PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
10704220-2	2000	60 degrees and translate through an appreciable distance between two binding sites, proximal to cytochrome c(1) and to the lumen-side quinol binding site.	Hydroquinones	134-140	cytochrome c1	Homo sapiens	96-111
10704220-7	2000	This suggests that upon initiation of electron transfer by a light flash, cytochrome b(6) reduction requires movement of reduced ISP from an initial position predominantly proximal to cytochrome f, apparently favored by the reduced ISP, to the quinol binding site at which the oxidant-induced reduction of cytochrome b(6) is initiated.	Hydroquinones	244-250	mitochondrially encoded cytochrome b	Homo sapiens	74-86
10704220-7	2000	This suggests that upon initiation of electron transfer by a light flash, cytochrome b(6) reduction requires movement of reduced ISP from an initial position predominantly proximal to cytochrome f, apparently favored by the reduced ISP, to the quinol binding site at which the oxidant-induced reduction of cytochrome b(6) is initiated.	Hydroquinones	244-250	mitochondrially encoded cytochrome b	Homo sapiens	306-318
10640505-1	2000	We have already reported that the quinol formation from some para-alkylphenols, which is a novel metabolic pathway catalyzed by cytochrome P-450, occurs in a rat liver microsomal system ().	Hydroquinones	34-40	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	128-144
10640505-2	2000	In the present study, we investigated whether estrone and 17beta-estadiol, each of which contains a p-alkylphenol moiety, are also oxidized into the corresponding quinols by cytochrome P-450.	Hydroquinones	163-170	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	174-190
10640505-4	2000	The results show that estrone and 17beta-estadiol were converted into the corresponding quinols by CYP1A1, CYP2B6, and CYP2E1.	Hydroquinones	88-95	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	99-105
10640505-4	2000	The results show that estrone and 17beta-estadiol were converted into the corresponding quinols by CYP1A1, CYP2B6, and CYP2E1.	Hydroquinones	88-95	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	107-113
10640505-4	2000	The results show that estrone and 17beta-estadiol were converted into the corresponding quinols by CYP1A1, CYP2B6, and CYP2E1.	Hydroquinones	88-95	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	119-125
10651825-3	2000	Modular kinetic analysis around coenzyme Q revealed that stimulation of the rate was due to stimulation of quinol oxidation via the cytochrome pathway (cytochrome bc1, cytochrome c and cytochrome c oxidase).	Hydroquinones	107-113	cytochrome c	Solanum tuberosum	168-180
10651825-3	2000	Modular kinetic analysis around coenzyme Q revealed that stimulation of the rate was due to stimulation of quinol oxidation via the cytochrome pathway (cytochrome bc1, cytochrome c and cytochrome c oxidase).	Hydroquinones	107-113	cytochrome c	Solanum tuberosum	185-197
9062116-0	1997	Function-directed mutagenesis of the cytochrome b6f complex in Chlamydomonas reinhardtii: involvement of the cd loop of cytochrome b6 in quinol binding to the Q(o) site.	Hydroquinones	137-143	cytochrome b	Chlamydomonas reinhardtii	37-49
10512801-1	1999	Crystallographic structures of the mitochondrial ubiquinol/cytochrome c oxidoreductase (cytochrome bc(1) complex) suggest that the mechanism of quinol oxidation by the bc(1) complex involves a substantial movement of the soluble head of the Rieske iron-sulfur protein (ISP) between reaction domains in cytochrome b and cytochrome c(1) subunits.	Hydroquinones	52-58	mitochondrially encoded cytochrome b	Homo sapiens	88-100
10512801-1	1999	Crystallographic structures of the mitochondrial ubiquinol/cytochrome c oxidoreductase (cytochrome bc(1) complex) suggest that the mechanism of quinol oxidation by the bc(1) complex involves a substantial movement of the soluble head of the Rieske iron-sulfur protein (ISP) between reaction domains in cytochrome b and cytochrome c(1) subunits.	Hydroquinones	52-58	cytochrome c1	Homo sapiens	319-334
10397748-1	1999	NAD(P)H:quinone oxidoreductase (NQO1) converts benzene-derived quinones to less toxic hydroquinones and has been implicated in benzene-associated hematotoxicity.	Hydroquinones	86-99	crystallin zeta	Homo sapiens	8-30
10397748-1	1999	NAD(P)H:quinone oxidoreductase (NQO1) converts benzene-derived quinones to less toxic hydroquinones and has been implicated in benzene-associated hematotoxicity.	Hydroquinones	86-99	NAD(P)H quinone dehydrogenase 1	Homo sapiens	32-36
9703276-3	1998	In this report, the mutagenicity and carcinogenicity of hydroquinones of benzo(a)pyrene and benzene was investigated to address two important questions: (1) do hydroquinones contribute to benzo(a)pyrene and benzene carcinogenicity; and (2) how safe is it to increase the levels of NAD(P)H:quinone oxidoreductase 1 (NQO1), a key enzyme in the generation of hydroquinone.	Hydroquinones	56-69	NAD(P)H dehydrogenase [quinone] 1	Cricetulus griseus	281-313
9703276-3	1998	In this report, the mutagenicity and carcinogenicity of hydroquinones of benzo(a)pyrene and benzene was investigated to address two important questions: (1) do hydroquinones contribute to benzo(a)pyrene and benzene carcinogenicity; and (2) how safe is it to increase the levels of NAD(P)H:quinone oxidoreductase 1 (NQO1), a key enzyme in the generation of hydroquinone.	Hydroquinones	56-69	NAD(P)H dehydrogenase [quinone] 1	Cricetulus griseus	315-319
10748880-1	1999	AIMS: The two electron reduction of quinones to hydroquinones by NAD(P)H quinone oxidoreductase (NQO1) plays an important role in both activation and detoxification of quinone and similarly reactive compounds.	Hydroquinones	48-61	NAD(P)H quinone dehydrogenase 1	Homo sapiens	97-101
9394028-9	1997	A strong correlation was found between the immunoquantified concentrations of CYP3A and the rates of formation of the sulfoxide and quinol metabolites of tazofelone.	Hydroquinones	132-138	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	78-83
10932727-7	1997	The main difference between quinol- and the aa3-type cytochrome c-oxidases is the CuA center, which is absent in the quinol oxidases.	Hydroquinones	28-34	cytochrome c, somatic	Homo sapiens	53-65
10932727-7	1997	The main difference between quinol- and the aa3-type cytochrome c-oxidases is the CuA center, which is absent in the quinol oxidases.	Hydroquinones	117-123	cytochrome c, somatic	Homo sapiens	53-65
27406966-4	1997	Redox cycling of 2,3-dimethyl-, 2,3-dimethoxy- and 2-methoxy-1,4-naphthoquinone, and the autoxidation of their respective hydroquinones, were similarly inhibited by diaphorase.	Hydroquinones	122-135	dihydrolipoamide dehydrogenase	Homo sapiens	165-175
8573194-5	1996	SOD also inhibited the rate of quinol oxidation by oxygen, after quinone reduction by a stoichiometric amount of DHLA.	Hydroquinones	31-37	superoxide dismutase 1	Homo sapiens	0-3
12226388-11	1996	As in the case with DT-diaphorase in animals, the main NAD(P)H-QR function in plant cells may be the reduction of quinones to quinols, which prevents the production of semiquinones and oxygen radicals.	Hydroquinones	126-133	NAD(P)H quinone dehydrogenase 1	Homo sapiens	20-33
7786300-5	1995	It was found that rat and human UGT1.6 and human UGT1.7 catalyse monoglucuronide formation of planar PAH quinols.	Hydroquinones	105-112	UDP glucuronosyltransferase family 1 member A6	Homo sapiens	32-38
7639539-1	1995	NAD(P)H: quinone-acceptor oxidoreductase (EC 1.6.99.2), also referred to as DT-diaphorase, is a flavoprotein that catalyzes the two-electron reduction of quinones and quinonoid compounds to hydroquinones, using either NADH or NADPH as the electron donor.	Hydroquinones	190-203	NAD(P)H quinone dehydrogenase 1	Homo sapiens	76-89
8558523-7	1996	From comparing the structural requirements for crosslinking and the cytotoxicities, a mechanism has been proposed wherein some hydroquinones can associate and react at TGC sequences in DNA.	Hydroquinones	127-140	transglutaminase 2	Homo sapiens	168-171
7673215-11	1995	The respiratory activities and the amounts of reduced cytochrome b measured during steady state suggest that the W142S mutation also modified the quinol-cytochrome c1 electron transfer pathway.	Hydroquinones	146-152	cytochrome b	Saccharomyces cerevisiae S288C	54-66
7673215-13	1995	Of the four amino acids tested at position 142, only arginine resulted in a decrease in cytochrome b reduction through center N. These findings are discussed in terms of the structure and function of the quinol oxidation site and seem to indicate that Trp-142 is not critical to the kinetic interaction of ubiquinol with the reductase, but plays an important role in the electron transfer reactions that intervene between ubiquinol oxidation and cytochrome c1 reduction.	Hydroquinones	204-210	cytochrome b	Saccharomyces cerevisiae S288C	88-100
