PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21123042-1 2011 This paper describes the preparation of a biomimetic Langmuir-Blodgett film of tyrosinase incorporated in a lipidic layer and the use of lutetium bisphthalocyanine as an electron mediator for the voltammetric detection of phenol derivatives, which include one monophenol (vanillic acid), two diphenols (catechol and caffeic acid) and two triphenols (gallic acid and pyrogallol). caffeic acid 316-328 tyrosinase Homo sapiens 79-89 21458432-11 2011 Caffeic acid, a hydrolyzed product of CAPE, showed a similar GST inhibition in the presence of tyrosinase. caffeic acid 0-12 tyrosinase Homo sapiens 95-105 21458432-13 2011 In conclusion, both CAPE and caffeic acid selectively inhibited GST in the presence of tyrosinase. caffeic acid 29-41 tyrosinase Homo sapiens 87-97 16325827-1 2006 The products of tyrosinase-catalyzed caffeic acid oxidation at pH 6.5 were investigated using high-performance liquid chromatography (HPLC) coupled to electrospray ionization mass spectrometry (ESI-MS). caffeic acid 37-49 tyrosinase Homo sapiens 16-26 17716620-2 2007 In the present study, we show that the polyphenols, (+)-catechin and caffeic acid, which contain a catechol moiety, inhibit tyrosinase-induced formation of 5-S-cysteinyl-dopamine via their capacity to undergo tyrosinase-induced oxidation to yield cysteinyl-polyphenol adducts. caffeic acid 69-81 tyrosinase Homo sapiens 124-134 17716620-2 2007 In the present study, we show that the polyphenols, (+)-catechin and caffeic acid, which contain a catechol moiety, inhibit tyrosinase-induced formation of 5-S-cysteinyl-dopamine via their capacity to undergo tyrosinase-induced oxidation to yield cysteinyl-polyphenol adducts. caffeic acid 69-81 tyrosinase Homo sapiens 209-219 30042336-1 2018 Caffeic acid derivatives represent promising lead compounds in the search for tyrosinase inhibitors to be used in the treatment of skin local hyperpigmentation associated to an overproduction or accumulation of melanin. caffeic acid 0-12 tyrosinase Homo sapiens 78-88 32625101-5 2020 In addition, coumaric acid- and caffeic acid-conjugated peptides suppressed tyrosinase activity more than arbutin, a known tyrosinase inhibitor. caffeic acid 32-44 tyrosinase Homo sapiens 76-86 32625101-5 2020 In addition, coumaric acid- and caffeic acid-conjugated peptides suppressed tyrosinase activity more than arbutin, a known tyrosinase inhibitor. caffeic acid 32-44 tyrosinase Homo sapiens 123-133 32337685-8 2020 Kinetic data showed that tyrosinase had the greatest substrate affnity to chlorogenic acid compared with its isomers and caffeic acid. caffeic acid 121-133 tyrosinase Homo sapiens 25-35 30063931-3 2018 However, 3-hydroxycinnamic, 4-hydroxycinnamic and 3,4-dihydroxycinnamic acids were seen to be substrates of tyrosinase at the same time. caffeic acid 50-77 tyrosinase Homo sapiens 108-118 30042336-2 2018 We recently reported the marked inhibitory activity of a conjugate of caffeic acid with dihydrolipoic acid, 2-S-lipoylcaffeic acid (LCA), on the tyrosine hydroxylase (TH) and dopa oxidase (DO) activities of mushroom tyrosinase. caffeic acid 70-82 tyrosinase Homo sapiens 216-226 28388092-5 2017 The kcat value of tyrosinase obtained for caffeic acid was higher than that obtained for p-coumaric acid, while the affinity was higher for p-coumaric acid. caffeic acid 42-54 tyrosinase Homo sapiens 18-28 29080822-0 2018 Action of tyrosinase on caffeic acid and its n-nonyl ester. caffeic acid 24-36 tyrosinase Homo sapiens 10-20 29080822-3 2018 The action of tyrosinase on caffeic acid and its n-nonyl ester (n-nonyl caffeate) was characterized kinetically in this work. caffeic acid 28-40 tyrosinase Homo sapiens 14-24 28012343-3 2017 To this purpose, we evaluated the capability of tyrosinase to oxidize a natural o-diphenol substrate to o-quinone analyzing the changes in the UV-Vis spectrum of a solution of caffeic acid and the reduction of the cathodic current in a tyrosinase-biosensor, respectively. caffeic acid 176-188 tyrosinase Homo sapiens 48-58