PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
11535067-0	2001	The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in polycyclic aromatic hydrocarbon activation.	o-quinones	95-105	aldo-keto reductase family 1 member A1	Homo sapiens	35-41
11535067-2	2001	Human dihydrodiol dehydrogenase isoforms (AKR1C1-AKR1C4), members of the aldo-keto reductase (AKR) superfamily, activate trans-dihydrodiols by converting them to reactive and redox-active o-quinones.	o-quinones	188-198	aldo-keto reductase family 1 member C1	Homo sapiens	42-55
11535067-3	2001	We now show that the constitutively and widely expressed human AKR, aldehyde reductase (AKR1A1), will oxidize potent proximate carcinogen trans-dihydrodiols to their corresponding o-quinones.	o-quinones	180-190	aldo-keto reductase family 1 member A1	Homo sapiens	68-86
11535067-3	2001	We now show that the constitutively and widely expressed human AKR, aldehyde reductase (AKR1A1), will oxidize potent proximate carcinogen trans-dihydrodiols to their corresponding o-quinones.	o-quinones	180-190	aldo-keto reductase family 1 member A1	Homo sapiens	88-94
11060293-3	2001	Physiologically, AKR1C1 regulates progesterone action by converting the hormone into its inactive metabolite 20alpha-hydroxyprogesterone, and toxicologically this enzyme activates polycyclic aromatic hydrocarbon trans-dihydrodiols to redox-cycling o-quinones.	o-quinones	248-258	aldo-keto reductase family 1 member C1	Homo sapiens	17-23
11409947-8	2001	Both 2-hydroxy-8,9-dehydroestrone and 4-hydroxy-8,9-dehydroestrone were oxidized by tyrosinase or rat liver microsomes to o-quinones which reacted with GSH to give one mono-GSH conjugate and two di-GSH conjugates.	o-quinones	122-132	tyrosinase	Rattus norvegicus	84-94
11181039-1	2001	Recent studies have revealed that GSTM1 and M2 of the mu-class glutathione S-transferases catalyze a glutathione conjugate of catechol o-quinones including dopachrome, noradrenochrome, and adrenochrome under physiological conditions.	o-quinones	135-145	glutathione S-transferase mu 1	Homo sapiens	34-39
1337996-2	1992	A recent study of a range of alkoxy- and alkylthio-phenol analogues of tyrosine has shown that sulphur-containing compounds exhibit different behaviour to that of similar oxygen-containing compounds, indicating modified reactivities of their corresponding tyrosinase-induced o-quinones towards crucial cellular targets, in particular, thiols.	o-quinones	275-285	tyrosinase	Homo sapiens	256-266
10849837-1	2000	The production of L-DOPA using L-tyrosine as substrate, the enzyme tyrosinase (EC 1.14.18.1) as biocatalyst, and L-ascorbate as reducing agent for the o-quinones produced by the enzymatic oxidation of the substrates was studied.	o-quinones	151-161	tyrosinase	Homo sapiens	67-77
9671538-9	1998	In contrast, the endogenous catechol estrogens, 4-hydroxyestrone (4-OHE) and 2-hydroxyestrone (2-OHE), were without effect unless tyrosinase was present to convert the catechols to o-quinones.	o-quinones	181-191	tyrosinase	Equus caballus	130-140
8261447-1	1994	Dihydrodiol dehydrogenase (DD; EC 1.3.1.20) catalyzes a novel pathway of polycyclic aromatic hydrocarbon (PAH) metabolism in which trans-dihydrodiols (proximate carcinogens) are oxidized to reactive o-quinones which are cytotoxic and genotoxic.	o-quinones	199-209	dihydrodiol dehydrogenase	Rattus norvegicus	0-25
8261447-1	1994	Dihydrodiol dehydrogenase (DD; EC 1.3.1.20) catalyzes a novel pathway of polycyclic aromatic hydrocarbon (PAH) metabolism in which trans-dihydrodiols (proximate carcinogens) are oxidized to reactive o-quinones which are cytotoxic and genotoxic.	o-quinones	199-209	dihydrodiol dehydrogenase	Rattus norvegicus	27-29
