PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
7547240-5	1995	DTD activity was highest in non-small-cell lung (NSCLC)-tumours (mean 123 nmol DCPIP min-1 mg-1), followed by colon carcinoma (mean 75 nmol min-1 mg-1) and squamous cell carcinoma of the head and neck (6-fold lower than NSCLC).	2,6-Dichloroindophenol	79-84	CD59 molecule (CD59 blood group)	Homo sapiens	85-95
8863816-3	1996	In our study, we transfected human NQO1 into Chinese hamster ovary cells that do not normally express NQO1 activity and obtained stable clones that expressed NQO1 activity of 19-3527 nmol of 2,6-dichlorophenolindophenol reduced/min/mg of protein.	2,6-Dichloroindophenol	191-219	NAD(P)H quinone dehydrogenase 1	Homo sapiens	35-39
8702805-8	1996	Calmodulin binding to the recombinant reductase protein increased its rate of NADPH-dependent flavin reduction and its rate of electron transfer to cytochrome c, FeCN6, or dichlorophenolindophenol to fully match the rate increases achieved when calmodulin bound to native full-length nNOS.	2,6-Dichloroindophenol	172-196	calmodulin 1	Rattus norvegicus	0-10
1324836-5	1992	In the presence of a concentration of Ph2I sufficient to fully inhibit O2- production (around 10 nmol/mg membrane protein), addition of catalytic amounts of the redox mediator dichloroindophenol (Cl2Ind) resulted in a by-pass of the electron flow to cytochrome c, the rate of which was about half of that determined in non-inhibited oxidase.	2,6-Dichloroindophenol	176-194	LOC104968582	Bos taurus	250-262
7515050-6	1994	The addition of Ca2+/calmodulin increased cytochrome c reduction from 10-15-fold while stimulating the rate of 2,6-dichlorophenolindophenol and ferricyanide reduction only slightly, if at all.	2,6-Dichloroindophenol	111-139	calmodulin 1	Homo sapiens	21-31
7512584-9	1994	Dichlorophenolindophenol (DPIP), an artificial electron acceptor and an inhibitor of NO formation, totally suppressed NADPH-d staining of neurons, supporting the concept that the NADPH-d of neuron somata is due to nNOS.	2,6-Dichloroindophenol	0-24	nitric oxide synthase 1	Rattus norvegicus	214-218
7512584-9	1994	Dichlorophenolindophenol (DPIP), an artificial electron acceptor and an inhibitor of NO formation, totally suppressed NADPH-d staining of neurons, supporting the concept that the NADPH-d of neuron somata is due to nNOS.	2,6-Dichloroindophenol	26-30	nitric oxide synthase 1	Rattus norvegicus	214-218
8218221-4	1993	Ionization of the basic group has a more pronounced effect on binding of substrate (cytochrome c or dichloroindophenol) than on catalysis, since ionization has only a 2-fold effect on Vmax with cytochrome c, and only a 5-fold effect on Vmax with dichloroindophenol, while (V/K) for both substrates continues to drop at high pH with no sign of reaching a plateau.	2,6-Dichloroindophenol	100-118	cytochrome c, somatic	Homo sapiens	194-206
8218221-4	1993	Ionization of the basic group has a more pronounced effect on binding of substrate (cytochrome c or dichloroindophenol) than on catalysis, since ionization has only a 2-fold effect on Vmax with cytochrome c, and only a 5-fold effect on Vmax with dichloroindophenol, while (V/K) for both substrates continues to drop at high pH with no sign of reaching a plateau.	2,6-Dichloroindophenol	246-264	cytochrome c, somatic	Homo sapiens	84-96
8218221-4	1993	Ionization of the basic group has a more pronounced effect on binding of substrate (cytochrome c or dichloroindophenol) than on catalysis, since ionization has only a 2-fold effect on Vmax with cytochrome c, and only a 5-fold effect on Vmax with dichloroindophenol, while (V/K) for both substrates continues to drop at high pH with no sign of reaching a plateau.	2,6-Dichloroindophenol	246-264	cytochrome c, somatic	Homo sapiens	194-206
8218221-6	1993	It is most likely located on the surface of the protein at the cytochrome c/dichloroindophenol binding site, near the FMN prosthetic group.	2,6-Dichloroindophenol	76-94	cytochrome c, somatic	Homo sapiens	63-75
