PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
26881706-2	2016	In this pathway, Ty catalyzes the tyrosine monooxygenation into L-DOPA-quinone, which is the precursor of the skin pigment melanin.	dopaquinone	64-78	tyrosinase	Homo sapiens	17-19
26633377-1	2015	Tyrosinase catalyzes two distinct sequential reactions in melanin biosynthesis: The hydroxylation of tyrosine to dihydroxyphenylalanine (DOPA) and the oxidation of DOPA to dopaquinone.	dopaquinone	172-183	tyrosinase	Mus musculus	0-10
20481436-6	2010	The hydrolysis of (4) yields the tyrosine units that are oxidized by O(2)/tyrosinase to the respective dopaquinone product.	dopaquinone	103-114	tyrosinase	Homo sapiens	74-84
26544630-1	2015	Tyrosinase catalyzes two distinct sequential reactions in melanin biosynthesis: the hydroxylation of tyrosine to DOPA followed by the oxidation of DOPA to dopaquinone.	dopaquinone	155-166	tyrosinase	Mus musculus	0-10
26440479-4	2015	When the dopamine moiety in Dopa-CQDs conjugate was oxidized to a dopaquinone derivative under specific catalysis of TYR, an intraparticle photoinduced electron transfer (PET) process between CQDs and dopaquinone moiety took place, and then the fluorescence of the conjugate could be quenched simultaneously.	dopaquinone	66-77	tyrosinase	Homo sapiens	117-120
26440479-4	2015	When the dopamine moiety in Dopa-CQDs conjugate was oxidized to a dopaquinone derivative under specific catalysis of TYR, an intraparticle photoinduced electron transfer (PET) process between CQDs and dopaquinone moiety took place, and then the fluorescence of the conjugate could be quenched simultaneously.	dopaquinone	201-212	tyrosinase	Homo sapiens	117-120
21054558-3	2011	In human skin melanocytes, the cellular tyrosinase inhibition was examined by the conversion of l-tyrosine and oxidation of l-DOPA to dopaquinone.	dopaquinone	134-145	tyrosinase	Homo sapiens	40-50
21048351-5	2010	Tyrosinase is the enzyme that oxidizes tyrosine to DOPA and further oxidizes DOPA to the melanin precursor dopaquinone.	dopaquinone	107-118	tyrosinase	Homo sapiens	0-10
20141169-12	2010	However, Grx was inactivated in a time- and concentration-dependent fashion indicative of irreversible adduction of dopaquinone to its nucleophilic active-site Cys-22, consistent with the intracellular loss of Grx activity but not Grx protein content after l-DOPA treatment.	dopaquinone	116-127	glutaredoxin	Homo sapiens	9-12
22110954-1	2010	Tyrosinase is a bifunctional enzyme which oxidizes the initial step of melanin biosynthesis, that is, conversion of tyrosine to dopa and subsequently dopa to dopaquinone.	dopaquinone	158-169	tyrosinase	Mus musculus	0-10
20055419-3	2010	Tyrosinase catalyzes the conversion of dopamine to o-dopaquinone, and the reduction of o-dopaquinone, which requires a low potential difference, was detected electrochemically.	dopaquinone	51-64	tyrosinase	Rattus norvegicus	0-10
20055419-3	2010	Tyrosinase catalyzes the conversion of dopamine to o-dopaquinone, and the reduction of o-dopaquinone, which requires a low potential difference, was detected electrochemically.	dopaquinone	87-100	tyrosinase	Rattus norvegicus	0-10
20083145-5	2010	In this study, we developed a novel technology for the production of l-DOPA, an electroenzymatic synthesis with a tyrosinase-immobilized cathode under the reduction potential of DOPAquinone, which is -530 mV.	dopaquinone	178-189	tyrosinase	Homo sapiens	114-124
18324837-3	2008	Oxidation of the capping layer by TR/O2 yields the respective L-DOPA and dopaquinone products.	dopaquinone	73-84	tyrosinase	Homo sapiens	34-36