11306097-2	2001	CYP1A1 or aldo-keto reductases (AKRs) from the 1C subfamily can further activate the trans-dihydrodiols by forming either anti-diol-epoxides or reactive and redox active o-quinones, respectively.	o-quinones	170-180	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	0-6
11306097-3	2001	To determine whether other AKR superfamily members can divert trans-dihydrodiols to o-quinones, the cDNA encoding human aldehyde reductase (AKR1A1) was isolated from hepatoma HepG2 cells using RT-PCR, subcloned into a prokaryotic expression vector, overexpressed in E. coli and purified to homogeneity in milligram amounts.	o-quinones	84-94	aldo-keto reductase family 1 member A1	Homo sapiens	120-138
11306097-3	2001	To determine whether other AKR superfamily members can divert trans-dihydrodiols to o-quinones, the cDNA encoding human aldehyde reductase (AKR1A1) was isolated from hepatoma HepG2 cells using RT-PCR, subcloned into a prokaryotic expression vector, overexpressed in E. coli and purified to homogeneity in milligram amounts.	o-quinones	84-94	aldo-keto reductase family 1 member A1	Homo sapiens	140-146
9578563-2	1998	Previous studies demonstrated that rat liver 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3 alpha-HSD/DD), a member of the aldo-keto reductase (AKR) superfamily, oxidizes PAH trans-dihydrodiols to redox-cycling o-quinones.	o-quinones	230-240	aldo-keto reductase family 1, member C14	Rattus norvegicus	45-81
9495812-1	1998	Rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase (3alpha-HSD/DD), a member of the aldo-keto reductase superfamily, inactivates circulating steroid hormones and may contribute to the carcinogenicity of polycyclic aromatic hydrocarbons (PAHs) by oxidizing trans-dihydrodiols to reactive o-quinones with the concomitant generation of reactive oxygen species.	o-quinones	294-304	aldo-keto reductase family 1, member C14	Rattus norvegicus	59-69
8885846-2	1996	A novel pathway of polycyclic aromatic hydrocarbon metabolism involves the oxidation of non-K-region trans-dihydrodiols to yield o-quinones, a reaction catalyzed by dihydrodiol dehydrogenase (DD).	o-quinones	129-139	dihydrodiol dehydrogenase	Rattus norvegicus	165-190
7710634-0	1995	Tyrosinase-mediated cytotoxicity of 4-substituted phenols: quantitative structure-thiol-reactivity relationships of the derived o-quinones.	o-quinones	128-138	tyrosinase	Homo sapiens	0-10
8297016-1	1993	We describe a convenient and sensitive assay of polyphenol oxidase (PPO, EC 1.14.18.1) consisting of spectrophotometry at 300 nm based on the stoichiometric reaction of cysteine with o-quinones produced during the enzymatic oxidation of phenols.	o-quinones	183-193	polyphenol oxidase, chloroplastic	Malus domestica	68-71
1963166-1	1990	Tyrosinase-dependent activation of hydroxybenzenes forms reactive compounds, including catechols and o-quinones, and some of which show antitumor activity against pigmented melanomas.	o-quinones	101-111	tyrosinase	Homo sapiens	0-10
1391625-1	1992	Dihydrodiol dehydrogenase (DD; EC 1.3.1.20) can suppress the formation of anti-diol epoxides that arise from the metabolic activation of PAH by oxidizing their precursor trans-dihydrodiols to o-quinones [Smithgall, T.E., et al.	o-quinones	192-202	dihydrodiol dehydrogenase	Rattus norvegicus	0-25
32093466-2	2020	Recently, we reported that the tyrosinase-mediated oxidation of phenol-tagged cargo molecules is a particularly convenient method of generating o-quinones in situ.	o-quinones	144-154	tyrosinase	Homo sapiens	31-41
2964867-1	1987	The usual substrates of tyrosinase, a copper-containing monooxygenase (EC 1.14.18.1), are monophenols and o-diphenols which are both converted to o-quinones.	o-quinones	146-156	tyrosinase	Homo sapiens	24-34