8229302-6	1993	The enzyme was specific for NADPH as electron donor and had the ability to reduce cytochrome c (15.4 mumol.min-1 x mg protein-1), potassium ferricyanide (4.9 mumol.min-1 x mg protein-1) and 2,6-dichlorophenolindophenol (16.8 mumol.min-1.mg protein-1) as well as aquacobalamin (6.4 mumol.min-1 x mg protein-1).	2,6-Dichloroindophenol	190-218	cytochrome c, somatic	Homo sapiens	82-94
16652965-1	1992	Ferric leghemoglobin reductase (FLbR) from soybean (Glycine max [L.] Merr) nodules catalyzed oxidation of NADH, reduction of ferric leghemoglobin (Lb(+3)), and reduction of dichloroindophenol (diaphorase activity).	2,6-Dichloroindophenol	173-191	leghemoglobin A	Glycine max	7-20
16652965-1	1992	Ferric leghemoglobin reductase (FLbR) from soybean (Glycine max [L.] Merr) nodules catalyzed oxidation of NADH, reduction of ferric leghemoglobin (Lb(+3)), and reduction of dichloroindophenol (diaphorase activity).	2,6-Dichloroindophenol	173-191	leghemoglobin A	Glycine max	132-145
1567482-7	1992	There was formation of electron spin resonance-detectable semiquinoid free radicals upon incubation of diaziquone, doxorubicin and 2,6-dichloroindophenol with TR and NADPH under anaerobic conditions.	2,6-Dichloroindophenol	131-153	peroxiredoxin 5	Rattus norvegicus	159-161
1322732-2	1992	The kinetics of electron-transfer involved in reactions of reduction of 2,6-dichlorophenol indophenol and Fe(CN)3-(6) by L-ascorbic acid and reduction of ferric cytochrome c by both L-ascorbic acid and reduced hydroxylamine oxidoreductase were studied as a function of three parameters: ionic strength, pressure (1-2000 bar) and temperature (4-20 degrees C) using the high-pressure stopped-flow method.	2,6-Dichloroindophenol	72-101	cytochrome c, somatic	Homo sapiens	161-173
1731621-5	1992	The catalytic activities of ETFR and ETFB are comparable when they mediate the transfer of reducing equivalents between medium chain acyl-CoA dehydrogenase and 2,6-dichlorophenolindophenol.	2,6-Dichloroindophenol	160-188	electron transfer flavoprotein subunit beta	Homo sapiens	37-41
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	2,6-Dichloroindophenol	201-229	xanthine dehydrogenase	Homo sapiens	40-62
1551461-2	1992	Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP).	2,6-Dichloroindophenol	231-235	xanthine dehydrogenase	Homo sapiens	40-62
1499270-8	1992	Vmax values of reductase II for the various electron acceptors, namely, 2,6-dichlorophenolindophenol, ferricyanide and cytochrome c through cytochrome b5 were found to be 1.9, 1.8 and 2 times higher than those of reductase I.	2,6-Dichloroindophenol	72-100	cytochrome b5 type A	Homo sapiens	140-153
1370456-4	1992	As with several other lens crystallins of limited phylogenetic distribution, zeta-crystallin has been characterized as an "enzyme/crystallin" based on its ability to reduce catalytically the electron acceptor 2,6-dichlorophenolindophenol.	2,6-Dichloroindophenol	209-237	quinone oxidoreductase	Cavia porcellus	77-92
1899380-16	1991	Further characterization of the product of NQO1 cDNA, which was present at approximately 20-30-fold higher levels in transfected COS cells than the endogenous product in uninduced human Hep-G2 cells indicated that it had very high capacity (greater than 1000-fold over background) to catalyze the reduction of 2.6-dichloroindophenol and menadione.	2,6-Dichloroindophenol	310-332	NAD(P)H quinone dehydrogenase 1	Homo sapiens	43-47
1844913-1	1991	Artificial substrates, including ferricyanide and dichlorophenol indophenol (IP), are frequently used to model the activity of NADPH-cytochrome P-450 reductase, in the xenobiotic-metabolic pathway catalyzed by the P-450 complex.	2,6-Dichloroindophenol	50-75	cytochrome p450 oxidoreductase	Gallus gallus	127-159
1989495-3	1991	zeta-Crystallin exhibited an NADPH-dependent oxidoreductase activity with 2,6-dichlorophenolindophenol (DCIP).	2,6-Dichloroindophenol	74-102	quinone oxidoreductase	Cavia porcellus	0-15