7786300-5	1995	It was found that rat and human UGT1.6 and human UGT1.7 catalyse monoglucuronide formation of planar PAH quinols.	Hydroquinones	105-112	UDP glucuronosyltransferase family 1 member A7	Homo sapiens	49-55
7786300-9	1995	The results suggest that planar PAH phenols and quinols are conjugated more efficiently by human UGT1.7 than by UGT1.6, which preferentially conjugates simple planar phenols.	Hydroquinones	48-55	UDP glucuronosyltransferase family 1 member A7	Homo sapiens	97-103
7786300-9	1995	The results suggest that planar PAH phenols and quinols are conjugated more efficiently by human UGT1.7 than by UGT1.6, which preferentially conjugates simple planar phenols.	Hydroquinones	48-55	UDP glucuronosyltransferase family 1 member A6	Homo sapiens	112-118
7832587-2	1994	The substrate specificity (quinol vs. cytochrome c) is reflected in the presence of a unique copper centre (CuA) in cytochrome c oxidases.	Hydroquinones	27-33	cytochrome c, somatic	Homo sapiens	116-128
7531691-1	1995	NAD(P)H:quinone oxidoreductase (EC 1.6.99.2) (DT-diaphorase) is an FAD-containing enzyme that catalyzes the 2-electron reduction of quinones to hydroquinones using either NADH or NADPH as the electron donor.	Hydroquinones	144-157	NAD(P)H quinone dehydrogenase 1	Homo sapiens	46-59
7531691-11	1995	The enzyme reconstituted with oxidized 5-deaza-FAD has significant catalytic activity, confirming that DT-diaphorase is an obligatory 2-electron transfer enzyme and plays a role in the detoxification of quinones and quinoid compounds by reducing them to the relatively stable hydroquinones.	Hydroquinones	276-289	NAD(P)H quinone dehydrogenase 1	Homo sapiens	103-116
7989327-7	1994	This conclusion is confirmed by the results, which indicate that pi-ADH very efficiently catalyzes the reduction of BQI and 1,4-benzoquinone (BQ) to the corresponding hydroquinones.	Hydroquinones	167-180	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	68-71
24311289-8	1994	With added quinol, reduction of cytochrome b-563 occurred.	Hydroquinones	11-17	mitochondrially encoded cytochrome b	Homo sapiens	32-44
2846049-5	1988	The extreme specificity of myxothiazol binding at or near the quinol oxidase domain of mitochondrial cytochrome b, i.e., b-566, suggests a defect in this region of complex III which may perturb the kinetics or thermodynamics of quinol oxidation in the complex.	Hydroquinones	62-68	mitochondrially encoded cytochrome b	Homo sapiens	101-113
8461317-1	1993	NAD(P)H:quinone reductase, or DT-diaphorase, has been studied primarily in the liver where it appears to function as an antioxidant-like enzyme in the 2-electron reduction of some quinones to less toxic hydroquinones.	Hydroquinones	203-216	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	30-43
1764253-2	1991	This semiquinone redox cycling is prevented by the NAD(P)H:quinone reductase (NQR; EC 1.6.99.2) because it mediates a 2-electron reduction which results in the formation of hydroquinones instead of semiquinones.	Hydroquinones	173-186	crystallin zeta	Homo sapiens	51-76
1764253-2	1991	This semiquinone redox cycling is prevented by the NAD(P)H:quinone reductase (NQR; EC 1.6.99.2) because it mediates a 2-electron reduction which results in the formation of hydroquinones instead of semiquinones.	Hydroquinones	173-186	crystallin zeta	Homo sapiens	78-81
2176839-7	1990	(4) In pre-steady-state assays of cytochrome b reduction by quinol, the mutant shows a reduced extent of reduction.	Hydroquinones	60-66	cytochrome b, mitochondrial	Mus musculus	34-46
1973524-1	1990	Several lines of evidence suggest that the renal-specific toxicity of quinol-linked GSH conjugates is probably a result of their metabolism by gamma-glutamyl transpeptidase and selective accumulation by proximal tubular cells.	Hydroquinones	70-76	inactive glutathione hydrolase 2	Homo sapiens	143-172
1971126-5	1990	The ability of gamma-GT to facilitate quinol oxidation by catalyzing the formation of the labile cysteine conjugate may have important biological consequences.	Hydroquinones	38-44	inactive glutathione hydrolase 2	Homo sapiens	15-23
2162450-11	1990	The activity of cytochrome P-450 reductase, which reduces quinones to hydroquinones in the estrogen redox cycle, was 6-fold higher in liver than in kidney of both control and estrogen-treated animals.	Hydroquinones	70-83	cytochrome P450 2A3-like	Mesocricetus auratus	16-32
2307529-1	1990	NAD(P)H:(quinone-acceptor)oxidoreductase (QAO), previously known as DT-diaphorase, catalyzes the reduction of quinones to hydroquinones.	Hydroquinones	122-135	NAD(P)H quinone dehydrogenase 1	Homo sapiens	68-81
33768254-4	2021	Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site.	Hydroquinones	177-183	NADH dehydrogenase subunit 1	Arabidopsis thaliana	128-131
33768254-4	2021	Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site.	Hydroquinones	177-183	NADH dehydrogenase subunit 1	Arabidopsis thaliana	133-161
34356648-2	2021	Based on the findings of clinical trials, it is safe to conclude that genetic predisposition and environmental factors are the main factors responsible for the formation of colorectal cancer.The NQO1 gene plays an important role in reducing endogenous and exogenous quinones as well as quinone compounds to hydroquinones.	Hydroquinones	307-320	NAD(P)H quinone dehydrogenase 1	Homo sapiens	195-199
34276623-6	2021	These multiheme c-Cyts may form the pathways similar to those found in bacteria for transferring electrons from the quinone/quinol pool in the cytoplasmic membrane to the Fe(III) (oxyhydr)oxides external to the archaeal cells.	Hydroquinones	124-130	general transcription factor IIE subunit 1	Homo sapiens	171-178
8329437-7	1993	The comparison of inhibition titrations in combination with the analysis of the primary structures has enabled us to identify amino acid residues in cytochrome b that may be involved in the binding of the inhibitors and, by extrapolation, quinone/quinol.	Hydroquinones	247-253	mitochondrially encoded cytochrome b	Homo sapiens	149-161
1510689-1	1992	Two new methods have been devised for measuring fumarate reduction by beef heart succinate-ubiquinone oxidoreductase with quinols as electron donors.	Hydroquinones	122-129	thioredoxin reductase 1	Homo sapiens	102-116
1914494-1	1991	UDP-glucuronosyltransferases (UGT) play a major role in the elimination of nucleophilic metabolites of carcinogens, such as phenols and quinols of polycyclic aromatic hydrocarbons.	Hydroquinones	136-143	beta-1,3-glucuronyltransferase 2	Homo sapiens	0-28
1914494-1	1991	UDP-glucuronosyltransferases (UGT) play a major role in the elimination of nucleophilic metabolites of carcinogens, such as phenols and quinols of polycyclic aromatic hydrocarbons.	Hydroquinones	136-143	beta-1,3-glucuronyltransferase 2	Homo sapiens	30-33
2244516-0	1990	Effect of superoxide dismutase on the autoxidation of hydroquinones formed during DT-diaphorase catalysis and glutathione nucleophilic addition.	Hydroquinones	54-67	NAD(P)H quinone dehydrogenase 1	Homo sapiens	82-95
2538447-10	1989	These results suggest that the quinol oxidizing sites in the cytochrome b6-f complex may differ from those in the mitochondrial cytochrome b-c1 complex.	Hydroquinones	31-37	mitochondrially encoded cytochrome b	Homo sapiens	61-73
3129984-1	1988	DT diaphorase catalyzes the transfer of two electrons to quinones to form relatively stable hydroquinones, thus protecting cells from damage by semiquinone production and subsequent superoxide radical formation.	Hydroquinones	92-105	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	0-13
2455523-6	1988	The results support the hypothesis that DT-diaphorase competes with one-electron quinone-reducing enzymes (such as cytochrome P-450 reductase) which generate auto-oxidizable semiquinones and forms more stable hydroquinones as an initial step in the detoxification of quinones in 10T1/2 cells.	Hydroquinones	209-222	NAD(P)H dehydrogenase, quinone 1	Mus musculus	40-53
3934671-4	1985	Structurally dissimilar catechols (1,2-diphenols) and hydroquinones (1,4-diphenols) induce quinone reductase in these systems, but resorcinol (1,3-diphenol) and its substituted analogues are inactive.	Hydroquinones	54-67	crystallin, zeta	Mus musculus	91-108
2830916-3	1987	Cytochrome P-450 and NADPH-cytochrome P-450 reductase are capable of DCNQ reduction to semi- and hydroquinones.	Hydroquinones	97-110	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	0-16
2830916-3	1987	Cytochrome P-450 and NADPH-cytochrome P-450 reductase are capable of DCNQ reduction to semi- and hydroquinones.	Hydroquinones	97-110	cytochrome p450 oxidoreductase	Homo sapiens	21-53
24442953-3	1985	Three mechanisms of quinol oxidation are possible: (1) The removal of an electron from the quinol, QH inf2 (sup t) , directly to produce the radical cation, QH 2 ( +) .	Hydroquinones	20-26	inverted formin 2	Homo sapiens	102-106
24442953-3	1985	Three mechanisms of quinol oxidation are possible: (1) The removal of an electron from the quinol, QH inf2 (sup t) , directly to produce the radical cation, QH 2 ( +) .	Hydroquinones	91-97	inverted formin 2	Homo sapiens	102-106