3146978-1	1988	Tyrosinase usually catalyses the conversion of monophenols into o-diphenols and the oxidation of diphenols to the corresponding o-quinones.	o-quinones	128-138	tyrosinase	Homo sapiens	0-10
23334240-9	2013	Addition of BC-1 in rat microsome incubation resulted in formation of di-quinone methides and o-quinones, followed by formation of GSH conjugates.	o-quinones	94-104	brain cytoplasmic RNA 1	Rattus norvegicus	12-16
28777094-1	2017	Tyrosinases are type 3 copper enzymes that belong to the polyphenol oxidase (PPO) family and are able to catalyze both the ortho-hydroxylation of monophenols and their subsequent oxidation to o-quinones, which are precursors for the biosynthesis of colouring substances such as melanin.	o-quinones	192-202	polyphenol oxidase, chloroplastic	Malus domestica	57-75
28777094-1	2017	Tyrosinases are type 3 copper enzymes that belong to the polyphenol oxidase (PPO) family and are able to catalyze both the ortho-hydroxylation of monophenols and their subsequent oxidation to o-quinones, which are precursors for the biosynthesis of colouring substances such as melanin.	o-quinones	192-202	polyphenol oxidase, chloroplastic	Malus domestica	77-80
28219012-4	2017	Therefore, it is expected that RK exerts its cytotoxicity to melanocytes through the tyrosinase-catalyzed oxidation to cytotoxic o-quinones.	o-quinones	129-139	tyrosinase	Homo sapiens	85-95
29527287-4	2017	The genotoxicity of the o-quinones is exacerbated by nuclear translocation of estrogen o-quinones by the estrogen receptor and by the nuclear translocation of PAH o-quinones by the aryl hydrocarbon receptor.	o-quinones	24-34	aryl hydrocarbon receptor	Homo sapiens	181-206
26899308-13	2016	CONCLUSION: Ellagic acid is oxidized by tyrosinase, producing reactive o-quinones.	o-quinones	71-81	tyrosinase	Homo sapiens	40-50
24704693-1	2014	Tyrosinase is a copper-containing enzyme that mediates the hydroxylation of monophenols and oxidation of o-diphenols to o-quinones.	o-quinones	120-130	tyrosinase	Crassostrea gigas	0-10
24853564-1	2014	Tyrosinase is a multifunctional copper-containing enzyme widely distributed in plants and animals, which catalyzes both the hydroxylation of tyrosine into o-diphenols and the oxidation of o-diphenols into o-quinones.	o-quinones	205-215	tyrosinase	Homo sapiens	0-10
23411245-4	2013	Apple PPO was thermolabile, denaturing after 10min at 70 C. Losses of PPO activity were favoured by the presence of EPI in model solutions, compared with CG, due to the formation of o-quinones of EPI (QEPI) lowering PPO stability.	o-quinones	182-192	polyphenol oxidase, chloroplastic	Malus domestica	6-9
23411245-4	2013	Apple PPO was thermolabile, denaturing after 10min at 70 C. Losses of PPO activity were favoured by the presence of EPI in model solutions, compared with CG, due to the formation of o-quinones of EPI (QEPI) lowering PPO stability.	o-quinones	182-192	polyphenol oxidase, chloroplastic	Malus domestica	70-73
23411245-4	2013	Apple PPO was thermolabile, denaturing after 10min at 70 C. Losses of PPO activity were favoured by the presence of EPI in model solutions, compared with CG, due to the formation of o-quinones of EPI (QEPI) lowering PPO stability.	o-quinones	182-192	polyphenol oxidase, chloroplastic	Malus domestica	70-73
25873687-1	2015	Polyphenol oxidase (PPO) catalyses the oxidation of monophenols and/or o-diphenols to o-quinones with the concomitant reduction of oxygen to water which results in protein complexing and the formation of brown melanin pigments.	o-quinones	86-96	protoporphyrinogen oxidase	Homo sapiens	0-18