19270393-5	2009	Additionally, the incubation of SH in mushroom tyrosinase inhibited the oxidation of l-dopa to o-dopaquinone, which implies that SH is a potent tyrosinase inhibitor.	dopaquinone	95-108	tyrosinase	Mus musculus	47-57
19270393-5	2009	Additionally, the incubation of SH in mushroom tyrosinase inhibited the oxidation of l-dopa to o-dopaquinone, which implies that SH is a potent tyrosinase inhibitor.	dopaquinone	95-108	tyrosinase	Mus musculus	144-154
19007228-1	2008	Tyrosinase catalyzes the biological conversion of tyrosine to dopaquinone with dioxygen at the dinuclear copper active site under physiological conditions.	dopaquinone	62-73	tyrosinase	Homo sapiens	0-10
16841367-3	2006	Tyrosinase catalyses three different reactions in the biosynthetic pathway of melanin in melanocytes: the hydroxylation of tyrosine to l-DOPA and the oxidation of l-DOPA to dopaquinone; furthermore, in humans, dopaquinone is converted by a series of complex reactions to melanin.	dopaquinone	173-184	tyrosinase	Homo sapiens	0-10
17567175-2	2007	Upon oxidation of the surface to dopaquinone as a result of tyrosinase activity, force interactions are switched "OFF".	dopaquinone	33-44	tyrosinase	Homo sapiens	60-70
17685382-5	2007	The TR-induced oxidation of the tyramine- or 1-functionalized ISFETs resulted in the formation of the redox-active dopaquinone units.	dopaquinone	115-126	tyrosinase	Homo sapiens	4-6
17685382-6	2007	The control of the gate potential by the redox-active dopaquinone units allowed a quantitative assay of TR to be performed.	dopaquinone	54-65	tyrosinase	Homo sapiens	104-106
16841367-3	2006	Tyrosinase catalyses three different reactions in the biosynthetic pathway of melanin in melanocytes: the hydroxylation of tyrosine to l-DOPA and the oxidation of l-DOPA to dopaquinone; furthermore, in humans, dopaquinone is converted by a series of complex reactions to melanin.	dopaquinone	210-221	tyrosinase	Homo sapiens	0-10
15778083-1	2005	The tyrosinase/oxygen enzymatic system catalyses the orthohydroxylation of L-tyrosine to L-dopa and the oxidation of this to dopaquinone, which evolves non-enzymatically towards to form melanins.	dopaquinone	125-136	tyrosinase	Homo sapiens	4-14
16445854-2	2006	Tyrosinase, the primary enzyme in melanin synthesis commonly mutated in albinism, oxidizes l-tyrosine to l-dopaquinone using l-3,4-dihydroxyphenylalanine (L-DOPA) as an intermediate product.	dopaquinone	105-118	tyrosinase	Homo sapiens	0-10
16442796-3	2006	Tyrosinase is a key enzyme involved in the first stage of melanin synthesis, catalyzing the transformation of tyrosine to l-dopaquinone.	dopaquinone	122-135	tyrosinase	Homo sapiens	0-10
16392817-1	2006	Tyrosinase is a copper-dependent enzyme which converts l- tyrosine to dopaquinone and is involved in different biological processes such as melanogenesis and skin hyperpigmentation.	dopaquinone	70-81	tyrosinase	Homo sapiens	0-10
12878190-1	2003	Synthesis of melanin starts from the conversion of L-tyrosine to 3,4-dihydroxyphenylalanine (L-dopa) and then the oxidation of L-dopa yields dopaquinone by tyrosinase.	dopaquinone	141-152	tyrosinase	Mus musculus	156-166
16046863-6	2005	Finally, the intracellular tyrosine concentration was lowered by overexpression of tyrosinase converting tyrosine to dopaquinone.	dopaquinone	117-128	tyrosinase	Homo sapiens	83-93
12755639-1	2003	Tyrosinase oxidizes tyrosine to dopaquinone, which undergoes nonenzymatic reactions leading to precursors of melanin pigments.	dopaquinone	32-43	tyrosinase	Homo sapiens	0-10
12755639-4	2003	Using a combination of enzyme oximetry, pulse radiolysis, and chemical oxidation, the study of structurally modified dopaquinones provides firm evidence of nonenzymatic catechol formation during tyrosinase oxidation of phenols and reveals significant differences in their modes of reaction.	dopaquinone	117-129	tyrosinase	Homo sapiens	195-205
