PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32271705-4 2020 The conversion of the phenols by tyrosinase to quinones is the rate-limiting step in the biochemical manufacture of melanin. Quinones 47-55 tyrosinase Homo sapiens 33-43 2846069-1 1988 Tyrosinase usually catalyzes the conversion of monophenols to o-diphenols and the oxidation of o-diphenols to the corresponding quinones. Quinones 128-136 tyrosinase Homo sapiens 0-10 2869525-2 1985 In vertebrates tyrosinase is present only in specialized cells (melanocytes), where it catalyses the oxidation of tyrosine and certain diphenolic intermediate products to quinones which polymerize to give rise to melanin. Quinones 171-179 tyrosinase Homo sapiens 15-25 6173137-0 1981 Inhibition of reverse transcriptase by tyrosinase generated quinones related to levodopa and dopamine. Quinones 60-68 tyrosinase Homo sapiens 39-49 3136917-10 1988 Spectrophotometric data indicated that Compounds 1 and 2 were oxidized by tyrosinase to quinones. Quinones 88-96 tyrosinase Homo sapiens 74-84 29374432-3 2017 Of these, only tyrosinase has two activities: (1) oxygenase activity to hydroxylate monophenols to ortho-diphenols and (2) oxidase activity responsible for further oxidation of ortho-diphenols to ortho-quinones. Quinones 202-210 tyrosinase Homo sapiens 15-25 29345904-2 2018 Specifically, the strategy was illustrated by using a model quinones-generating oxidase of tyrosinase (Tyr) to catalytically produce 1,2-bezoquinone or its derivative, which can easily and selectively be conjugated onto the surface of the chitosan deposited PbS/NiO/FTO photocathode via the QCCC. Quinones 60-68 tyrosinase Homo sapiens 91-101 29345904-2 2018 Specifically, the strategy was illustrated by using a model quinones-generating oxidase of tyrosinase (Tyr) to catalytically produce 1,2-bezoquinone or its derivative, which can easily and selectively be conjugated onto the surface of the chitosan deposited PbS/NiO/FTO photocathode via the QCCC. Quinones 60-68 tyrosinase Homo sapiens 103-106 25130058-7 2014 These results support the notion that the melanocyte toxicity of RD depends on its tyrosinase-catalyzed conversion to toxic quinones and the concomitant production of reactive oxygen species. Quinones 124-132 tyrosinase Homo sapiens 83-93 25713930-2 2015 To explore the mechanism underlying that effect, we previously showed that oxidation of RD with mushroom tyrosinase produces RD-quinone, which is converted to secondary quinone products, and we suggested that those quinones are cytotoxic because they bind to cellular proteins and produce reactive oxygen species. Quinones 215-223 tyrosinase Homo sapiens 105-115 26821466-5 2015 Tyrosinase-mediated oxidation of these chemicals yields toxic ortho-quinones which bind to cellular proteins and produce reactive oxygen species. Quinones 68-76 tyrosinase Homo sapiens 0-10 21458432-12 2011 Although, as controls, 4-hydroxyanisole and L-tyrosine were metabolized by tyrosinase to form quinones and glutathione conjugates, they exhibited no GST inhibition in the absence and presence of tyrosinase. Quinones 94-102 tyrosinase Homo sapiens 75-85 23252650-4 2013 Similarly, the effective quenching of the AgNCs by quinones enabled the detection of tyrosinase through the biocatalyzed oxidation of tyrosine, dopamine, or tyramine to the respective quinone products. Quinones 51-59 tyrosinase Homo sapiens 85-95 20852777-4 2010 The entrapped tyrosinase could carry out enzyme-catalyzed oxidation of phenol to produce quinones, which subsequently quenched the fluorescence of QDs within hydrogel microarray. Quinones 89-97 tyrosinase Homo sapiens 14-24 21255087-2 2011 The melanocyte specificity is attributed to the tyrosinase-catalysed production of haptogenic ortho-quinones that covalently bind to tyrosinase or other melanosomal proteins to generate neo-antigens. Quinones 100-108 tyrosinase Homo sapiens 48-58 21255087-2 2011 The melanocyte specificity is attributed to the tyrosinase-catalysed production of haptogenic ortho-quinones that covalently bind to tyrosinase or other melanosomal proteins to generate neo-antigens. Quinones 100-108 tyrosinase Homo sapiens 133-143 15773923-3 2005 Whether tyrosinase is beneficial or detrimental to neurons is unclear; whilst the enzyme activity of tyrosinase generates dopamine-quinones and other oxidizing compounds, NM may form a sink for such radical species. Quinones 131-139 tyrosinase Homo sapiens 101-111 20460701-0 2010 Effects of tetrahydropterines on the generation of quinones catalyzed by tyrosinase. Quinones 51-59 tyrosinase Homo sapiens 73-83 18972140-1 2009 Tyrosinase catalyzes the ortho hydroxylation of monophenols and the subsequent oxidation of the diphenolic products to the resulting quinones. Quinones 133-141 tyrosinase Homo sapiens 0-10 17850508-5 2007 Such reactive quinones can be covalently bound to the catalytic centre of tyrosinase (haptenation). Quinones 14-22 tyrosinase Homo sapiens 74-84 17883274-0 2007 Tyrosinase-generated quinones induce covalent modification, unfolding, and aggregation of human holo-myoglobin. Quinones 21-29 tyrosinase Homo sapiens 0-10 16167833-0 2005 Tyrosinase-catalyzed oxidation of 17beta-estradiol: structure elucidation of the products formed beyond catechol estrogen quinones. Quinones 122-130 tyrosinase Homo sapiens 0-10 7626118-3 1995 Consequently, some of the observed inhibition of tyrosinase by azide can be explained by the reaction of enzymatically generated quinones with azide to form azido catechol. Quinones 129-137 tyrosinase Homo sapiens 49-59