{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T06:26:30Z","timestamp":1790317590093,"version":"4.1.0"},"reference-count":59,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2019,6,3]],"date-time":"2019-06-03T00:00:00Z","timestamp":1559520000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000053","name":"National Eye Institute","doi-asserted-by":"publisher","award":["ZIA EY000476-10"],"award-info":[{"award-number":["ZIA EY000476-10"]}],"id":[{"id":"10.13039\/100000053","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Pigment Cell Melanoma Res"],"published-print":{"date-parts":[[2019,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Tyrosinases are melanocyte\u2010specific enzymes involved in melanin biosynthesis. Mutations in their genes cause oculocutaneous albinism associated with reduced or altered pigmentation of skin, hair, and eyes. Here, the recombinant human intra\u2010melanosomal domains of tyrosinase, TYRtr (19\u2013469), and tyrosinase\u2010related protein 1, TYRP1tr (25\u2013472), were studied in vitro to define their functional relationship. Proteins were expressed or coexpressed in whole <jats:italic>Trichoplusia ni<\/jats:italic> larvae and purified. Their associations were studied using gel filtration and sedimentation equilibrium methods. Protection of TYRtr was studied by measuring the kinetics of tyrosinase diphenol oxidase activity in the presence (1:1 and 1:20 molar ratios) or the absence of TYRP1tr for 10\u00a0hr under conditions mimicking melanosomal and ER pH values. Our data indicate that TYRtr incubation with excess TYRP1tr protects TYR, increasing its stability over time. However, this mechanism does not appear to involve the formation of stable hetero\u2010oligomeric complexes to maintain the protective function.<\/jats:p>","DOI":"10.1111\/pcmr.12791","type":"journal-article","created":{"date-parts":[[2019,5,11]],"date-time":"2019-05-11T16:13:22Z","timestamp":1557591202000},"page":"753-765","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["The TYRP1\u2010mediated protection of human tyrosinase activity does not involve stable interactions of tyrosinase domains"],"prefix":"10.1111","volume":"32","author":[{"given":"Monika B.","family":"Dolinska","sequence":"first","affiliation":[{"name":"National Eye Institute National Institutes of Health Bethesda Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul T.","family":"Wingfield","sequence":"additional","affiliation":[{"name":"National Institute of Arthritis and Musculoskeletal and Skin Diseases National Institutes of Health Bethesda Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"II","given":"Kenneth L.","family":"Young","sequence":"additional","affiliation":[{"name":"National Eye Institute National Institutes of Health Bethesda Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7204-6572","authenticated-orcid":false,"given":"Yuri V.","family":"Sergeev","sequence":"additional","affiliation":[{"name":"National Eye Institute National Institutes of Health Bethesda Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,6,3]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja404404h"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/srep32274"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/srep26570"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1993.1577"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M404444200"},{"key":"e_1_2_8_7_1","first-page":"48","volume-title":"Proteins, amino acids and peptides","author":"Cohn E. 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