseudomonas aeruginosa","volume":"146","author":"Wibowo","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"issue":"37","key":"10.1016\/bs.enz.2024.06.004_bib17","doi-asserted-by":"crossref","DOI":"10.1021\/acs.est.3c02910","article-title":"Biochemical investigations of five recombinantly expressed tyrosinases reveal two novel mechanisms impacting carbon storage in wetland ecosystems","volume":"57","author":"Panis","year":"2023","journal-title":"Environ. Sci. Technol."},{"key":"10.1016\/bs.enz.2024.06.004_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2014.02.048","article-title":"Tyrosinase: the four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation","volume":"22","author":"Ramsden","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib19","doi-asserted-by":"crossref","DOI":"10.1016\/j.ica.2017.04.041","article-title":"What causes the different functionality in type-III-copper enzymes? A state of the art perspective","volume":"481","author":"Pretzler","year":"2018","journal-title":"Inorg. Chim. Acta"},{"issue":"9","key":"10.1016\/bs.enz.2024.06.004_bib20","doi-asserted-by":"crossref","DOI":"10.1016\/j.cub.2021.03.054","article-title":"Copper biology","volume":"31","author":"Tsang","year":"2021","journal-title":"Curr. Biol."},{"key":"10.1016\/bs.enz.2024.06.004_bib21","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19020633","article-title":"On the metal cofactor in the tyrosinase family","volume":"19","author":"Solano","year":"2018","journal-title":"Int. J. Mol. Sci."},{"issue":"3","key":"10.1016\/bs.enz.2024.06.004_bib22","doi-asserted-by":"crossref","DOI":"10.1038\/nchem.2916","article-title":"Transferring the entatic-state principle to copper photochemistry","volume":"10","author":"Dicke","year":"2018","journal-title":"Nat. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib23","doi-asserted-by":"crossref","DOI":"10.1002\/1873-3468.14503","article-title":"New mechanistic insights into coupled binuclear copper monooxygenases from the recent elucidation of the ternary intermediate of tyrosinase","volume":"597","author":"Kipouros","year":"2023","journal-title":"FEBS Lett."},{"key":"10.1016\/bs.enz.2024.06.004_bib24","doi-asserted-by":"crossref","DOI":"10.1007\/s00775-016-1420-5","article-title":"High-valent copper in biomimetic and biological oxidations","volume":"22","author":"Keown","year":"2017","journal-title":"J. Biol. Inorg. Chem."},{"issue":"33","key":"10.1016\/bs.enz.2024.06.004_bib25","doi-asserted-by":"crossref","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.\u2014Int. Ed."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib26","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-01813-1","article-title":"Heterologous expression and characterization of functional mushroom tyrosinase (AbPPO4)","volume":"7","author":"Pretzler","year":"2017","journal-title":"Sci. Rep."},{"issue":"24","key":"10.1016\/bs.enz.2024.06.004_bib27","doi-asserted-by":"crossref","DOI":"10.1021\/bi200395t","article-title":"Crystal structure of agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone","volume":"50","author":"Ismaya","year":"2011","journal-title":"Biochemistry"},{"issue":"9","key":"10.1016\/bs.enz.2024.06.004_bib28","doi-asserted-by":"crossref","DOI":"10.1107\/S1399004714013777","article-title":"Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal","volume":"70","author":"Mauracher","year":"2014","journal-title":"Acta Crystallogr. Sect. D. Biol. Crystallogr."},{"issue":"30","key":"10.1016\/bs.enz.2024.06.004_bib29","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M113.477612","article-title":"Crystal structures of copper-depleted and copper-bound fungal pro-tyrosinase: insights into endogenous cysteine-dependent copper incorporation","volume":"288","author":"Fujieda","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"32","key":"10.1016\/bs.enz.2024.06.004_bib30","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202004733","article-title":"Copper\u2013oxygen dynamics in the tyrosinase mechanism","volume":"59","author":"Fujieda","year":"2020","journal-title":"Angew. Chem.\u2014Int. Ed."},{"issue":"3","key":"10.1016\/bs.enz.2024.06.004_bib32","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21030915","article-title":"Phenylthiourea binding to human tyrosinase-related protein 1","volume":"21","author":"Lai","year":"2020","journal-title":"Int. J. Mol. Sci."