{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T17:41:30Z","timestamp":1790876490066,"version":"4.1.0"},"reference-count":143,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2023,5,22]],"date-time":"2023-05-22T00:00:00Z","timestamp":1684713600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Tyrosinase is a copper-containing enzyme which is widely distributed in nature (e.g., bacteria, mammals, fungi) and involved in two consecutive steps of melanin biosynthesis. In humans, an excessive production of melanin can determine hyperpigmentation disorders as well as neurodegenerative processes in Parkinson\u2019s disease. The development of molecules able to inhibit the high activity of the enzyme remain a current topic in medicinal chemistry, because the inhibitors reported so far present several side effects. Heterocycle-bearing molecules are largely diffuse in this sense. Due to their importance as biologically active compounds, we decided to report a comprehensive review of synthetic tyrosinase inhibitors possessing heterocyclic moieties reported within the last five years. For the reader\u2019s convenience, we classified them as inhibitors of mushroom tyrosinase (Agaricus bisporus) and human tyrosinase.<\/jats:p>","DOI":"10.3390\/ijms24109097","type":"journal-article","created":{"date-parts":[[2023,5,23]],"date-time":"2023-05-23T03:20:06Z","timestamp":1684812006000},"page":"9097","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":36,"title":["Heterocyclic Compounds as Synthetic Tyrosinase Inhibitors: Recent Advances"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6092-5011","authenticated-orcid":false,"given":"Serena","family":"Vittorio","sequence":"first","affiliation":[{"name":"Dipartimento di Scienze Farmaceutiche, Universit\u00e0 degli Studi di Milano, Via Mangiagalli, 25, 20133 Milano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7440-4153","authenticated-orcid":false,"given":"Christian","family":"Dank","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry, University of Vienna, W\u00e4hringer Strasse 38, 1090 Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9976-0170","authenticated-orcid":false,"given":"Laura","family":"Ielo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Turin, Via P. Giuria 7, 10125 Torino, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,5,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Solano, F. (2018). On the metal cofactor in the tyrosinase family. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19020633"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1002\/pro.2734","article-title":"Structure\u2013Function correlations in tyrosinases","volume":"24","author":"Kanteev","year":"2015","journal-title":"Protein Sci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/s00702-023-02617-6","article-title":"The role of tyrosine hydroxylase as a key player in neuromelanin synthesis and the association of neuromelanin with Parkinson\u2019s disease","volume":"130","author":"Nagatsu","year":"2023","journal-title":"J. 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