6319123-3	1983	Measurements of the H+/e- stoichiometry, with three different methods, show that four protons are released from the vesicles per 2e- flowing from quinols to cytochrome c, two of these protons formally deriving from scalar oxidation of quinols by cytochrome c.	Hydroquinones	146-153	cytochrome c, somatic	Homo sapiens	157-169
6319123-3	1983	Measurements of the H+/e- stoichiometry, with three different methods, show that four protons are released from the vesicles per 2e- flowing from quinols to cytochrome c, two of these protons formally deriving from scalar oxidation of quinols by cytochrome c.	Hydroquinones	146-153	cytochrome c, somatic	Homo sapiens	246-258
6319123-3	1983	Measurements of the H+/e- stoichiometry, with three different methods, show that four protons are released from the vesicles per 2e- flowing from quinols to cytochrome c, two of these protons formally deriving from scalar oxidation of quinols by cytochrome c.	Hydroquinones	235-242	cytochrome c, somatic	Homo sapiens	157-169
6284121-2	1982	The kinetics of reduction of cytochrome c by catechol(s), quinol(s) and related compounds were investigated by stopped-flow spectrophotometry.	Hydroquinones	58-64	cytochrome c, somatic	Homo sapiens	29-41
6313461-7	1983	Finally, cytosolic DT diaphorase, which carries out a two-electron reduction of quinones to more stable hydroquinones, may compete with the one-electron systems and participate in the detoxification of quinones by supplying hydroquinones for conjugation reactions.	Hydroquinones	104-117	NAD(P)H quinone dehydrogenase 1	Homo sapiens	19-32
6313461-7	1983	Finally, cytosolic DT diaphorase, which carries out a two-electron reduction of quinones to more stable hydroquinones, may compete with the one-electron systems and participate in the detoxification of quinones by supplying hydroquinones for conjugation reactions.	Hydroquinones	224-237	NAD(P)H quinone dehydrogenase 1	Homo sapiens	19-32
6293557-3	1982	At low concentrations of cytochrome c, however, the titrations as a function of quinol concentration appear biphasic both in mitochondria and in submitochondrial particles containing trapped cytochrome c inside the vesicle space, fitting two apparent Km values for ubiquinol-1.	Hydroquinones	80-86	LOC104968582	Bos taurus	25-37
6293557-3	1982	At low concentrations of cytochrome c, however, the titrations as a function of quinol concentration appear biphasic both in mitochondria and in submitochondrial particles containing trapped cytochrome c inside the vesicle space, fitting two apparent Km values for ubiquinol-1.	Hydroquinones	80-86	LOC104968582	Bos taurus	191-203
32165217-1	2020	The NAD(P)H:quinone oxidoreductase 1 (NQO1) gene encodes a cytosolic flavoenzyme that catalyzes the two-electron reduction of quinones to hydroquinones.	Hydroquinones	138-151	NAD(P)H dehydrogenase, quinone 1	Mus musculus	4-36
14285230-0	1965	PHOTOREACTIONS OF CHLOROPLASTS AND CHLOROPHYLL A WITH HYDROQUINONES AND QUINONES: COUPLED PHOTOREDUCTION OF CYTOCHROME C.	Hydroquinones	54-67	cytochrome c, somatic	Homo sapiens	108-120
34040527-9	2021	Both EPR and LCMS studies confirmed a significant increase in the ROS production in the NQO2 overexpressing cells due to the fast reduction of quinone into quinol that can re-oxidize to form superoxide radicals.	Hydroquinones	156-162	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	88-92
34040527-11	2021	Whereas NQO2 inhibition decreases the amount of superoxide in the first case by decreasing the amount of quinol formed, it increased the toxicity of menadione in the cells co-expressing both enzymes.	Hydroquinones	105-111	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	8-12
39633-4	1979	The data obtained are in favour of the idea that when illuminating the solutions of these pigments in ethanol containing pure p-benzoquinone at pH higher than the definite value, PhP initiation is conditioned by photochemical reaction of pigments with equilibrium amounts of hydroquinones or semiquinone always present in quinone solutions.	Hydroquinones	275-288	N-acylsphingosine amidohydrolase 1	Homo sapiens	179-182
33652166-2	2021	DT-diaphorase (DTD), whose level is strongly elevated in various tumors, is a cytosolic flavoenzyme that promotes intracellular reactive oxygen species (ROS) generation via the redox cycling of hydroquinones.	Hydroquinones	194-207	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-13
31900833-2	2020	Past studies found that continuous exposure of human AML U937 cells to HQ selectively produces malignant U937/HQ cells in which FOXP3 upregulation modulates malignant progression.	Hydroquinones	71-73	forkhead box P3	Homo sapiens	128-133
31900833-6	2020	Treatment of parental Original Article and HQ-selected malignant U937 cells with compound C induced ROS-mediated p38 MAPK activation, leading to a suppression of AMPKalpha, TET2, and FOXP3 expression.	Hydroquinones	43-45	mitogen-activated protein kinase 14	Homo sapiens	113-116
31900833-6	2020	Treatment of parental Original Article and HQ-selected malignant U937 cells with compound C induced ROS-mediated p38 MAPK activation, leading to a suppression of AMPKalpha, TET2, and FOXP3 expression.	Hydroquinones	43-45	tet methylcytosine dioxygenase 2	Homo sapiens	173-177
31900833-6	2020	Treatment of parental Original Article and HQ-selected malignant U937 cells with compound C induced ROS-mediated p38 MAPK activation, leading to a suppression of AMPKalpha, TET2, and FOXP3 expression.	Hydroquinones	43-45	forkhead box P3	Homo sapiens	183-188
31900833-10	2020	Restoration of AMPKalpha1 or FOXP3 expression increased cell survival after treatment with compound C. In conclusion, our results show that compound C suppresses AMPK/TET2 axis-mediated FOXP3 expression and induces autophagy-dependent apoptosis in parental and HQ-selected malignant U937 cells, suggesting that the AMPK/TET2/FOXP3 axis is a promising target for improving AML therapy and attenuating benzene exposure-induced AML progression.	Hydroquinones	261-263	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	15-25
31900833-10	2020	Restoration of AMPKalpha1 or FOXP3 expression increased cell survival after treatment with compound C. In conclusion, our results show that compound C suppresses AMPK/TET2 axis-mediated FOXP3 expression and induces autophagy-dependent apoptosis in parental and HQ-selected malignant U937 cells, suggesting that the AMPK/TET2/FOXP3 axis is a promising target for improving AML therapy and attenuating benzene exposure-induced AML progression.	Hydroquinones	261-263	forkhead box P3	Homo sapiens	29-34
31900833-10	2020	Restoration of AMPKalpha1 or FOXP3 expression increased cell survival after treatment with compound C. In conclusion, our results show that compound C suppresses AMPK/TET2 axis-mediated FOXP3 expression and induces autophagy-dependent apoptosis in parental and HQ-selected malignant U937 cells, suggesting that the AMPK/TET2/FOXP3 axis is a promising target for improving AML therapy and attenuating benzene exposure-induced AML progression.	Hydroquinones	261-263	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	15-19
31900833-10	2020	Restoration of AMPKalpha1 or FOXP3 expression increased cell survival after treatment with compound C. In conclusion, our results show that compound C suppresses AMPK/TET2 axis-mediated FOXP3 expression and induces autophagy-dependent apoptosis in parental and HQ-selected malignant U937 cells, suggesting that the AMPK/TET2/FOXP3 axis is a promising target for improving AML therapy and attenuating benzene exposure-induced AML progression.	Hydroquinones	261-263	tet methylcytosine dioxygenase 2	Homo sapiens	167-171
31900833-10	2020	Restoration of AMPKalpha1 or FOXP3 expression increased cell survival after treatment with compound C. In conclusion, our results show that compound C suppresses AMPK/TET2 axis-mediated FOXP3 expression and induces autophagy-dependent apoptosis in parental and HQ-selected malignant U937 cells, suggesting that the AMPK/TET2/FOXP3 axis is a promising target for improving AML therapy and attenuating benzene exposure-induced AML progression.	Hydroquinones	261-263	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	162-166
32165217-1	2020	The NAD(P)H:quinone oxidoreductase 1 (NQO1) gene encodes a cytosolic flavoenzyme that catalyzes the two-electron reduction of quinones to hydroquinones.	Hydroquinones	138-151	NAD(P)H dehydrogenase, quinone 1	Mus musculus	38-42
31881324-8	2020	We observed that treatment with fluoxetine or the Nrf2 activator tBHQ (tert-butyl hydroquinone), could reverse depression-like-symptoms and mitigate alterations in autophagy and cell death pathways in the hippocampus by activating Nrf2-dependent gene expressions.	Hydroquinones	65-69	nuclear factor, erythroid derived 2, like 2	Mus musculus	50-54