25873687-1	2015	Polyphenol oxidase (PPO) catalyses the oxidation of monophenols and/or o-diphenols to o-quinones with the concomitant reduction of oxygen to water which results in protein complexing and the formation of brown melanin pigments.	o-quinones	86-96	protoporphyrinogen oxidase	Homo sapiens	20-23
25911656-4	2015	Metabolism of PAHs through the CYP1A1/1B1/EH pathway, CYP peroxidase pathway, and AKR pathway leads to the formation of the active carcinogens diol-epoxides, radical cations, and o-quinones.	o-quinones	179-189	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	31-41
22290292-6	2012	Tyrosinase incubations in the presence of GSH gave the expected GSH conjugates resulting from trapping of the o-quinones, which were characterized by LC-MS/MS.	o-quinones	110-120	tyrosinase	Equus caballus	0-10
21622560-5	2011	PAH o-quinones were reduced to the corresponding catechols by dithiothreitol under anaerobic conditions and then further O-methylated by human S-COMT in the presence of S-[3H]adenosyl-l-methionine as a methyl group donor.	o-quinones	4-14	catechol-O-methyltransferase	Homo sapiens	145-149
25084402-4	2009	Standard solutions of phenolic compounds (200 muL) were injected, and the cathodic peak currents due to the reduction current of o-quinones produced by the TYR-catalyzed oxidation (phenolase activity) were detected at the applied potential of -50 mV vs. Ag/AgCl.	o-quinones	129-139	tyrosinase	Homo sapiens	156-159
25084402-5	2009	In this reaction, the electrochemically generated catechol compounds from o-quinones are re-oxidized repeatedly by catecholase activity of the TYR, leading to a sufficient amplified signal.	o-quinones	74-84	tyrosinase	Homo sapiens	143-146
18402469-2	2008	PAH trans-dihydrodiols are further activated in humans by cytochrome P450 (P450) 1A1 and 1B1 to yield diol-epoxides or by aldo-keto reductases (AKR) 1A1 and 1C1-1C4 to yield reactive and redox-active o-quinones.	o-quinones	200-210	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	58-92
18402469-2	2008	PAH trans-dihydrodiols are further activated in humans by cytochrome P450 (P450) 1A1 and 1B1 to yield diol-epoxides or by aldo-keto reductases (AKR) 1A1 and 1C1-1C4 to yield reactive and redox-active o-quinones.	o-quinones	200-210	aldo-keto reductase family 1 member A1	Homo sapiens	144-147
17407318-1	2007	Polyphenol oxidase (PPO; EC 1.14.18.1) catalyzes the hydroxylation of monophenols to o-diphenols (cresolase activity) and the oxidation of o-diphenols to o-quinones (catecholase activity), leading to browning in plants and produce.	o-quinones	154-164	protoporphyrinogen oxidase	Homo sapiens	0-18
18489080-3	2008	Alternatively, aldo-keto reductases (AKRs) convert intermediate PAH trans-dihydrodiols to o-quinones, which cause DNA damage by generating reactive oxygen species (ROS).	o-quinones	90-100	phenylalanine hydroxylase	Homo sapiens	64-67
18489080-9	2008	Nanomolar concentrations of PAH o-quinones generated 8-oxo-dGuo (detected by HPLC-ECD) in a concentration dependent manner that correlated in a linear fashion with mutagenic frequency.	o-quinones	32-42	phenylalanine hydroxylase	Homo sapiens	28-31
17407318-1	2007	Polyphenol oxidase (PPO; EC 1.14.18.1) catalyzes the hydroxylation of monophenols to o-diphenols (cresolase activity) and the oxidation of o-diphenols to o-quinones (catecholase activity), leading to browning in plants and produce.	o-quinones	154-164	protoporphyrinogen oxidase	Homo sapiens	20-23
14643889-1	2004	The kinetic behaviour of tyrosinase is very complex because the enzymatic oxidation of monophenol and o-diphenol to o-quinones occurs simultaneously with the coupled non-enzymatic reactions of the latter.	o-quinones	116-126	tyrosinase	Homo sapiens	25-35