1989495-3	1991	zeta-Crystallin exhibited an NADPH-dependent oxidoreductase activity with 2,6-dichlorophenolindophenol (DCIP).	2,6-Dichloroindophenol	104-108	quinone oxidoreductase	Cavia porcellus	0-15
1989495-4	1991	The NADPH:DCIP oxidoreductase activity of zeta-crystallin exhibits a linear response with increasing protein concentration, and saturation kinetics with NADPH and DCIP.	2,6-Dichloroindophenol	10-14	quinone oxidoreductase	Cavia porcellus	42-57
1458556-7	1992	Quinone reductase activities in soluble extracts of HCT 116-R30A cells for the reduction of dichlorophenol indophenol (DCPIP) and menadione-cytochrome c at optimal pHs were decreased by 95% as compared with those obtained in parent cells.	2,6-Dichloroindophenol	119-124	cytochrome c, somatic	Homo sapiens	140-152
1768430-6	1991	NQR was determined in the cytoplasm of murine skin, liver, and human keratinocytes using 2,6-dichlorophenolindophenol as the substrate.	2,6-Dichloroindophenol	89-117	crystallin zeta	Homo sapiens	0-3
1654286-1	1991	The S9 fraction of MCF-7 human breast carcinoma cells has NAD(P)H (quinone-acceptor) oxidoreductase activity as measured by the reduction of dichlorophenol-indophenol (DCPIP).	2,6-Dichloroindophenol	141-166	thioredoxin reductase 1	Homo sapiens	85-99
1654286-1	1991	The S9 fraction of MCF-7 human breast carcinoma cells has NAD(P)H (quinone-acceptor) oxidoreductase activity as measured by the reduction of dichlorophenol-indophenol (DCPIP).	2,6-Dichloroindophenol	168-173	thioredoxin reductase 1	Homo sapiens	85-99
1691923-7	1990	COS1 cells transfected with NQO2 cDNA showed a 5-7-fold increase in NAD(P)H:quinone oxidoreductase activity as compared to nontransfected cells when either 2,6-dichlorophenolindophenol or menadione was used as substrate.	2,6-Dichloroindophenol	156-184	N-ribosyldihydronicotinamide:quinone reductase 2	Homo sapiens	28-32
1703398-8	1990	It utilized either NADPH or NADH as electron donor at equal efficiency and displayed high activities in reduction of menadione, 1,4-benzoquinone, and 2,6-dichlorophenolindophenol which are typical substrates for DT-diaphorase.	2,6-Dichloroindophenol	150-178	NAD(P)H quinone dehydrogenase 1	Homo sapiens	212-225
1764253-6	1991	We determined NQR in the cytoplasma of murine skin, liver, and human keratinocytes using 2,6-dichlorophenol-indophenol as substrate.	2,6-Dichloroindophenol	89-118	crystallin zeta	Homo sapiens	14-17
1691923-7	1990	COS1 cells transfected with NQO2 cDNA showed a 5-7-fold increase in NAD(P)H:quinone oxidoreductase activity as compared to nontransfected cells when either 2,6-dichlorophenolindophenol or menadione was used as substrate.	2,6-Dichloroindophenol	156-184	crystallin zeta	Homo sapiens	76-98
35266940-1	2022	We describe herein the rational development of an organopolysulfide-based fluorogenic donor of hydrogen sulfide (H2S) DCI-PS, which can be activated by the antioxidant selenoenzyme thioredoxin reductase (TrxR) with concomitant release of the dicyanoisophorone-based near-infrared (NIR) fluorophore.	2,6-Dichloroindophenol	118-124	peroxiredoxin 5	Homo sapiens	181-202
2105732-2	1990	NAD(P)H:quinone oxidoreductase (EC 1.6.99.2; DT-diaphorase) was present in the liver of 18- and 19-day-old chick embryos as assayed both by reduction of resorufin and by the more traditional assay, reduction of 2,6-dichlorophenolindophenol (DCPIP).	2,6-Dichloroindophenol	211-239	crystallin zeta	Gallus gallus	8-30
2105732-2	1990	NAD(P)H:quinone oxidoreductase (EC 1.6.99.2; DT-diaphorase) was present in the liver of 18- and 19-day-old chick embryos as assayed both by reduction of resorufin and by the more traditional assay, reduction of 2,6-dichlorophenolindophenol (DCPIP).	2,6-Dichloroindophenol	211-239	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	45-58