31881324-8	2020	We observed that treatment with fluoxetine or the Nrf2 activator tBHQ (tert-butyl hydroquinone), could reverse depression-like-symptoms and mitigate alterations in autophagy and cell death pathways in the hippocampus by activating Nrf2-dependent gene expressions.	Hydroquinones	65-69	nuclear factor, erythroid derived 2, like 2	Mus musculus	231-235
31881324-8	2020	We observed that treatment with fluoxetine or the Nrf2 activator tBHQ (tert-butyl hydroquinone), could reverse depression-like-symptoms and mitigate alterations in autophagy and cell death pathways in the hippocampus by activating Nrf2-dependent gene expressions.	Hydroquinones	71-94	nuclear factor, erythroid derived 2, like 2	Mus musculus	50-54
31881324-8	2020	We observed that treatment with fluoxetine or the Nrf2 activator tBHQ (tert-butyl hydroquinone), could reverse depression-like-symptoms and mitigate alterations in autophagy and cell death pathways in the hippocampus by activating Nrf2-dependent gene expressions.	Hydroquinones	71-94	nuclear factor, erythroid derived 2, like 2	Mus musculus	231-235
31505859-2	2019	We report on the discovery and characterisation of small organic molecules from Piper genus plants exhibiting XIAP antagonism, namely erioquinol, a quinol substituted in the 4-position with an alkenyl group and the alkenylphenols eriopodols A-C. Another isolated compound was originally identified as gibbilimbol B.	Hydroquinones	138-144	X-linked inhibitor of apoptosis	Homo sapiens	110-114
31812062-0	2020	Exosomes derived from normal human bronchial epithelial cells down-regulate proliferation and migration of hydroquinone-transformed malignant recipient cells via up-regulating PTEN expression.	Hydroquinones	107-119	phosphatase and tensin homolog	Homo sapiens	176-180
31812062-3	2020	The goal of this study was to explore whether exosomes derived from normal human bronchial epithelial cells (16HBE) could transmit PTEN to hydroquinone-transformed malignant recipient cells (16HBE-t) and its possible effects on cell proliferation and migration.	Hydroquinones	139-151	phosphatase and tensin homolog	Homo sapiens	131-135
32039323-1	2020	A novel composite film of hydroquinone/resorcinol-based poly(arylene ether nitrile) (HQ/RS-PEN) improved by bisphenol A based poly(arylene ether nitrile) (BPA-PEN) was prepared, in which BPA-PEN acts as a plasticizer, leading to improved fluidity of the material, thereby favoring the crystallinity of HQ/RS-PEN.	Hydroquinones	26-38	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	91-94
32039323-1	2020	A novel composite film of hydroquinone/resorcinol-based poly(arylene ether nitrile) (HQ/RS-PEN) improved by bisphenol A based poly(arylene ether nitrile) (BPA-PEN) was prepared, in which BPA-PEN acts as a plasticizer, leading to improved fluidity of the material, thereby favoring the crystallinity of HQ/RS-PEN.	Hydroquinones	26-38	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	159-162
32039323-1	2020	A novel composite film of hydroquinone/resorcinol-based poly(arylene ether nitrile) (HQ/RS-PEN) improved by bisphenol A based poly(arylene ether nitrile) (BPA-PEN) was prepared, in which BPA-PEN acts as a plasticizer, leading to improved fluidity of the material, thereby favoring the crystallinity of HQ/RS-PEN.	Hydroquinones	26-38	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	159-162
31899212-0	2020	Up-regulation of DNMT3b contributes to HOTAIRM1 silencing via DNA hypermethylation in cells transformed by long-term exposure to hydroquinone and workers exposed to benzene.	Hydroquinones	129-141	DNA methyltransferase 3 beta	Homo sapiens	17-23
31899212-0	2020	Up-regulation of DNMT3b contributes to HOTAIRM1 silencing via DNA hypermethylation in cells transformed by long-term exposure to hydroquinone and workers exposed to benzene.	Hydroquinones	129-141	HOXA transcript antisense RNA, myeloid-specific 1	Homo sapiens	39-47
31899212-4	2020	But the influence of benzene or HQ on HOTAIRM1 expression in AML associated pathway is still unclear.	Hydroquinones	32-34	HOXA transcript antisense RNA, myeloid-specific 1	Homo sapiens	38-46
31899212-5	2020	In the TK6 cells with short-term exposure to HQ (HQ-ST cells) or long term HQ exposure induced malignant transformed TK6 cells (HQ-MT cells), the relationship between DNMT3b and HOTAIRM1 was explored.	Hydroquinones	45-47	HOXA transcript antisense RNA, myeloid-specific 1	Homo sapiens	178-186
31899212-10	2020	These suggest that long term exposure to HQ or benzene might induce the increase of DNMT3b expression and the promoter hypermethylation to silence the expression of HOTAIRM1, a possible tumor-suppressor in the AML associated carcinogenesis pathway.	Hydroquinones	41-43	DNA methyltransferase 3 beta	Homo sapiens	84-90
31899212-10	2020	These suggest that long term exposure to HQ or benzene might induce the increase of DNMT3b expression and the promoter hypermethylation to silence the expression of HOTAIRM1, a possible tumor-suppressor in the AML associated carcinogenesis pathway.	Hydroquinones	41-43	HOXA transcript antisense RNA, myeloid-specific 1	Homo sapiens	165-173
31949167-5	2020	In Rhodobacter cytochrome bc1 complex the equivalent substitution causes a kinetics defect with longer occupancy of RISP head domain towards the quinol oxidation site.	Hydroquinones	145-151	brain cytoplasmic RNA 1	Mus musculus	26-29
31949167-5	2020	In Rhodobacter cytochrome bc1 complex the equivalent substitution causes a kinetics defect with longer occupancy of RISP head domain towards the quinol oxidation site.	Hydroquinones	145-151	ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1	Mus musculus	116-120
30097722-3	2018	AOX catalyzes the oxidation of quinol and the reduction of oxygen into water.	Hydroquinones	31-37	alternative oxidase 2	Arabidopsis thaliana	0-3
30062552-2	2018	NAD(P)H:quinone oxidoreductase 1 (NQO-1), the enzyme responsible for biotransformation of quinones into hydroquinones, was examined for its involvement in these endothelium-dependent augmentations, establishing a link between the metabolism of quinones by NQO-1 and biased sGC activity.	Hydroquinones	104-117	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	0-32
30062552-2	2018	NAD(P)H:quinone oxidoreductase 1 (NQO-1), the enzyme responsible for biotransformation of quinones into hydroquinones, was examined for its involvement in these endothelium-dependent augmentations, establishing a link between the metabolism of quinones by NQO-1 and biased sGC activity.	Hydroquinones	104-117	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	34-39
30118240-2	2018	Key to their assembly is the development of a stereocontrolled p-quinol functionalization sequence which enables rapid access to DDO C-ring stereopolyads from simple precursors.	Hydroquinones	65-71	D-aspartate oxidase	Homo sapiens	129-132
28578385-1	2017	NQO1 is a FAD-binding protein that can form homodimers and reduce quinones to hydroquinones, and a growing body of evidence currently suggests that NQO1 is dramatically elevated in solid cancers.	Hydroquinones	78-91	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-4
29937372-3	2018	Here, we have incorporated an alternative quinol oxidase (AOX) into mammalian heart mitochondrial membranes to introduce a competing pathway for quinol oxidation and test for channeling.	Hydroquinones	42-48	acyl-CoA oxidase 1	Homo sapiens	58-61
29937372-5	2018	Therefore, the quinol generated in supercomplexes by complex I is reoxidized more rapidly outside the supercomplex by AOX than inside the supercomplex by complex III.	Hydroquinones	15-21	acyl-CoA oxidase 1	Homo sapiens	118-121
29705394-0	2018	Functional flexibility of electron flow between quinol oxidation Qo site of cytochrome bc1 and cytochrome c revealed by combinatory effects of mutations in cytochrome b, iron-sulfur protein and cytochrome c1.	Hydroquinones	48-54	mitochondrially encoded cytochrome b	Homo sapiens	76-88
29705394-1	2018	Transfer of electron from quinol to cytochrome c is an integral part of catalytic cycle of cytochrome bc1.	Hydroquinones	26-32	cytochrome c, somatic	Homo sapiens	36-48
29705394-2	2018	It is a multi-step reaction involving: i) electron transfer from quinol bound at the catalytic Qo site to the Rieske iron-sulfur ([2Fe-2S]) cluster, ii) large-scale movement of a domain containing [2Fe-2S] cluster (ISP-HD) towards cytochrome c1, iii) reduction of cytochrome c1 by reduced [2Fe-2S] cluster, iv) reduction of cytochrome c by cytochrome c1.	Hydroquinones	65-71	cytochrome c, somatic	Homo sapiens	231-243
28681474-1	2017	In vivo specific isotope labeling at the residue or substituent level is used to probe menasemiquinone (MSK) binding to the quinol oxidation site of respiratory nitrate reductase A (NarGHI) from E. coli.	Hydroquinones	124-130	salt inducible kinase 1	Homo sapiens	104-107
28645578-4	2017	Consistently, quinones are easier than hydroquinones in Nrf2 activation and ARE-driven antioxidant protein expressions.	Hydroquinones	39-52	NFE2 like bZIP transcription factor 2	Homo sapiens	56-60