12180986-0	2002	Redox reaction between amino-(3,4-dihydroxyphenyl)methyl phosphonic acid and dopaquinone is responsible for the apparent inhibitory effect on tyrosinase.	dopaquinone	77-88	tyrosinase	Homo sapiens	142-152
11171088-2	2001	Tyrosinase catalyses the rate-limiting generation of L-dopaquinone from L-tyrosine and is also able to oxidize L-dopa to L-dopaquinone.	dopaquinone	53-66	tyrosinase	Homo sapiens	0-10
11744399-5	2001	This is consistent with the dopa detected during melanogenesis catalysed by tyrosinase being formed indirectly by a combination of dopaquinone intramolecular reductive addition to form leucodopachrome (cyclodopa), followed by redox exchange between remaining dopaquinone and leucodopachrome.	dopaquinone	131-142	tyrosinase	Homo sapiens	76-86
11744399-5	2001	This is consistent with the dopa detected during melanogenesis catalysed by tyrosinase being formed indirectly by a combination of dopaquinone intramolecular reductive addition to form leucodopachrome (cyclodopa), followed by redox exchange between remaining dopaquinone and leucodopachrome.	dopaquinone	259-270	tyrosinase	Homo sapiens	76-86
12069489-4	2002	In 1993, Ito proposed that melanogenic switching is due to the covalent binding of the intermediate DOPAquinone to the enzyme glutathione reductase.	dopaquinone	100-111	glutathione-disulfide reductase	Homo sapiens	126-147
12444326-3	2002	However, it is now believed that tyrosinase is responsible for the conversion of tyrosine to dopa and of dopa to dopaquinone, and that peroxidase accomplishes the oxidative polymerization of the eventually formed indoles to eumelanin pigments.	dopaquinone	113-124	tyrosinase	Homo sapiens	33-43
11171088-2	2001	Tyrosinase catalyses the rate-limiting generation of L-dopaquinone from L-tyrosine and is also able to oxidize L-dopa to L-dopaquinone.	dopaquinone	121-134	tyrosinase	Homo sapiens	0-10
8819121-9	1996	Our data clearly indicate that 5-S-CD is formed in human melanoma cells by a tyrosinase-dependent mechanism involving the addition of CysH to dopaquinone.	dopaquinone	142-153	tyrosinase	Homo sapiens	77-87
11041367-11	2000	Because of the absence of TRP-1 and TRP-2 in pheomelanogenesis, it may be suggested that tyrosinase is involved in lysosomal degradation after forming dopaquinone, to which the cysteine present in the lysosomal granule binds to form cysteinyldopas that will then be auto-oxidized to become pheomelanin.	dopaquinone	151-162	tyrosinase	Homo sapiens	89-99
10952395-1	2000	Eumelanogenesis and phaeomelanogenesis diverge at an early stage in pigment formation, namely at the point where dopaquinone, the initial product of tyrosine oxidation by tyrosinase, undergoes one of two types of reaction: either (1) a reductive endocyclisation in which a Michael addition of the side-chain amino group takes place; or (2) a reductive addition of cysteine to give cysteinyldopa.	dopaquinone	113-124	tyrosinase	Homo sapiens	171-181
10952395-5	2000	We have examined quantitatively the role of dopaquinone in the non-enzymatic oxidation of 5-S-cysteinyldopa using pulse radiolysis and have demonstrated that the redox exchange reaction between dopaquinone and 5-S-cysteinyldopa occurs spontaneously with a rate constant of 8.8 x 10(5) M(-1) sec(-1).	dopaquinone	194-205	secretory blood group 1, pseudogene	Homo sapiens	291-297
10952395-6	2000	This study has also enabled an improved estimate of < or = 4 x 10(7) M(-1) sec(-1) to be obtained for the rate constant of the reaction of dopaquinone with cyclodopa.	dopaquinone	142-153	secretory blood group 1, pseudogene	Homo sapiens	78-84