},{"issue":"49","key":"10.1016\/bs.enz.2024.06.004_bib33","doi-asserted-by":"crossref","DOI":"10.1002\/anie.201506994","article-title":"The structure of a plant tyrosinase from Walnut leaves reveals the importance of \u201csubstrate-guiding residues\u201d for enzymatic specificity","volume":"54","author":"Bijelic","year":"2015","journal-title":"Angew. Chem.\u2014Int. Ed."},{"issue":"22","key":"10.1016\/bs.enz.2024.06.004_bib34","doi-asserted-by":"crossref","DOI":"10.1002\/anie.201901332","article-title":"A peptide-induced self-cleavage reaction initiates the activation of tyrosinase","volume":"58","author":"Kampatsikas","year":"2019","journal-title":"Angew. Chem.\u2014Int. Ed."},{"key":"10.1016\/bs.enz.2024.06.004_bib35","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.06.019","article-title":"Exploiting the 1-(4-fluorobenzyl)piperazine fragment for the development of novel tyrosinase inhibitors as anti-melanogenic agents: Design, synthesis, structural insights and biological profile","volume":"178","author":"Ielo","year":"2019","journal-title":"Eur. J. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2024.06.004_bib36","doi-asserted-by":"crossref","DOI":"10.1021\/acs.jmedchem.7b01745","article-title":"Targeting tyrosinase: development and structural insights of novel inhibitors bearing arylpiperidine and arylpiperazine fragments","volume":"61","author":"Ferro","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib37","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\/bs.enz.2024.06.004_bib38","doi-asserted-by":"crossref","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."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.004_bib39","doi-asserted-by":"crossref","DOI":"10.1007\/s00775-013-1034-0","article-title":"The mechanism of copper uptake by tyrosinase from Bacillus megaterium","volume":"18","author":"Kanteev","year":"2013","journal-title":"J. Biol. Inorg. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib40","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2010.10.048","article-title":"First structures of an active bacterial tyrosinase reveal copper plasticity","volume":"405","author":"Sendovski","year":"2011","journal-title":"J. Mol. Biol."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib41","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-39687-0","article-title":"Biochemical and structural characterization of tomato polyphenol oxidases provide novel insights into their substrate specificity","volume":"9","author":"Kampatsikas","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/bs.enz.2024.06.004_bib42","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2021.05.206","article-title":"The basicity of an active-site water molecule discriminates between tyrosinase and catechol oxidase activity","volume":"183","author":"Matoba","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"issue":"34","key":"10.1016\/bs.enz.2024.06.004_bib43","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M111.256818","article-title":"A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein","volume":"286","author":"Matoba","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2024.06.004_bib44","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M509785200","article-title":"Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis","volume":"281","author":"Matoba","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.004_bib45","doi-asserted-by":"crossref","DOI":"10.1128\/AEM.00396-21","article-title":"Considerations regarding activity determinants of fungal polyphenol oxidases based on mutational and structural studies","volume":"87","author":"Nikolaivits","year":"2021","journal-title":"Appl. Environ. Microbiol."