30134616-1	2018	The sea is a rich source of biological active compounds, among which terpenyl-quinones/hydroquinones constitute a family of secondary metabolites with diverse pharmacological properties.	Hydroquinones	87-100	S13 erythroblastosis (avian) oncogene homolog	Homo sapiens	4-7
29025057-1	2017	NRH: quinone oxidoreductase 2 (NQO2) is a cytosolic and ubiquitously expressed flavoprotein that catalyzes the two-electron reduction of quinone to hydroquinones.	Hydroquinones	148-161	N-ribosyldihydronicotinamide quinone reductase 2	Mus musculus	0-29
29025057-1	2017	NRH: quinone oxidoreductase 2 (NQO2) is a cytosolic and ubiquitously expressed flavoprotein that catalyzes the two-electron reduction of quinone to hydroquinones.	Hydroquinones	148-161	N-ribosyldihydronicotinamide quinone reductase 2	Mus musculus	31-35
28578385-1	2017	NQO1 is a FAD-binding protein that can form homodimers and reduce quinones to hydroquinones, and a growing body of evidence currently suggests that NQO1 is dramatically elevated in solid cancers.	Hydroquinones	78-91	NAD(P)H quinone dehydrogenase 1	Homo sapiens	148-152
27508986-2	2016	The analogue, H2B-Q, consists of the redox-active quinone segment found in ubiquinone, 2,3-dimethoxy-1,4-benzoquinone, coupled to a boron-dipyrromethene (BODIPY) fluorophore segment that both imparts lipophilicity in lieu of the isoprenyl tail of ubiquinone, and reports on redox changes at the quinone/quinol segment.	Hydroquinones	303-309	H2B clustered histone 21	Homo sapiens	14-19
27913299-2	2017	NQO1 reduces quinones to hydroquinones using NADH as an electron donor and consequently increases the intracellular NAD+/NADH ratio.	Hydroquinones	25-38	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-4
27758861-3	2016	Mechanistically, the electron transfer reaction requires docking of its Rieske iron-sulfur protein (ISP) subunit to the quinol oxidation site (QP) of the complex.	Hydroquinones	120-126	ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1	Homo sapiens	72-98
27502282-5	2016	PA1024 could reduce a broad spectrum of quinone substrates via a Ping Pong Bi Bi steady-state kinetic mechanism, generating the corresponding hydroquinones.	Hydroquinones	142-155	nitronate monooxygenase	Pseudomonas aeruginosa PAO1	0-6
27656164-7	2016	These results lead us to conclude that all quinol species of E. coli can reduce (i.e., activate) the sensor ArcB and all three quinones oxidize (i.e., de-activate) it.	Hydroquinones	43-49	hypothetical protein	Escherichia coli	108-112
27432958-5	2016	bc1-CytcO quinol oxidation-oxygen-reduction activities in mitochondria in which Rcf1 or Rcf2 were removed genetically (strains rcf1Delta and rcf2Delta, respectively).	Hydroquinones	10-16	Rcf1p	Saccharomyces cerevisiae S288C	80-84
27432958-5	2016	bc1-CytcO quinol oxidation-oxygen-reduction activities in mitochondria in which Rcf1 or Rcf2 were removed genetically (strains rcf1Delta and rcf2Delta, respectively).	Hydroquinones	10-16	Rcf2p	Saccharomyces cerevisiae S288C	88-92
26333016-0	2016	Transcriptional and post-translational modifications of B-Raf in quinol-thioether induced tuberous sclerosis renal cell carcinoma.	Hydroquinones	65-71	B-Raf proto-oncogene, serine/threonine kinase	Rattus norvegicus	56-61
26798996-2	2016	In this study, a refined method to determine the specific activity of a single quinol oxidase is exemplarily described for the alternative oxidase (AOX) isoform AOX1A from Arabidopsis thaliana and its corresponding mutants, using the respiratory chain of an Escherichia coli cytochrome bo and bd-I oxidase double mutant as a source to provide electrons necessary for O2 reduction via quinol oxidases.	Hydroquinones	79-85	alternative oxidase 2	Arabidopsis thaliana	127-146
26798996-2	2016	In this study, a refined method to determine the specific activity of a single quinol oxidase is exemplarily described for the alternative oxidase (AOX) isoform AOX1A from Arabidopsis thaliana and its corresponding mutants, using the respiratory chain of an Escherichia coli cytochrome bo and bd-I oxidase double mutant as a source to provide electrons necessary for O2 reduction via quinol oxidases.	Hydroquinones	79-85	alternative oxidase 2	Arabidopsis thaliana	148-151
26798996-2	2016	In this study, a refined method to determine the specific activity of a single quinol oxidase is exemplarily described for the alternative oxidase (AOX) isoform AOX1A from Arabidopsis thaliana and its corresponding mutants, using the respiratory chain of an Escherichia coli cytochrome bo and bd-I oxidase double mutant as a source to provide electrons necessary for O2 reduction via quinol oxidases.	Hydroquinones	79-85	alternative oxidase 1A	Arabidopsis thaliana	161-166
26887982-0	2016	The cannabinoid quinol VCE-004.8 alleviates bleomycin-induced scleroderma and exerts potent antifibrotic effects through peroxisome proliferator-activated receptor-gamma and CB2 pathways.	Hydroquinones	16-22	peroxisome proliferator activated receptor gamma	Mus musculus	121-169
26887982-0	2016	The cannabinoid quinol VCE-004.8 alleviates bleomycin-induced scleroderma and exerts potent antifibrotic effects through peroxisome proliferator-activated receptor-gamma and CB2 pathways.	Hydroquinones	16-22	cannabinoid receptor 2 (macrophage)	Mus musculus	174-177
26887982-4	2016	We have developed a non-thiophilic and chemically stable derivative of the CBD quinol (VCE-004.8) that behaves as a dual agonist of PPARgamma and CB2 receptors, VCE-004.8 inhibited TGFbeta-induced Col1A2 gene transcription and collagen synthesis.	Hydroquinones	79-85	peroxisome proliferator activated receptor gamma	Mus musculus	132-141
26887982-4	2016	We have developed a non-thiophilic and chemically stable derivative of the CBD quinol (VCE-004.8) that behaves as a dual agonist of PPARgamma and CB2 receptors, VCE-004.8 inhibited TGFbeta-induced Col1A2 gene transcription and collagen synthesis.	Hydroquinones	79-85	cannabinoid receptor 2 (macrophage)	Mus musculus	146-149
26887982-4	2016	We have developed a non-thiophilic and chemically stable derivative of the CBD quinol (VCE-004.8) that behaves as a dual agonist of PPARgamma and CB2 receptors, VCE-004.8 inhibited TGFbeta-induced Col1A2 gene transcription and collagen synthesis.	Hydroquinones	79-85	transforming growth factor, beta 1	Mus musculus	181-188
26887982-4	2016	We have developed a non-thiophilic and chemically stable derivative of the CBD quinol (VCE-004.8) that behaves as a dual agonist of PPARgamma and CB2 receptors, VCE-004.8 inhibited TGFbeta-induced Col1A2 gene transcription and collagen synthesis.	Hydroquinones	79-85	collagen, type I, alpha 2	Mus musculus	197-203
23688079-5	2014	In particular, the cytochrome b subunit offers two distinct active sites that can be targeted for inhibition - the quinol oxidation site and the quinone reduction site.	Hydroquinones	115-121	mitochondrially encoded cytochrome b	Homo sapiens	19-31
25151970-9	2014	We further demonstrated that NQO1 mediated reduction to unstable hydroquinones and subsequent redox cycling was important for the activation of the ER stress response and toxicity for both AC and MD.	Hydroquinones	65-78	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	29-33
24884893-1	2014	BACKGROUND NAD(P)H: quinone oxidoreductase 1 (NQO1) plays a central role in catalyzing the two-electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	140-153	NAD(P)H quinone dehydrogenase 1	Homo sapiens	11-44
24884893-1	2014	BACKGROUND NAD(P)H: quinone oxidoreductase 1 (NQO1) plays a central role in catalyzing the two-electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	140-153	NAD(P)H quinone dehydrogenase 1	Homo sapiens	46-50
26245902-2	2015	Its operation involves a large scale movement of a head domain of iron-sulfur protein (ISP-HD), which functionally connects the catalytic quinol oxidation Qo site in cytochrome b with cytochrome c1.	Hydroquinones	138-144	mitochondrially encoded cytochrome b	Homo sapiens	166-178
25602258-1	2015	BACKGROUND:  NAD(P)H: quinone oxidoreductase 1 (NQO1), an obligate two-electron reductase, plays an important role in reducing reactive quinones to less reactive and less toxic hydroquinones.	Hydroquinones	177-190	NAD(P)H quinone dehydrogenase 1	Homo sapiens	13-46
25602258-1	2015	BACKGROUND:  NAD(P)H: quinone oxidoreductase 1 (NQO1), an obligate two-electron reductase, plays an important role in reducing reactive quinones to less reactive and less toxic hydroquinones.	Hydroquinones	177-190	NAD(P)H quinone dehydrogenase 1	Homo sapiens	48-52
24830960-4	2014	NQO1 catalyzes the two-electron reduction of quinones to hydroquinones, thereby preventing the formation of ROS.	Hydroquinones	57-70	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-4
24213850-1	2014	NAD(P)H: quinone oxidoreductase 1 (NQO1) is an important enzyme which can catalyze the two-electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	136-149	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-33
24213850-1	2014	NAD(P)H: quinone oxidoreductase 1 (NQO1) is an important enzyme which can catalyze the two-electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	136-149	NAD(P)H quinone dehydrogenase 1	Homo sapiens	35-39