10506262-3	1999	Within the melanocyte, tyrosine is converted to dopa, and then dopaquinone via the bifunctional enzyme tyrosinase.	dopaquinone	63-74	tyrosinase	Homo sapiens	103-113
8610070-2	1995	The melanin-affinic properties are apparently due to binding to intermediates, preferably dopaquinone, produced in the melanin synthetic pathway by tyrosinase-catalysed oxidation of tyrosine.	dopaquinone	90-101	tyrosinase	Mus musculus	148-158
8433004-7	1993	When tyrosinase activity is low, dopaquinone, a reactive intermediate in melanogenesis, is quantitatively converted to glutathionyldopa, which gives rise exclusively to pheomelanin.	dopaquinone	33-44	tyrosinase	Homo sapiens	5-15
7659677-6	1995	The different extent of inhibition is shown to reflect i) the ability of the two monomers to compete with tyrosinase substrates for the enzyme"s active center and ii) the rate of interaction between melanin monomers and DOPAquinone.	dopaquinone	220-231	tyrosinase	Homo sapiens	106-116
8064113-2	1994	The assay measures the pink pigment formed by the reaction of Besthorn"s hydrazone (3-methyl-2-benzothiazoninone hydrazone, or MBTH) with dopaquinone, the product of oxidation of L-dopa by tyrosinase.	dopaquinone	138-149	tyrosinase	Homo sapiens	189-199
18965738-2	1993	The method involves the conversion of tyrosine into dopaquinone by reaction of tyrosinase, followed by derivation of the dopaquinone with fluorogenic agent 1,2-diphenylethylenediamine.	dopaquinone	52-63	tyrosinase	Homo sapiens	79-89
8433004-8	1993	When tyrosinase activity is high, an excess of dopaquinone is produced, which results in the inactivation of glutathione reductase and gamma-glutamyl transpeptidase, enzymes essential for pheomelanogenesis.	dopaquinone	47-58	tyrosinase	Homo sapiens	5-15
8433004-8	1993	When tyrosinase activity is high, an excess of dopaquinone is produced, which results in the inactivation of glutathione reductase and gamma-glutamyl transpeptidase, enzymes essential for pheomelanogenesis.	dopaquinone	47-58	glutathione-disulfide reductase	Homo sapiens	109-130
8433004-8	1993	When tyrosinase activity is high, an excess of dopaquinone is produced, which results in the inactivation of glutathione reductase and gamma-glutamyl transpeptidase, enzymes essential for pheomelanogenesis.	dopaquinone	47-58	inactive glutathione hydrolase 2	Homo sapiens	135-164
1429711-1	1992	Tyrosinase (EC 1.14.18.1) is a copper-containing metalloglycoprotein that catalyzes several steps in the melanin pigment biosynthetic pathway; the hydroxylation of tyrosine to L-3,4-dihydroxyphenylalanine (dopa) and the subsequent oxidation of dopa to dopaquinone.	dopaquinone	252-263	tyrosinase	Homo sapiens	0-10
8440890-4	1993	The enzyme tyrosinase is a product of the C locus and catalyzes the conversion of tyrosine to dopa and the following reaction (dopa to dopaquinone).	dopaquinone	135-146	tyrosinase	Ovis aries	11-21
1445949-1	1992	The oxidation of 3,4-dihydroxyphenylalanine (dopa) by O2 catalyzed by tyrosinase yields 4-(2-carboxy-2-aminoethyl)-1,2-benzoquinone, with its amino group protonated (o-dopaquinone-H+).	dopaquinone	88-131	tyrosinase	Homo sapiens	70-80
1445949-1	1992	The oxidation of 3,4-dihydroxyphenylalanine (dopa) by O2 catalyzed by tyrosinase yields 4-(2-carboxy-2-aminoethyl)-1,2-benzoquinone, with its amino group protonated (o-dopaquinone-H+).	dopaquinone	166-179	tyrosinase	Homo sapiens	70-80