2105732-2	1990	NAD(P)H:quinone oxidoreductase (EC 1.6.99.2; DT-diaphorase) was present in the liver of 18- and 19-day-old chick embryos as assayed both by reduction of resorufin and by the more traditional assay, reduction of 2,6-dichlorophenolindophenol (DCPIP).	2,6-Dichloroindophenol	241-246	crystallin zeta	Gallus gallus	8-30
2105732-2	1990	NAD(P)H:quinone oxidoreductase (EC 1.6.99.2; DT-diaphorase) was present in the liver of 18- and 19-day-old chick embryos as assayed both by reduction of resorufin and by the more traditional assay, reduction of 2,6-dichlorophenolindophenol (DCPIP).	2,6-Dichloroindophenol	241-246	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	45-58
2113031-12	1990	Both the DTT-dependent reduction of vitamin K1 epoxide and quinone, and the reduction of DCPIP by purified DT-diaphorase were inhibited by dicoumarol, warfarin, lapachol, and sulphaquinoxaline.	2,6-Dichloroindophenol	89-94	NAD(P)H quinone dehydrogenase 1	Homo sapiens	107-120
35266940-1	2022	We describe herein the rational development of an organopolysulfide-based fluorogenic donor of hydrogen sulfide (H2S) DCI-PS, which can be activated by the antioxidant selenoenzyme thioredoxin reductase (TrxR) with concomitant release of the dicyanoisophorone-based near-infrared (NIR) fluorophore.	2,6-Dichloroindophenol	118-124	peroxiredoxin 5	Homo sapiens	204-208
35266940-5	2022	Considering the overexpression of mammalian TrxR in cancer cells, the turn-on fluorogenic H2S donation process from the cellular non-toxic DCI-PS was validated in a representative breast cancer cell line (MDA-MB-231) for the sustained donation of H2S with concomitant release of the red-emitting NIR fluorophore.	2,6-Dichloroindophenol	139-145	peroxiredoxin 5	Homo sapiens	44-48
35266940-6	2022	The TrxR-triggered fluorescence turn-on process in DCI-PS was further supported by the significant inhibition of the fluorogenic process in the presence of TrxR-selective small-molecule inhibitors and by the significant binding affinity predicted by the protein-ligand docking study.	2,6-Dichloroindophenol	51-57	peroxiredoxin 5	Homo sapiens	4-8
35266940-6	2022	The TrxR-triggered fluorescence turn-on process in DCI-PS was further supported by the significant inhibition of the fluorogenic process in the presence of TrxR-selective small-molecule inhibitors and by the significant binding affinity predicted by the protein-ligand docking study.	2,6-Dichloroindophenol	51-57	peroxiredoxin 5	Homo sapiens	156-160
15092450-2	1989	After the oxidants have been quantitatively destroyed by a mixture of NaNO(2) and NaHCO(3), the horse-serum cholinesterase catalyses the hydrolysis of the orange-red 2,6-dichloro-indophenyl acetate producing the blue 2,6-dichloroindophenol.	2,6-Dichloroindophenol	217-239	butyrylcholinesterase	Homo sapiens	108-122
2496944-6	1989	The two reductases were catalytically active in reducing cytochrome c, ferricyanide and dichlorophenolindophenol, and in supporting rabbit liver cytochrome P450 Form 4 metabolism of 2-acetylaminofluorene.	2,6-Dichloroindophenol	88-112	cytochrome c	Oryctolagus cuniculus	57-69
3542040-8	1986	The addition of low concentrations of DCIP to both wild-type and mutant mitochondria reduced with succinate in the presence of antimycin resulted in a rapid oxidation of cytochrome b perhaps by the pathway involving center o, which does not require coenzyme Q.	2,6-Dichloroindophenol	38-42	cytochrome b	Saccharomyces cerevisiae S288C	170-182
2844120-0	1988	Reduction of exogenous quinones and 2,6-dichlorophenol indophenol in cytochrome b-deficient yeast mitochondria: a differential effect on center i and center o of the cytochrome b-c1 complex.	2,6-Dichloroindophenol	36-65	cytochrome b	Saccharomyces cerevisiae S288C	69-81
2844120-0	1988	Reduction of exogenous quinones and 2,6-dichlorophenol indophenol in cytochrome b-deficient yeast mitochondria: a differential effect on center i and center o of the cytochrome b-c1 complex.	2,6-Dichloroindophenol	36-65	cytochrome b	Saccharomyces cerevisiae S288C	166-178