},{"issue":"9","key":"10.1016\/bs.enz.2024.06.004_bib46","doi-asserted-by":"crossref","DOI":"10.3390\/biom13091360","article-title":"The crystal structure of tyrosinase from Verrucomicrobium spinosum reveals it to be an atypical bacterial tyrosinase","volume":"13","author":"Fekry","year":"2023","journal-title":"Biomolecules"},{"issue":"2","key":"10.1016\/bs.enz.2024.06.004_bib47","doi-asserted-by":"crossref","DOI":"10.1021\/jf902939q","article-title":"Cloning, sequencing, purification, and crystal structure of grenache (Vitis vinifera) polyphenol oxidase","volume":"58","author":"Virador","year":"2010","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib48","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkaa1038","article-title":"RCSB protein data bank: powerful new tools for exploring 3D structures of biological macromolecules for basic and applied research and education in fundamental biology, biomedicine, biotechnology, bioengineering and energy sciences","author":"Burley","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/bs.enz.2024.06.004_bib49","doi-asserted-by":"crossref","DOI":"10.1038\/sdata.2018.212","article-title":"Analysis: analysis of impact metrics for the protein data bank","volume":"5","author":"Markosian","year":"2018","journal-title":"Sci. Data"},{"key":"10.1016\/bs.enz.2024.06.004_bib50","doi-asserted-by":"crossref","DOI":"10.1002\/pro.3730","article-title":"RCSB protein data bank: enabling biomedical research and drug discovery","author":"Goodsell","year":"2020","journal-title":"Protein Sci."},{"issue":"7873","key":"10.1016\/bs.enz.2024.06.004_bib51","doi-asserted-by":"crossref","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/bs.enz.2024.06.004_bib52","doi-asserted-by":"crossref","DOI":"10.1002\/iub.435","article-title":"The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1-h) reveals disulfide bridges","author":"Jaenicke","year":"2011","journal-title":"IUBMB Life"},{"key":"10.1016\/bs.enz.2024.06.004_bib53","doi-asserted-by":"crossref","DOI":"10.1007\/s12551-017-0349-4","article-title":"Molluscan hemocyanin: structure, evolution, and physiology","volume":"10","author":"Kato","year":"2018","journal-title":"Biophys. Rev."},{"issue":"22","key":"10.1016\/bs.enz.2024.06.004_bib54","doi-asserted-by":"crossref","DOI":"10.1002\/cbic.201800387","article-title":"Unraveling substrate specificity and catalytic promiscuity of Aspergillus oryzae catechol oxidase","volume":"19","author":"Penttinen","year":"2018","journal-title":"ChemBioChem"},{"key":"10.1016\/bs.enz.2024.06.004_bib55","doi-asserted-by":"crossref","DOI":"10.1016\/S0959-440X(99)00029-9","article-title":"Catechol oxidase\u2014structure and activity","volume":"9","author":"Eicken","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"13","key":"10.1016\/bs.enz.2024.06.004_bib56","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1523575113","article-title":"Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases","volume":"113","author":"Molitor","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2024.06.004_bib57","article-title":"Similar but still different: which amino acid residues are responsible for varying activities in type-III copper enzymes?","volume":"22","author":"Kampatsikas","year":"2021","journal-title":"ChemBioChem"},{"issue":"31","key":"10.1016\/bs.enz.2024.06.004_bib58","doi-asserted-by":"crossref","DOI":"10.1002\/chem.200800799","article-title":"Aromatic hydroxylation in a copper bis(imine) complex mediated by a \u03bc-\u03b72:\u03b72 peroxo dicopper core: a mechanistic scenario","volume":"14","author":"Sander","year":"2008","journal-title":"Chem.\u2014Eur. J."},{"key":"10.1016\/bs.enz.2024.06.004_bib59","doi-asserted-by":"crossref","DOI":"10.1002\/anie.200601255","article-title":"The first crystal structure of tyrosinase: all questions answered?","volume":"45","author":"Decker","year":"2006","journal-title":"Angew. Chem.\u2014Int. Ed."},{"key":"10.1016\/bs.enz.2024.06.004_bib60","doi-asserted-by":"crossref","DOI":"10.1038\/4193","article-title":"Crystal structure of a plant catechol oxidase containing a dicopper center","volume":"5","author":"Klabunde","year":"1998","journal-title":"Nat. Struct. Biol."},{"issue":"2","key":"10.1016\/bs.enz.2024.06.004_bib61","doi-asserted-by":"crossref","DOI":"10.1007\/s00775-009-0577-6","article-title":"Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations","volume":"15","author":"Deeth","year":"2010","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib62","doi-asserted-by":"crossref","DOI":"10.1016\/j.fochx.2024.101128","article-title":"Synthesis, anti-browning effect and mechanism research of kojic acid-coumarin derivatives as anti-tyrosinase inhibitors","volume":"21","author":"He","year":"2024","journal-title":"Food Chem. X"},{"key":"10.1016\/bs.enz.2024.06.004_bib63","doi-asserted-by":"crossref","DOI":"10.1080\/10408398.2021.1871724","article-title":"A systematic review of synthetic tyrosinase inhibitors and their structure-activity relationship","volume":"Vol. 