14751451-1	2004	The purpose of this study was to evaluate the contribution of DT-diaphorase inhibition to in vivo neurodegenerative effects of dopamine (DA) oxidation to the corresponding o-quinones.	o-quinones	172-182	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	62-75
14639047-1	2003	OBJECTIVE: Glutathione-S-transferases, NAD(P)H: quinone oxidoreductase1 (NQO1) and NRH: quinone oxidoreductase2 (NQO2) provide important cellular defences against the neurotoxicity induced by catecholamine-derived o-quinones and oxidative stress during redox cycling.	o-quinones	214-224	NAD(P)H quinone dehydrogenase 1	Homo sapiens	39-71
14639047-1	2003	OBJECTIVE: Glutathione-S-transferases, NAD(P)H: quinone oxidoreductase1 (NQO1) and NRH: quinone oxidoreductase2 (NQO2) provide important cellular defences against the neurotoxicity induced by catecholamine-derived o-quinones and oxidative stress during redox cycling.	o-quinones	214-224	NAD(P)H quinone dehydrogenase 1	Homo sapiens	73-77
14639047-1	2003	OBJECTIVE: Glutathione-S-transferases, NAD(P)H: quinone oxidoreductase1 (NQO1) and NRH: quinone oxidoreductase2 (NQO2) provide important cellular defences against the neurotoxicity induced by catecholamine-derived o-quinones and oxidative stress during redox cycling.	o-quinones	214-224	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	113-117
12771134-5	2003	o-Quinones formed in the reaction of catechols with either peroxynitrite or NO2 react with cysteine residues in TH and inhibit catalytic function.	o-quinones	0-10	tyrosine hydroxylase	Homo sapiens	112-114
12453669-1	2003	A tyrosinase-directed therapeutic approach for malignant melanoma therapy uses the depigmenting phenolic agents such as 4-hydroxyanisole (4-HA) to form cytotoxic o-quinones.	o-quinones	162-172	tyrosinase	Rattus norvegicus	2-12
15962938-0	2005	Formation of 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxo-dGuo) by PAH o-quinones: involvement of reactive oxygen species and copper(II)/copper(I) redox cycling.	o-quinones	69-79	phenylalanine hydroxylase	Homo sapiens	65-68
12269833-2	2002	PAH trans-dihydrodiol proximate carcinogens are oxidized by aldo-keto reductases (AKRs) to their corresponding reactive and redox-active o-quinones which may have the properties of initiators and promoters.	o-quinones	137-147	phenylalanine hydroxylase	Homo sapiens	0-3
12269833-3	2002	To determine whether these o-quinones target protein kinase C (PKC), their effects on human recombinant PKCalpha and PKCdelta and the catalytic fragment of rat brain PKC were determined.	o-quinones	27-37	proline rich transmembrane protein 2	Homo sapiens	45-61
12269833-3	2002	To determine whether these o-quinones target protein kinase C (PKC), their effects on human recombinant PKCalpha and PKCdelta and the catalytic fragment of rat brain PKC were determined.	o-quinones	27-37	proline rich transmembrane protein 2	Homo sapiens	63-66
12269833-3	2002	To determine whether these o-quinones target protein kinase C (PKC), their effects on human recombinant PKCalpha and PKCdelta and the catalytic fragment of rat brain PKC were determined.	o-quinones	27-37	protein kinase C alpha	Homo sapiens	104-112
12269833-3	2002	To determine whether these o-quinones target protein kinase C (PKC), their effects on human recombinant PKCalpha and PKCdelta and the catalytic fragment of rat brain PKC were determined.	o-quinones	27-37	protein kinase C delta	Homo sapiens	117-125
12269833-3	2002	To determine whether these o-quinones target protein kinase C (PKC), their effects on human recombinant PKCalpha and PKCdelta and the catalytic fragment of rat brain PKC were determined.	o-quinones	27-37	protein kinase C, gamma	Rattus norvegicus	104-107