1953749-1	1991	The early enzyme-mediated reaction sequence in the biosynthesis of melanin from L-tyrosine involves an initial hydroxylation (monophenol oxidase activity, MPO) of the aromatic amino acid precursor to form L-dopa (3,4-dihydroxyphenylalanine), and the ensuing oxidation (diphenol oxidase activity, DPO) of the resultant diphenol to form dopaquinone.	dopaquinone	335-346	Prophenoloxidase 1	Drosophila melanogaster	126-144
33804376-1	2021	Tyrosinase is a copper-containing monooxygenase catalyzing the O-hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine then to dopaquinone that is profoundly involved in melanin synthesis in eukaryotes.	dopaquinone	129-140	tyrosinase	Homo sapiens	0-10
1900435-2	1991	Tyrosinase catalyzes the oxidation by molecular oxygen of L-dopa to o-dopaquinone, which evolves non-enzymatically through a branched pathway with cyclization or hydroxylation reactions.	dopaquinone	68-81	tyrosinase	Homo sapiens	0-10
1898730-4	1991	By use of immune affinity purification protocols, we have isolated the proteins encoded by the brown and albino loci and have determined that both have the catalytic functions ascribed to tyrosinase, i.e. hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine (DOPA) and the oxidation of DOPA to DOPAquinone.	dopaquinone	297-308	tyrosinase	Mus musculus	188-198
2124140-8	1990	These results suggest that selective TU incorporation in pigmented melanomas and other melanin-producing systems is due to the covalent binding to dopaquinone, produced by tyrosinase catalyzed oxidation of tyrosine.	dopaquinone	147-158	tyrosinase	Homo sapiens	172-182
34757293-4	2021	The congener proteins treated with tyrosinase convert 3, 4-dihydroxy-l-phenylalanine to dopaquinone for strain-promoted click chemistry.	dopaquinone	88-99	tyrosinase	Homo sapiens	35-45
2938636-2	1986	The nature of the covalent binding was studied with dopaquinone formed on tyrosinase oxidation of 3,4-dihydroxyphenylalanine (DOPA).	dopaquinone	52-63	tyrosinase	Homo sapiens	74-84
2515217-5	1989	Furthermore, the accuracy is also enhanced by the proposed modifications, since all reactions from dopaquinone are standardized, and the assay becomes only dependent on the tyrosinase activity.	dopaquinone	99-110	tyrosinase	Homo sapiens	173-183
2903772-3	1988	(a) The reaction of the thiol groups with dopaquinone after the tyrosinase-catalyzed oxidation of tyrosine and dopa.	dopaquinone	42-53	tyrosinase	Homo sapiens	64-74
34474817-4	2021	Introducing amino groups through aminolysis and inducing dopaquinones by tyrosinase can take part in the Michael additions to cause the adhesion.	dopaquinone	57-69	tyrosinase	Homo sapiens	73-83
34439449-8	2021	Experiments using mushroom TYR suggest that L-cysteinamide at certain concentrations can inhibit eumelanin synthesis through a dual mechanism by inhibiting TYR-catalyzed dopaquinone synthesis and by diverting the synthesized dopaquinone to the formation of DOPA-cysteinamide conjugates rather than dopachrome.	dopaquinone	170-181	tyrosinase	Homo sapiens	156-159
34439449-8	2021	Experiments using mushroom TYR suggest that L-cysteinamide at certain concentrations can inhibit eumelanin synthesis through a dual mechanism by inhibiting TYR-catalyzed dopaquinone synthesis and by diverting the synthesized dopaquinone to the formation of DOPA-cysteinamide conjugates rather than dopachrome.	dopaquinone	225-236	tyrosinase	Homo sapiens	27-30
34088368-5	2021	Mechanically, the tyrosine groups on the surface of ECDY can be specifically recognized by tyrosinase and further converted into dopaquinone, which consequently causes the intramolecular fluorescence quenching of the probe through photoinduced electron transfer (PET).	dopaquinone	129-140	tyrosinase	Mus musculus	91-101