62","author":"Peng","year":"2022","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"10.1016\/bs.enz.2024.06.004_bib64","series-title":"Metalloenzymes: From Bench to Bedside","article-title":"Tyrosinase enzyme and its inhibitors: an update of the literature","author":"Carradori","year":"2023"},{"key":"10.1016\/bs.enz.2024.06.004_bib65","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2018.1545767","article-title":"A comprehensive review on tyrosinase inhibitors","volume":"34","author":"Zolghadri","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib66","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2018.12.006","article-title":"Kojic acid applications in cosmetic and pharmaceutical preparations","volume":"110","author":"Saeedi","year":"2019","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/bs.enz.2024.06.004_bib67","doi-asserted-by":"crossref","DOI":"10.3390\/cosmetics11010021","article-title":"Nanotechnology-enhanced cosmetic application of kojic acid dipalmitate, a kojic acid derivate with improved properties","volume":"11","author":"Ayuhastuti","year":"2024","journal-title":"Cosmetics"},{"key":"10.1016\/bs.enz.2024.06.004_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115771","article-title":"Computational methods to analyze and predict the binding mode of inhibitors targeting both human and mushroom tyrosinase","volume":"260","author":"Ricci","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib69","doi-asserted-by":"crossref","DOI":"10.1111\/pcmr.12951","article-title":"Human TYRP1: two functions for a single gene?","volume":"34","author":"Gautron","year":"2021","journal-title":"Pigment. Cell Melanoma Res."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib70","doi-asserted-by":"crossref","DOI":"10.1006\/jsbi.1997.3904","article-title":"Crystallization and preliminary X-ray analysis of human D-dopachrome tautomerase","volume":"120","author":"Sugimoto","year":"1997","journal-title":"J. Struct. Biol."},{"issue":"46","key":"10.1016\/bs.enz.2024.06.004_bib71","doi-asserted-by":"crossref","DOI":"10.1002\/anie.201708214","article-title":"The recent crystal structure of human tyrosinase related protein 1 (HsTYRP1) solves an old problem and poses a new one","volume":"56","author":"Decker","year":"2017","journal-title":"Angew. Chem.\u2014Int. Ed."},{"issue":"31","key":"10.1016\/bs.enz.2024.06.004_bib72","doi-asserted-by":"crossref","DOI":"10.2174\/0929867323666160627094938","article-title":"Melanogenesis inhibitors: strategies for searching for and evaluation of active compounds","volume":"23","author":"Gunia-Krzy\u017cak","year":"2016","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.004_bib73","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."},{"issue":"3","key":"10.1016\/bs.enz.2024.06.004_bib74","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19030690","article-title":"Structure-activity relationships of thiazolyl resorcinols, potent and selective inhibitors of human tyrosinase","volume":"19","author":"Mann","year":"2018","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.004_bib75","doi-asserted-by":"crossref","DOI":"10.1055\/s-2000-11113","article-title":"Inhibition of tyrosinase by flavonoids, stilbenes and related 4- substituted resorcinols: structure-activity investigations","volume":"66","author":"Shimizu","year":"2000","journal-title":"Planta Med."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.004_bib76","doi-asserted-by":"crossref","DOI":"10.1016\/j.jid.2019.02.013","article-title":"Effective tyrosinase inhibition by thiamidol results in significant improvement of mild to moderate melasma","volume":"139","author":"Arrowitz","year":"2019","journal-title":"J. Invest. Dermatol."}],"container-title":["The Enzymes","Tyrosinase"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604724000210?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604724000210?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,9,19]],"date-time":"2024-09-19T03:52:23Z","timestamp":1726717943000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604724000210"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"ISBN":["9780443295201"],"references-count":75,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2024.06.004","relation":{},"ISSN":["1874-6047"],"issn-type":[{"value":"1874-6047","type":"print"}],"subject":[],"published":{"date-parts":[[2024]]}}}