3508132-1	1987	Micromolar amounts of superoxide dismutase (SOD) or parabenzoquinone (PBQ) inhibit the membrane-bound myoinositol dehydrogenase of Bacillus pumilus strain 5 in the mode of this enzyme transferring electrons to 2,6-dichlorophenol indophenol (DCPIP).	2,6-Dichloroindophenol	241-246	AKO65_RS13780	Bacillus pumilus	22-42
3508132-1	1987	Micromolar amounts of superoxide dismutase (SOD) or parabenzoquinone (PBQ) inhibit the membrane-bound myoinositol dehydrogenase of Bacillus pumilus strain 5 in the mode of this enzyme transferring electrons to 2,6-dichlorophenol indophenol (DCPIP).	2,6-Dichloroindophenol	241-246	AKO65_RS13780	Bacillus pumilus	44-47
3114017-3	1987	The Km values of colonic cytochrome P-450 reductase for the artificial electron acceptors cytochrome c, ferricyanide, and dichlorophenolindophenol and the electron donor NADPH are 6, 50, 11 and 11 microM, respectively.	2,6-Dichloroindophenol	122-146	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	25-41
3114017-3	1987	The Km values of colonic cytochrome P-450 reductase for the artificial electron acceptors cytochrome c, ferricyanide, and dichlorophenolindophenol and the electron donor NADPH are 6, 50, 11 and 11 microM, respectively.	2,6-Dichloroindophenol	122-146	cytochrome c, somatic	Homo sapiens	90-102
3003077-9	1986	NADPH-dependent reductions of ferricyanide or 2,6-dichloroindophenol catalyzed by glutathione reductase are also markedly influenced by NADP+.	2,6-Dichloroindophenol	46-68	glutathione-disulfide reductase	Homo sapiens	82-103
3032917-2	1986	Essentially all of the stimulation-specific DCIP reduction under aerobic conditions could be inhibited when high concentrations of superoxide dismutase (SOD), about 10 times those usually used to inhibit the superoxide (O-2)-mediated cytochrome c reduction, were used.	2,6-Dichloroindophenol	44-48	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	131-151
3032917-2	1986	Essentially all of the stimulation-specific DCIP reduction under aerobic conditions could be inhibited when high concentrations of superoxide dismutase (SOD), about 10 times those usually used to inhibit the superoxide (O-2)-mediated cytochrome c reduction, were used.	2,6-Dichloroindophenol	44-48	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	153-156
3032917-3	1986	SOD inhibited the DCIP reduction by chemically generated O2- in the same manner as the stimulation-specific DCIP reduction by the macrophage F2, and the concentration of SOD necessary for 50% inhibition was about 10 times that for the reduction of cytochrome c. Under anaerobic conditions, however, the NADPH oxidase could reduce DCIP, though the rate was slow because we could not use a sufficiently high DCIP concentration.	2,6-Dichloroindophenol	18-22	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	0-3
3032917-3	1986	SOD inhibited the DCIP reduction by chemically generated O2- in the same manner as the stimulation-specific DCIP reduction by the macrophage F2, and the concentration of SOD necessary for 50% inhibition was about 10 times that for the reduction of cytochrome c. Under anaerobic conditions, however, the NADPH oxidase could reduce DCIP, though the rate was slow because we could not use a sufficiently high DCIP concentration.	2,6-Dichloroindophenol	18-22	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	170-173
3032917-3	1986	SOD inhibited the DCIP reduction by chemically generated O2- in the same manner as the stimulation-specific DCIP reduction by the macrophage F2, and the concentration of SOD necessary for 50% inhibition was about 10 times that for the reduction of cytochrome c. Under anaerobic conditions, however, the NADPH oxidase could reduce DCIP, though the rate was slow because we could not use a sufficiently high DCIP concentration.	2,6-Dichloroindophenol	108-112	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	170-173