24447297-5	2014	Furthermore, the effects of quinols on Mtb NDH-2 catalytic activity demonstrate the presence of two binding sites for quinone ligands, one favoring the reduced form and the other favoring the oxidized form.	Hydroquinones	28-35	DExH-box helicase 9	Homo sapiens	43-48
23563617-0	2013	Tandem oxidation-oxidative C-H/C-H cross-coupling: synthesis of arylquinones from hydroquinones.	Hydroquinones	82-95	churchill domain containing 1	Homo sapiens	27-34
23749485-2	2013	NAD(P)H:quinone oxidoreductase 1 (NQO1) is a cytosolic enzyme that catalyzes the two-electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	130-143	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-32
23749485-2	2013	NAD(P)H:quinone oxidoreductase 1 (NQO1) is a cytosolic enzyme that catalyzes the two-electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	130-143	NAD(P)H quinone dehydrogenase 1	Homo sapiens	34-38
23563617-1	2013	A concise and efficient approach to arylquinones from widely available hydroquinones has been developed through a tandem reaction involving the oxidation of hydroquinones and subsequent oxidative C-H/C-H cross-coupling of the resulting quinones with arenes.	Hydroquinones	71-84	churchill domain containing 1	Homo sapiens	196-203
22972504-1	2013	NAD(P)H:quinone oxidoreductase 1 (NQO1) is a cytosolic flavoprotein that catalyzes the two-electron reduction of quinoid compounds into hydroquinones, thus protecting cells from oxidative damage.	Hydroquinones	136-149	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-32
22972504-1	2013	NAD(P)H:quinone oxidoreductase 1 (NQO1) is a cytosolic flavoprotein that catalyzes the two-electron reduction of quinoid compounds into hydroquinones, thus protecting cells from oxidative damage.	Hydroquinones	136-149	NAD(P)H quinone dehydrogenase 1	Homo sapiens	34-38
22940066-4	2012	Similarly, the rate of superoxide production by the complex III site of quinol oxidation (site III(Qo)) was calibrated to the reduction state of endogenous cytochrome b(566).	Hydroquinones	72-78	cytochrome b, mitochondrial	Rattus norvegicus	156-168
23109831-1	2012	NAD(P)H:quinone oxidoreductase 1 (NQO1) catalyses the reduction of quinoid compounds to hydroquinones, preventing the generation of free radicals and reactive oxygen.	Hydroquinones	88-101	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-32
22547613-2	2012	The complex contains two distinct quinone-binding sites, the quinol oxidation site of the bc(1) complex (Q(o)) and the quinone reduction site (Q(i)), located on opposite sides of the membrane within cytochrome b.	Hydroquinones	61-67	CYTB	Plasmodium falciparum	199-211
22458729-3	2012	Spectroscopic characterization of CymA from Shewanella oneidensis strain MR-1 identifies three low-spin His/His co-ordinated c-haems and a single high-spin c-haem with His/H(2)O co-ordination lying adjacent to the quinol-binding site.	Hydroquinones	214-220	cytochrome c	Shewanella oneidensis MR-1	34-38
22458729-7	2012	Spectroscopic studies suggest that CymA requires a non-haem co-factor for quinol oxidation and that the reduced enzyme forms a 1:1 complex with its redox partner Fcc3 (flavocytochrome c3 fumarate reductase).	Hydroquinones	74-80	cytochrome c	Shewanella oneidensis MR-1	35-39
23109831-1	2012	NAD(P)H:quinone oxidoreductase 1 (NQO1) catalyses the reduction of quinoid compounds to hydroquinones, preventing the generation of free radicals and reactive oxygen.	Hydroquinones	88-101	NAD(P)H quinone dehydrogenase 1	Homo sapiens	34-38
21212280-3	2011	In mammalian cells, quinols are proposed to inhibit the thioredoxin/thioredoxin reductase system, which is absent from trypanosomes.	Hydroquinones	20-27	thioredoxin	Homo sapiens	56-67
22984577-2	2012	The 2-electron reduction of quinones to hydroquinones by NQO1 is believed to be a detoxification process since this reaction bypasses the formation of the highly reactive semiquinone.	Hydroquinones	40-53	NAD(P)H quinone dehydrogenase 1	Homo sapiens	57-61
21693435-0	2011	cAMP-dependent cytosolic mislocalization of p27(kip)-cyclin D1 during quinol-thioether-induced tuberous sclerosis renal cell carcinoma.	Hydroquinones	70-76	calcium and integrin binding 1	Rattus norvegicus	44-52
21693435-0	2011	cAMP-dependent cytosolic mislocalization of p27(kip)-cyclin D1 during quinol-thioether-induced tuberous sclerosis renal cell carcinoma.	Hydroquinones	70-76	cyclin D1	Rattus norvegicus	53-62
21479364-1	2011	NAD(P)H:quinone oxidoreductase 1 (NQO1), is a cytosolic flavoenzyme that catalyzes the two-electron reduction of quinones into hydroquinones.	Hydroquinones	127-140	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-32
21479364-1	2011	NAD(P)H:quinone oxidoreductase 1 (NQO1), is a cytosolic flavoenzyme that catalyzes the two-electron reduction of quinones into hydroquinones.	Hydroquinones	127-140	NAD(P)H quinone dehydrogenase 1	Homo sapiens	34-38
21212280-3	2011	In mammalian cells, quinols are proposed to inhibit the thioredoxin/thioredoxin reductase system, which is absent from trypanosomes.	Hydroquinones	20-27	thioredoxin	Homo sapiens	68-79
20873851-0	2010	Scales of oxidation potentials, pK(a), and BDE of various hydroquinones and catechols in DMSO.	Hydroquinones	58-71	homeobox D13	Homo sapiens	43-46
21272324-11	2011	In the cases of cyoA and cydB mutants, arcA, fnr, fur, cydB (for cyoA mutant), and cyoA (for cydB mutant) genes were up-regulated, which may be due to incomplete oxidation of quinol.	Hydroquinones	175-181	arginine deiminase	Escherichia coli	39-43
22393995-1	2011	OBJECTIVE: NAD(P)H: quinone oxidoreductase 1 (NQO1) is a cytosolic flavoprotein that catalyzes the two- electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	149-162	NAD(P)H quinone dehydrogenase 1	Homo sapiens	11-44
22393995-1	2011	OBJECTIVE: NAD(P)H: quinone oxidoreductase 1 (NQO1) is a cytosolic flavoprotein that catalyzes the two- electron reduction of quinoid compounds into hydroquinones.	Hydroquinones	149-162	NAD(P)H quinone dehydrogenase 1	Homo sapiens	46-50
21671859-8	2011	According to different structural features, direct HIF-1 inhibitors are divided into several groups: polyamides, quinols and naphthoquinone spiroketal analogues, shikonin derivatives, epidithiodiketopiperazines, and two representative drugs: echinomycin and bortezomib.	Hydroquinones	113-120	hypoxia inducible factor 1 subunit alpha	Homo sapiens	51-56
20396966-0	2010	Crystal structures of human FIH-1 in complex with quinol family inhibitors.	Hydroquinones	50-56	hypoxia inducible factor 1 subunit alpha inhibitor	Homo sapiens	28-33
20599909-4	2010	Quinols, which due to their Michael acceptor moiety react readily with cysteine residues in selective cellular proteins, are good candidates for potential Nrf2 inducing chemopreventive agents.	Hydroquinones	0-7	NFE2 like bZIP transcription factor 2	Homo sapiens	155-159
20396966-5	2010	Quinol family compounds such as 5-chloro-7-iodo-8-hydroxyquinoline (Clioquinol) have been shown to inhibit the hydroxylation activity of FIH-1.	Hydroquinones	0-6	hypoxia inducible factor 1 subunit alpha inhibitor	Homo sapiens	137-142
19325183-1	2009	Quinol oxidation at center P of the cytochrome bc(1) complex involves bifurcated electron transfer to the Rieske iron-sulfur protein and cytochrome b.	Hydroquinones	0-6	cytochrome b	Saccharomyces cerevisiae S288C	36-48
19830680-2	2010	The molecular mechanisms of PCB toxicity have been attributed to the toxicological properties of its metabolites, such as hydroquinones, formed by cytochrome-P-450 oxidation.	Hydroquinones	122-135	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	147-163
19325183-6	2009	The rate and E(a) of the slow reaction of quinol with oxygen that are observed after cytochrome b is reduced were unaffected by the E272Q substitution, whereas the Y185F mutation modified only its rate.	Hydroquinones	42-48	cytochrome b	Saccharomyces cerevisiae S288C	85-97
19176478-2	2009	The addition of ilicicolin to the oxidized complex resulted in a non-linear inhibition of the extent of cytochrome b reduction by quinol together with a shift of the reduced b(H) heme spectrum, indicating electron transfer between monomers.	Hydroquinones	130-136	cytochrome b	Saccharomyces cerevisiae S288C	104-116
19544866-6	2009	In addition to As(III) oxidation by semiquinone radicals, hydroquinones that were also produced during quinone reduction reduced As(V) to As(III) at neutral and acidic pH values (less than 12%) but not at alkaline pH.	Hydroquinones	58-71	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	129-134
32688810-1	2008	Alternative oxidase (AOX) is a terminal quinol oxidase located in the respiratory electron transport chain that catalyses the oxidation of quinol and the reduction of oxygen to water.	Hydroquinones	40-46	acyl-CoA oxidase 1	Homo sapiens	21-24
18587424-3	2008	PMX464 is a novel thiol-reactive quinol thought to inhibit the Trx/TrxR system.	Hydroquinones	33-39	thioredoxin	Homo sapiens	63-66