35456994-4	2022	The synthesis of human NM is regarded to be similar to that of melanin in melanocytes; melanin synthesis in skin is via DOPAquinone (DQ) by tyrosinase, whereas NM synthesis in DA neurons is via DAquinone (DAQ) by tyrosine hydroxylase (TH) and aromatic L-amino acid decarboxylase (AADC).	dopaquinone	120-131	tyrosinase	Homo sapiens	140-150
3927772-3	1985	Final absorbance change reflects probably two activities of tyrosinase: the oxidation of dopa to dopaquinone and the conversion of 5,6-dihydroxyindole to melanochrome.	dopaquinone	97-108	tyrosinase	Homo sapiens	60-70
3103358-4	1986	The oxidation of 5-S-glutathionyldopa by dopaquinone, formed by the action of human tyrosinase and mushroom tyrosinase, is considerably slower than that of 5-S-cysteinyldopa.	dopaquinone	41-52	tyrosinase	Homo sapiens	84-118
3103358-5	1986	The higher oxidation potential of 5-S-glutathionyldopa, and/or the greater number of dopaquinone molecules necessary for pigment formation from 5-S-glutathionyldopa and/or the formation of tyrosinase-inhibiting products from 5-S-glutathionyldopa can explain the slower oxidation of this compound.	dopaquinone	85-96	tyrosinase	Homo sapiens	189-199
30996775-6	2019	Overall, the study showed the possibility that L-DOPA-quinone stabilizes GIRK in a preopen conformation through formation of a covalent adduct with cysteine-65 on the GIRK2 subunit of the protein.	dopaquinone	47-61	potassium inwardly rectifying channel subfamily J member 6	Homo sapiens	167-172
6413271-2	1983	The initial steps are the conversion of tyrosine to dihydroxyphenylalanine (dopa) and of dopa to dopaquinone by the enzyme tyrosinase (EC 1.10.3.1).	dopaquinone	97-108	tyrosinase	Mus musculus	123-133
6776205-3	1980	Tyrosinase inactivation also occurred when ascorbic acid was added to the reaction system; in which dopaquinone, an oxidation product of dopa which is immediately converted back to dopa by ascorbic acid thus preventing melanin formation.	dopaquinone	100-111	tyrosinase	Mus musculus	0-10
211676-2	1978	The inactivation similarly occurred in the dopa-tyrosinase reaction system containing ascorbic aicd, although in the presence of ascorbic acid the dopa-quinone is immediately converted back to dopa and therefore melanin formation does not take place.	dopaquinone	147-159	tyrosinase	Mus musculus	48-58
33308130-3	2021	Melanin synthesis starts via the hydroxylation of L-tyrosine to L-3,4-dihydroxyphenylalanine (DOPA) catalyzed by the enzyme known as tyrosinase (TYR), which triggers further conversion reaction to DOPAquinone and then to DOPAchrome.	dopaquinone	197-208	tyrosinase	Homo sapiens	133-143
33308130-3	2021	Melanin synthesis starts via the hydroxylation of L-tyrosine to L-3,4-dihydroxyphenylalanine (DOPA) catalyzed by the enzyme known as tyrosinase (TYR), which triggers further conversion reaction to DOPAquinone and then to DOPAchrome.	dopaquinone	197-208	tyrosinase	Homo sapiens	145-148
32776353-1	2021	Tyrosinase starts melanogenesis and determines its course, catalysing the oxidation by molecular oxygen of tyrosine to dopa, and that of dopa to dopaquinone.	dopaquinone	145-156	tyrosinase	Homo sapiens	0-10
31297616-5	2019	Tyrosinase catalyzes the oxidation of dopamine to form dopaquinone which reduces the fluorescence of the N-GQDs through a dynamic quenching process.	dopaquinone	55-66	tyrosinase	Homo sapiens	0-10
30907884-8	2019	In melanogenesis, tyrosinase catalyzes the rate-limiting step that converts L-tyrosine into 3,4-dihydroxyphenylalanine (L-DOPA) and then into dopaquinone.	dopaquinone	142-153	tyrosinase	Homo sapiens	18-28
30579605-3	2019	Tyrosinase, a copper-containing protein, is the rate-limiting enzyme in melanin biosynthesis and first catalyzes the hydroxylation of l-tyrosine to 3,4-dihydroxyphenylalanine (DOPA) and the further oxidization to dopaquinone.	dopaquinone	213-224	tyrosinase	Mus musculus	0-10