3032917-3	1986	SOD inhibited the DCIP reduction by chemically generated O2- in the same manner as the stimulation-specific DCIP reduction by the macrophage F2, and the concentration of SOD necessary for 50% inhibition was about 10 times that for the reduction of cytochrome c. Under anaerobic conditions, however, the NADPH oxidase could reduce DCIP, though the rate was slow because we could not use a sufficiently high DCIP concentration.	2,6-Dichloroindophenol	108-112	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	170-173
3032917-3	1986	SOD inhibited the DCIP reduction by chemically generated O2- in the same manner as the stimulation-specific DCIP reduction by the macrophage F2, and the concentration of SOD necessary for 50% inhibition was about 10 times that for the reduction of cytochrome c. Under anaerobic conditions, however, the NADPH oxidase could reduce DCIP, though the rate was slow because we could not use a sufficiently high DCIP concentration.	2,6-Dichloroindophenol	108-112	superoxide dismutase [Mn], mitochondrial	Cavia porcellus	170-173
2421769-5	1986	DT-diaphorase-type activity is also observed on the cell surface employing dichloroindophenol as external electron acceptor and it is found to be a dicoumarol-sensitive NADH dehydrogenase.	2,6-Dichloroindophenol	75-93	NAD(P)H quinone dehydrogenase 1	Homo sapiens	0-13
3000647-1	1985	Procedures are described for the estimation of the succinate:ubiquinone oxidoreductase and succinate:phenazine methosulfate oxidoreductase activities in post-nuclear supernatants of human skeletal muscle homogenates using 2,6-dichlorophenol indophenol as the terminal electron acceptor.	2,6-Dichloroindophenol	222-251	hydroxysteroid 17-beta dehydrogenase 6	Homo sapiens	124-138
6626606-2	1983	In the cyanide-inhibited submitochondrial particles of bovine heart, HOQNO strongly stimulates cytochrome b reduction by ascorbate in the presence of redox mediators, e. g. N,N,N",N"-tetramethylparaphenylene diamine, 2,6-dichlorophenolindophenol, diaminodurol and phenazine methosulfate; this effect can be reversed by antimycin.	2,6-Dichloroindophenol	217-245	cytochrome b	Bos taurus	95-107
6433885-2	1984	The results presented in this paper show that the degree of inhibition by Ant2p of the photosystem 2-supported electron transfer reactions, registered by the light-dependent rate of dichlorophenolindophenol reduction, varies according to the actinic light intensity.	2,6-Dichloroindophenol	182-206	solute carrier family 25 member 6	Homo sapiens	74-79
6093877-9	1984	The identical specific activity employing dichloroindophenol as an electron acceptor with NADH or NADPH as donor indicate a DT-diaphorase (EC 1.6.99.2) like activity in the astrocytes plasma membrane.	2,6-Dichloroindophenol	42-60	NAD(P)H quinone dehydrogenase 1	Homo sapiens	124-137
6798728-1	1981	The paper deals with the influence of 1-(o-chlorophenyl)-1-(p-chlorophenyl)-2.2-dichloroethane (o,p"-DDD, chloditane) on NADPH-dependent reduction of cytochrome c, ferricyanide, 2,6-dichlorophenolindophenol and neotetrazolium; 156 and 312 mumol o,p"-DDD was added to the dog adrenal mitochondrial and microsomal suspension.	2,6-Dichloroindophenol	178-206	cytochrome c, somatic	Canis lupus familiaris	150-162
7150582-1	1982	A significant lag in the thenoyltrifluoroacetone (TTFA)-sensitive succinate: ubiquinone reductase activity was observed when a ubiquinone-deficient resolved preparation of the enzyme was assayed in the presence of exogenous ubiquinone-2 (Q2) and 2,6-dichlorophenolindophenol.	2,6-Dichloroindophenol	246-274	NADH:ubiquinone oxidoreductase subunit A5	Homo sapiens	77-97
4462558-3	1974	Turkey liver xanthine dehydrogenase engaged in catalysing the oxidation of xanthine by dichlorophenol-indophenol was progressively inactivated by methanol.	2,6-Dichloroindophenol	87-112	xanthine dehydrogenase/oxidase	Meleagris gallopavo	13-35