18587424-3	2008	PMX464 is a novel thiol-reactive quinol thought to inhibit the Trx/TrxR system.	Hydroquinones	33-39	thioredoxin reductase 1	Homo sapiens	67-71
32688810-1	2008	Alternative oxidase (AOX) is a terminal quinol oxidase located in the respiratory electron transport chain that catalyses the oxidation of quinol and the reduction of oxygen to water.	Hydroquinones	40-46	acyl-CoA oxidase 1	Homo sapiens	0-19
19536200-5	2009	Quinone/quinol malfunction was postulated to activate ArcA, Fur, and PhoB in this study.	Hydroquinones	8-14	arginine deiminase	Escherichia coli	54-58
18635747-11	2008	Minimizing the propensity of BA derivatives to undergo one-electron reduction and glutathione conjugation while maximizing their two-electron reduction to stable Hsp90 inhibitory hydroquinones may be a useful strategy for optimizing the therapeutic index of BAs.	Hydroquinones	179-192	heat shock protein 90 alpha family class A member 1	Homo sapiens	162-167
18471987-2	2008	We review the kinetics of electron transfer and inhibitor binding that reveal functional interactions between the quinol oxidation site at center P and quinone reduction site at center N in opposite monomers in conjunction with electron equilibration between the cytochrome b subunits of the dimer.	Hydroquinones	114-120	mitochondrially encoded cytochrome b	Homo sapiens	263-275
16520231-3	2006	Toxicity arising from the high susceptibility of quinone toward endogenous nucleophiles (Q-TOX) was detected using OxyR(+) cells, in the presence of a nitric oxide donor to promote the quinol oxidation to the corresponding quinone.	Hydroquinones	185-191	thymocyte selection associated high mobility group box	Homo sapiens	91-94
18215069-0	2008	Is cytochrome b glutamic acid 272 a quinol binding residue in the bc1 complex of Saccharomyces cerevisiae?	Hydroquinones	36-42	cytochrome b	Saccharomyces cerevisiae S288C	3-15
16600173-1	2006	The Q-cycle mechanism of the bc1 complex explains how the electron transfer from ubihydroquinone (quinol, QH2) to cytochrome (cyt) c (or c2 in bacteria) is coupled to the pumping of protons across the membrane.	Hydroquinones	98-104	cytochrome c, somatic	Homo sapiens	114-132
16705337-1	2006	Coordination of the carbocyclic ring of hydroquinones to electrophilic transition-metal fragments such as Mn(CO)3+ and Rh(COD)+ produces stable pi-bonded eta6-complexes that are activated to facile reversible deprotonation of the -OH groups.	Hydroquinones	40-53	endothelin receptor type A	Homo sapiens	83-86
16700548-1	2006	NAD(P)H quinone oxidoreductase 1 (NQO1) is a ubiquitous flavoenzyme that catalyzes two-electron reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor.	Hydroquinones	121-134	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-32
16700548-1	2006	NAD(P)H quinone oxidoreductase 1 (NQO1) is a ubiquitous flavoenzyme that catalyzes two-electron reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor.	Hydroquinones	121-134	NAD(P)H quinone dehydrogenase 1	Homo sapiens	34-38
16702380-1	2006	UNLABELLED: NAD(P)H:quinone oxidoreductase 1 (NQO1) is a cytosolic enzyme that catalyzes the two-electron reduction of quinoid compounds into hydroquinones, their less toxic form.	Hydroquinones	142-155	NAD(P)H quinone dehydrogenase 1	Homo sapiens	12-44
16702380-1	2006	UNLABELLED: NAD(P)H:quinone oxidoreductase 1 (NQO1) is a cytosolic enzyme that catalyzes the two-electron reduction of quinoid compounds into hydroquinones, their less toxic form.	Hydroquinones	142-155	NAD(P)H quinone dehydrogenase 1	Homo sapiens	46-50
18454936-2	2008	The extent of this initial cytochrome b reduction corresponded to a level of b(H) heme reduction of 33%-55% depending on the quinol/quinone ratio.	Hydroquinones	125-131	cytochrome b	Saccharomyces cerevisiae S288C	27-39
18180330-0	2008	Thioredoxin reductase inhibition by antitumor quinols: a quinol pharmacophore effect correlating to antiproliferative activity.	Hydroquinones	46-53	peroxiredoxin 5	Homo sapiens	0-21
18180330-0	2008	Thioredoxin reductase inhibition by antitumor quinols: a quinol pharmacophore effect correlating to antiproliferative activity.	Hydroquinones	46-52	peroxiredoxin 5	Homo sapiens	0-21
18180330-5	2008	In this study, we demonstrate that structural analogs containing a quinol pharmacophore inhibited TrxR with potencies correlated with their antiproliferative and cytotoxic efficacies.	Hydroquinones	67-73	peroxiredoxin 5	Homo sapiens	98-102
18180330-6	2008	Benzenesulfonyl-6F-indole-substituted quinol (compound 6) irreversibly inhibited TrxR most strongly with a half-maximal inhibitory concentration of 2.7 microM after 1 h of incubation with recombinant rat TrxR.	Hydroquinones	38-44	peroxiredoxin 5	Homo sapiens	81-85
18180330-6	2008	Benzenesulfonyl-6F-indole-substituted quinol (compound 6) irreversibly inhibited TrxR most strongly with a half-maximal inhibitory concentration of 2.7 microM after 1 h of incubation with recombinant rat TrxR.	Hydroquinones	38-44	peroxiredoxin 5	Homo sapiens	204-208
18180330-8	2008	Moreover, TrxR activity in lysates of HCT 116 cells treated with apoptosis-inducing doses of quinols was significantly reduced.	Hydroquinones	93-100	peroxiredoxin 5	Homo sapiens	10-14
18180330-9	2008	From the results obtained, we propose that TrxR inhibition is a critical cellular event that contributes to the proapoptotic effects of quinols.	Hydroquinones	136-143	peroxiredoxin 5	Homo sapiens	43-47
18272433-0	2008	Quinol type compound in cytochrome c preparations leads to non-enzymatic reduction of cytochrome c during the measurement of complex III activity.	Hydroquinones	0-6	cytochrome c, somatic	Homo sapiens	24-36
18272433-0	2008	Quinol type compound in cytochrome c preparations leads to non-enzymatic reduction of cytochrome c during the measurement of complex III activity.	Hydroquinones	0-6	cytochrome c, somatic	Homo sapiens	86-98
18272433-4	2008	Analysis of cytochrome c (producing a high-background) by fast protein liquid chromatography yielded a contaminant peak containing a lipid extractable component with redox spectra and mass spectroscopy fragmentation suggestive of a quinol.	Hydroquinones	232-238	cytochrome c, somatic	Homo sapiens	12-24
17942934-1	2007	NRH:quinone oxidoreductase 2 (NQO2) is a cytosolic flavoprotein that catalyzes the two-electron reduction of quinones and quinoid compounds to hydroquinones.	Hydroquinones	143-156	N-ribosyldihydronicotinamide quinone reductase 2	Mus musculus	0-28
17942934-1	2007	NRH:quinone oxidoreductase 2 (NQO2) is a cytosolic flavoprotein that catalyzes the two-electron reduction of quinones and quinoid compounds to hydroquinones.	Hydroquinones	143-156	N-ribosyldihydronicotinamide quinone reductase 2	Mus musculus	30-34
17396564-1	2007	Phytogenous flavonoid-containing agents (PFCA) are able to initiate electron flow bypassing the NAD-dependent region of respiratory chain, which is related with the activity of DT-diaphorase catalyzing two-electron reduction of quinones to hydroquinones and hydrogen peroxide in the presence of NADH and oxygen.	Hydroquinones	240-253	NAD(P)H quinone dehydrogenase 1	Homo sapiens	177-190
17008316-2	2006	The quinol oxidase (Q(o)) site in this complex oxidizes a hydroquinone (quinol), reducing two one-electron carriers, a low potential cytochrome b heme and the "Rieske" iron-sulfur cluster.	Hydroquinones	4-10	mitochondrially encoded cytochrome b	Homo sapiens	133-145
17000671-4	2006	EXPERIMENTAL DESIGN: We investigated whether two novel anticancer drugs AJM290 and AW464 (quinols), which inhibit Trx-1 function, can inhibit the HIF pathway.	Hydroquinones	90-97	thioredoxin	Homo sapiens	114-119
16756956-8	2006	In further studies we determined other cellular proteins which bind to an immobilized quinol analog, and identified several proteins including beta-tubulin, heat shock protein 60, and peroxiredoxin 1 as potential molecular targets of quinols that may contribute to their proapoptotic and antiproliferative effects.	Hydroquinones	234-241	peroxiredoxin 1	Homo sapiens	184-199
16417979-13	2006	The 5-LOX and HET-CAM-assays provide good evidence that hydroquinones in the defence fluid of Palembus ocularis have anti-inflammatory properties which would explain the traditional use of this beetle to treat asthma.	Hydroquinones	56-69	calmodulin 3	Homo sapiens	18-21
15312779-1	2004	Cytochrome bc(1) is an integral membrane protein complex essential for cellular respiration and photosynthesis; it couples electron transfer from quinol to cytochrome c to proton translocation across the membrane.	Hydroquinones	146-152	LOC104968582	Bos taurus	156-168
15867391-0	2005	Elucidation of thioredoxin as a molecular target for antitumor quinols.	Hydroquinones	63-70	thioredoxin	Homo sapiens	15-26
15867391-6	2005	Molecular modeling predicted covalent irreversible binding between quinol analogues and cysteine residues 32 and 35 of thioredoxin, thereby inhibiting enzyme activity.	Hydroquinones	67-73	thioredoxin	Homo sapiens	119-130