6433900-3	1984	With this method, it is demonstrated that mushroom tyrosinase can catalyse hydroxylation of tyrosine residues in proteins to dopa and subsequent oxidation to dopaquinone residues.	dopaquinone	158-169	tyrosinase	Bos taurus	51-61
6433900-4	1984	The dopaquinone residues in proteins combine with cysteine residues to form 5-S-cysteinyldopa in bovine serum albumin and yeast alcohol dehydrogenase, whereas dopa is the major product in bovine insulin, which lacks cysteine residues.	dopaquinone	4-15	insulin	Bos taurus	195-202
30907884-10	2019	In cultured melanocytes, tyrosinase activity can be quantified by adding L-DOPA as a substrate and measuring dopaquinone production by spectrophotometry.	dopaquinone	109-120	tyrosinase	Homo sapiens	25-35
30411752-2	2019	The bioprobe (named CDs-TYR) can catalyze oxidation of dopamine and produce dopaquinone, and consequently the fluorescence of the CDs was quenched due to an efficient electron transfer mechanism from excited CDs to dopaquinone.	dopaquinone	76-87	tyrosinase	Homo sapiens	24-27
30411752-2	2019	The bioprobe (named CDs-TYR) can catalyze oxidation of dopamine and produce dopaquinone, and consequently the fluorescence of the CDs was quenched due to an efficient electron transfer mechanism from excited CDs to dopaquinone.	dopaquinone	215-226	tyrosinase	Homo sapiens	24-27
29190472-6	2018	Subsequently, this DECDs-AuNPs platform is further taken advantage to assess TYR activity by the aid of TYR"s capability for oxidation of DA into dopaquinone, which will not induce the agglomeration of AuNPs, so the fluorescence quenching of DECDs is associated with TYR activity.	dopaquinone	146-157	tyrosinase	Homo sapiens	77-80
30449837-5	2019	Peptides were effectively immobilized onto the AuNPs depending on the presence of tyrosine within the sequence, which suggests the DOPA-quinone produced from tyrosine, via tyrosinase, is connected to the chitosan amino group.	dopaquinone	131-143	tyrosinase	Homo sapiens	172-182
30246912-2	2018	Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa-moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers.	dopaquinone	78-90	tyrosinase	Homo sapiens	33-43
29223142-3	2018	Tyrosinase is a key enzyme in melanin synthesis, which regulates the rate-limiting step during conversion of tyrosine into DOPA and dopaquinone.	dopaquinone	132-143	tyrosinase	Homo sapiens	0-10
29190472-6	2018	Subsequently, this DECDs-AuNPs platform is further taken advantage to assess TYR activity by the aid of TYR"s capability for oxidation of DA into dopaquinone, which will not induce the agglomeration of AuNPs, so the fluorescence quenching of DECDs is associated with TYR activity.	dopaquinone	146-157	tyrosinase	Homo sapiens	104-107
29190472-6	2018	Subsequently, this DECDs-AuNPs platform is further taken advantage to assess TYR activity by the aid of TYR"s capability for oxidation of DA into dopaquinone, which will not induce the agglomeration of AuNPs, so the fluorescence quenching of DECDs is associated with TYR activity.	dopaquinone	146-157	tyrosinase	Homo sapiens	104-107
29283382-3	2017	Tyrosinase catalyses two successive oxidations in melanin biosynthesis: the conversions of tyrosine to dihydroxyphenylalanine (DOPA) and DOPA to dopaquinone.	dopaquinone	145-156	tyrosinase	Homo sapiens	0-10
29149994-2	2018	Tyrosine could be catalyzed by TYR to generate dopaquinone, which could efficiently quench the fluorescence of N-GQDs, and the degree of fluorescence quenching of N-GQDs was proportional to the concentration of TYR.	dopaquinone	47-58	tyrosinase	Homo sapiens	31-34
29149994-2	2018	Tyrosine could be catalyzed by TYR to generate dopaquinone, which could efficiently quench the fluorescence of N-GQDs, and the degree of fluorescence quenching of N-GQDs was proportional to the concentration of TYR.	dopaquinone	47-58	tyrosinase	Homo sapiens	211-214
28842016-4	2017	However, in the presence of TYR, DA could be oxidized to dopaquinone, which inhibited the reduction of oxTMB by DA, resulting in a blue color recovery and an increase of the absorbance at 652nm.	dopaquinone	57-68	tyrosinase	Homo sapiens	28-31
29126486-5	2017	When TYR was mixed with CODs-Dopa, the dopamine moiety in CQDs-Dopa conjugate was oxidized to O-dopaquinone, and an intra-particle photo-induced electron transfer (PET) process consequently occurred between CQDs and O-dopaquinone to quench the fluorescence of CQDs-Dopa.	dopaquinone	94-107	tyrosinase	Homo sapiens	5-8
29126486-5	2017	When TYR was mixed with CODs-Dopa, the dopamine moiety in CQDs-Dopa conjugate was oxidized to O-dopaquinone, and an intra-particle photo-induced electron transfer (PET) process consequently occurred between CQDs and O-dopaquinone to quench the fluorescence of CQDs-Dopa.	dopaquinone	216-229	tyrosinase	Homo sapiens	5-8
28902505-8	2017	Aggregation of the caddie protein, which is triggered by the conversion of the Tyr98 residue to dopaquinone, may ensure the generation of fully activated tyrosinase.	dopaquinone	96-107	tyrosinase	Homo sapiens	154-164
27711193-1	2016	Hydroxylation of L-tyrosine to 3,4-dihydroxyphenylalanine (L-DOPA) by immobilized tyrosinase in the presence of ascorbic acid (AH2), which reduces DOPA-quinone to L-DOPA, is characterized by low reaction yields that are mainly caused by the suicide inactivation of tyrosinase by L-DOPA and AH2.	dopaquinone	147-159	tyrosinase	Homo sapiens	82-92
27711193-1	2016	Hydroxylation of L-tyrosine to 3,4-dihydroxyphenylalanine (L-DOPA) by immobilized tyrosinase in the presence of ascorbic acid (AH2), which reduces DOPA-quinone to L-DOPA, is characterized by low reaction yields that are mainly caused by the suicide inactivation of tyrosinase by L-DOPA and AH2.	dopaquinone	147-159	zinc finger RANBP2-type containing 3	Homo sapiens	127-130
27711193-1	2016	Hydroxylation of L-tyrosine to 3,4-dihydroxyphenylalanine (L-DOPA) by immobilized tyrosinase in the presence of ascorbic acid (AH2), which reduces DOPA-quinone to L-DOPA, is characterized by low reaction yields that are mainly caused by the suicide inactivation of tyrosinase by L-DOPA and AH2.	dopaquinone	147-159	tyrosinase	Homo sapiens	265-275
27711193-1	2016	Hydroxylation of L-tyrosine to 3,4-dihydroxyphenylalanine (L-DOPA) by immobilized tyrosinase in the presence of ascorbic acid (AH2), which reduces DOPA-quinone to L-DOPA, is characterized by low reaction yields that are mainly caused by the suicide inactivation of tyrosinase by L-DOPA and AH2.	dopaquinone	147-159	zinc finger RANBP2-type containing 3	Homo sapiens	290-293
27657049-4	2016	Tyrosinase catalyzes the oxidation of tyrosine as well as dopa to dopaquinone.	dopaquinone	66-77	tyrosinase	Homo sapiens	0-10
26750991-2	2016	Tyrosinase, a type-3 copper protein, participates in two distinct reactions, hydroxylation of tyrosine to DOPA and conversion of DOPA to dopaquinone, in melanin biosynthesis.	dopaquinone	137-148	tyrosinase	Mus musculus	0-10
27448544-7	2016	This study discovers that Au/Ag NCs and dopaquinone can serve as a good electron acceptor and donor pair which results in an efficient intraparticle photoinduced electron transfer process, and also provides another alternative way for tyrosinase activity monitoring.	dopaquinone	40-51	tyrosinase	Homo sapiens	235-245