15867391-10	2005	Results are consistent with a mechanism of action of novel antitumor quinols involving inhibition of the small redox protein thioredoxin.	Hydroquinones	69-76	thioredoxin	Homo sapiens	125-136
15833742-1	2005	The kinetics and extent of cytochrome b reduced by quinol in the presence of variable concentrations of antimycin decreased non-linearly and could only be fitted to a model in which electrons entering through one center N can equilibrate between the two cytochrome b subunits of the bc(1) complex dimer.	Hydroquinones	51-57	cytochrome b	Saccharomyces cerevisiae S288C	27-39
15833742-1	2005	The kinetics and extent of cytochrome b reduced by quinol in the presence of variable concentrations of antimycin decreased non-linearly and could only be fitted to a model in which electrons entering through one center N can equilibrate between the two cytochrome b subunits of the bc(1) complex dimer.	Hydroquinones	51-57	cytochrome b	Saccharomyces cerevisiae S288C	254-266
14993213-1	2004	Previous electron microscopic studies of bacterial RCLH1 complexes demonstrated both circular and elliptical conformations of the LH1 ring, and this implied flexibility has been suggested to allow passage of quinol from the Q(B) site of the RC to the quinone pool prior to reduction of the cytochrome bc(1) complex.	Hydroquinones	208-214	procollagen-lysine,2-oxoglutarate 5-dioxygenase 1	Homo sapiens	53-56
15240547-1	2004	PURPOSE:  NAD(P)H: quinone oxidoreductase (NQO(1)) catalyzes the two-electron reduction of quinones to hydroquinones.	Hydroquinones	103-116	crystallin zeta	Homo sapiens	19-41
15240547-1	2004	PURPOSE:  NAD(P)H: quinone oxidoreductase (NQO(1)) catalyzes the two-electron reduction of quinones to hydroquinones.	Hydroquinones	103-116	NAD(P)H quinone dehydrogenase 1	Homo sapiens	43-49
15157909-7	2004	The data from both experiments, in the system devoid of quinol being the electron donor to cytochrome b(6), suggest that in case of electron transfer from cytochrome f to plastocyanin electron transfer can either bypass cytochrome f or the Rieske iron-sulfur protein can be reduced prior to its movement to the quinol binding site of cytochrome b(6).	Hydroquinones	56-62	mitochondrially encoded cytochrome b	Homo sapiens	91-103
15157909-7	2004	The data from both experiments, in the system devoid of quinol being the electron donor to cytochrome b(6), suggest that in case of electron transfer from cytochrome f to plastocyanin electron transfer can either bypass cytochrome f or the Rieske iron-sulfur protein can be reduced prior to its movement to the quinol binding site of cytochrome b(6).	Hydroquinones	311-317	mitochondrially encoded cytochrome b	Homo sapiens	91-103
15625561-1	2004	Cytochrome b is the central catalytic subunit of the quinol:cytochrome c oxidoreductase of complex III of the mitochondrial oxidative phosphorylation system and is essential to the viability of most eukaryotic cells.	Hydroquinones	53-59	mitochondrially encoded cytochrome b	Homo sapiens	0-12
15102952-8	2004	NQO1 can generate hydroquinones that are redox active, and the O(2)(*)(-) scavenging activity of NQO1 may allow protection against O(2)(*)(-) at the site of hydroquinone generation.	Hydroquinones	18-31	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-4
14503001-4	2003	Three of these enzymes utilize a quinol substrate, with two oxidizing the quinol (AOX and PTOX) and one hydroxylating it (DMQ hydroxylase).	Hydroquinones	33-39	acyl-CoA oxidase 1	Homo sapiens	82-85
14500388-1	2003	NADPH:quinone oxidoreductase (NQO(1)), a homodimeric, ubiquitous, flavoprotein, catalyzes the two-electron reduction of quinones to hydroquinones.	Hydroquinones	132-145	crystallin zeta	Homo sapiens	6-28
14500388-1	2003	NADPH:quinone oxidoreductase (NQO(1)), a homodimeric, ubiquitous, flavoprotein, catalyzes the two-electron reduction of quinones to hydroquinones.	Hydroquinones	132-145	NAD(P)H quinone dehydrogenase 1	Homo sapiens	30-36
12762808-0	2003	New sesquiterpene quinols from a Micronesian sponge, Aka sp.	Hydroquinones	18-25	neurogenin 1	Homo sapiens	53-56
12899636-6	2003	This indicates that no further proteins are required for electron transfer between the quinone pool and fumarate if we assume direct reduction of CymA by quinols.	Hydroquinones	154-161	cytochrome c	Shewanella oneidensis MR-1	146-150
14503001-4	2003	Three of these enzymes utilize a quinol substrate, with two oxidizing the quinol (AOX and PTOX) and one hydroxylating it (DMQ hydroxylase).	Hydroquinones	33-39	coenzyme Q7, hydroxylase	Homo sapiens	122-137
14503001-4	2003	Three of these enzymes utilize a quinol substrate, with two oxidizing the quinol (AOX and PTOX) and one hydroxylating it (DMQ hydroxylase).	Hydroquinones	74-80	acyl-CoA oxidase 1	Homo sapiens	82-85
11809856-1	2002	NAD(P)H:quinone oxidoreductase (NQO1) and dihydronicotinamide riboside:quinone oxidoreductases (NQO2) are cytosolic flavoproteins that catalyze the two-electron reduction of quinones and quinoid compounds to hydroquinones, thereby promoting detoxification and preventing the formation of highly reactive oxygen species, which lead to DNA and cell damage.	Hydroquinones	208-221	crystallin zeta	Homo sapiens	8-30
12270134-5	2002	Inhibition of nSMase by ubiquinols displayed similarities with inhibition by manumycin and the hydroquinones F11334"s, suggesting that these compounds could act as structural analogs of ubiquinol.	Hydroquinones	95-108	sphingomyelin phosphodiesterase 2	Homo sapiens	14-20
12372827-10	2002	Under these conditions quinols are known to produce superoxide, and because mitoQ is localized within the mitochondrial matrix this suggests that production of superoxide in the matrix was sufficient to activate UCP2.	Hydroquinones	23-30	uncoupling protein 2	Rattus norvegicus	212-216
11809856-1	2002	NAD(P)H:quinone oxidoreductase (NQO1) and dihydronicotinamide riboside:quinone oxidoreductases (NQO2) are cytosolic flavoproteins that catalyze the two-electron reduction of quinones and quinoid compounds to hydroquinones, thereby promoting detoxification and preventing the formation of highly reactive oxygen species, which lead to DNA and cell damage.	Hydroquinones	208-221	NAD(P)H quinone dehydrogenase 1	Homo sapiens	32-36
11809856-1	2002	NAD(P)H:quinone oxidoreductase (NQO1) and dihydronicotinamide riboside:quinone oxidoreductases (NQO2) are cytosolic flavoproteins that catalyze the two-electron reduction of quinones and quinoid compounds to hydroquinones, thereby promoting detoxification and preventing the formation of highly reactive oxygen species, which lead to DNA and cell damage.	Hydroquinones	208-221	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	96-100
11700316-4	2002	This stoichiometry was obtained when the inhibitors were titrated in cytochrome c reductase assays and in reactions of quinol with enzyme in which the inhibitors block pre-steady state reduction of cytochrome b.	Hydroquinones	119-125	cytochrome b	Saccharomyces cerevisiae S288C	198-210
11735393-0	2001	Deuterium kinetic isotope effects in the p-side pathway for quinol oxidation by the cytochrome b(6)f complex.	Hydroquinones	60-66	mitochondrially encoded cytochrome b	Homo sapiens	84-96
11697117-0	2001	Superoxide dismutase enhances chain-breaking antioxidant capability of hydroquinones.	Hydroquinones	71-84	superoxide dismutase 1	Homo sapiens	0-20
11248224-1	2001	The enzyme DT-diaphorase mediates the two-electron reduction of quinones to hydroquinones.	Hydroquinones	76-89	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	11-24
11035251-1	2000	An extensive body of evidence supports the conclusion that by catalyzing obligatory two-electron reductions of quinones to hydroquinones, NAD(P)H:quinone reductase (QR1) protects cells against the deleterious effects of redox cycling of quinones, their ability to deplete glutathione, and to produce neoplasia.	Hydroquinones	123-136	crystallin, zeta	Mus musculus	146-163
11035251-1	2000	An extensive body of evidence supports the conclusion that by catalyzing obligatory two-electron reductions of quinones to hydroquinones, NAD(P)H:quinone reductase (QR1) protects cells against the deleterious effects of redox cycling of quinones, their ability to deplete glutathione, and to produce neoplasia.	Hydroquinones	123-136	NAD(P)H dehydrogenase, quinone 1	Mus musculus	165-168
11035252-5	2000	QR2 is also capable of reducing quinones to hydroquinones, but unlike QR1, cannot use NAD(P)H.	Hydroquinones	44-57	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	0-3
11035256-1	2000	DT-diaphorase, also referred to as NQO1 or NAD(P)H: quinone acceptor oxidoreductase, is a flavoprotein that catalyzes the two-electron reduction of quinones and quinonoid compounds to hydroquinones, using either NADH or NADPH as the electron donor.	Hydroquinones	184-197	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-13
10788423-9	2000	Such a movement seems necessary to shuttle electrons from the membrane-soluble quinol to the extramembrane heme of cytochrome c(1).	Hydroquinones	79-85	cytochrome c, somatic	Homo sapiens	115-127