202259-3	1977	from the oxidation of adrenaline to adrenochrome catalysed by NADPH--cytochrome c reductase proceeds independently of the interaction of the enzyme with the artificial anaerobic acceptors cytochrome c or 2,6-dichlorophenol-indophenol.	2,6-Dichloroindophenol	204-233	cytochrome c, somatic	Homo sapiens	69-81
1165247-4	1975	The reduced cytochrome P-450 donates 2 electrons to dichlorophenolindophenol or to cytochrome c.	2,6-Dichloroindophenol	52-76	cytochrome P-450	Oryctolagus cuniculus	12-28
33045951-4	2020	A detailed kinetic mechanism has now been developed for the diaphorase (NADH-dehydrogenase) reaction catalyzed by pig heart LADH using 2,6-dichlorophenol-indophenol (DCPIP) as a model quinone electron acceptor.	2,6-Dichloroindophenol	135-164	dihydrolipoamide dehydrogenase	Sus scrofa	124-128
4138934-0	1973	[Is 2,6-dichlorophenolindophenol a specific inhibitor of catalase?].	2,6-Dichloroindophenol	4-32	catalase	Homo sapiens	57-66
33424902-6	2020	ProDH does not use NAD+ as electron acceptor but can be assayed with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCPIP) after detergent-mediated solubilization or enrichment of mitochondria.	2,6-Dichloroindophenol	102-130	proline dehydrogenase 1	Homo sapiens	0-5
33424902-6	2020	ProDH does not use NAD+ as electron acceptor but can be assayed with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCPIP) after detergent-mediated solubilization or enrichment of mitochondria.	2,6-Dichloroindophenol	132-137	proline dehydrogenase 1	Homo sapiens	0-5
33122156-4	2020	Emodin binds to the active site of the enzyme and acts as a competitive inhibitor with respect to 2, 6-Dichlorophenolindophenol, a known substrate of NADPH-Quinone reductase.	2,6-Dichloroindophenol	98-127	crystallin zeta	Rattus norvegicus	150-173
32615144-7	2020	We determined that the reaction between Tsa2-C170S-Cys-SOH and ascorbate proceeded with a rate constant of 1.40 +- 0.08 x 103 M-1 s-1 through a competition assay developed here, employing 2,6-dichlorophenol-indophenol (DCPIP).	2,6-Dichloroindophenol	188-217	radial spoke head component 1	Homo sapiens	40-44
32615144-7	2020	We determined that the reaction between Tsa2-C170S-Cys-SOH and ascorbate proceeded with a rate constant of 1.40 +- 0.08 x 103 M-1 s-1 through a competition assay developed here, employing 2,6-dichlorophenol-indophenol (DCPIP).	2,6-Dichloroindophenol	219-224	radial spoke head component 1	Homo sapiens	40-44
33045951-4	2020	A detailed kinetic mechanism has now been developed for the diaphorase (NADH-dehydrogenase) reaction catalyzed by pig heart LADH using 2,6-dichlorophenol-indophenol (DCPIP) as a model quinone electron acceptor.	2,6-Dichloroindophenol	166-171	dihydrolipoamide dehydrogenase	Sus scrofa	124-128
33045951-5	2020	Anaerobic stopped-flow experiments show that two-electron reduced LADH is 15-25-fold less active towards DCPIP reduction than four-electron reduced enzyme, or Zn2+-modified reduced LADH (the corresponding values of the rate constants are (6.5 +- 1.5) x 103 M-1 s-1, (9 +- 2) x 104 M-1 s-1, and (1.6 +- 0.5) x 105 M-1 s-1, respectively).	2,6-Dichloroindophenol	105-110	dihydrolipoamide dehydrogenase	Sus scrofa	66-70
32180910-2	2020	Methods: Diagnosis of G6PD deficiency was made by using the Di-chloroindophenol Dye test in two south west districts (Kalahandi and Rayagada) of Odisha State.	2,6-Dichloroindophenol	60-79	glucose-6-phosphate dehydrogenase	Homo sapiens	22-26
32449408-1	2020	The dichlorophenol-indophenol (DCIP) test and microcolumn chromatography are simple methods commonly used for screening of Hb E (HBB: c.79G>A) in Thailand.	2,6-Dichloroindophenol	4-29	hemoglobin subunit epsilon 1	Homo sapiens	123-127
32449408-1	2020	The dichlorophenol-indophenol (DCIP) test and microcolumn chromatography are simple methods commonly used for screening of Hb E (HBB: c.79G>A) in Thailand.	2,6-Dichloroindophenol	31-35	hemoglobin subunit epsilon 1	Homo sapiens	123-127
32449408-1	2020	The dichlorophenol-indophenol (DCIP) test and microcolumn chromatography are simple methods commonly used for screening of Hb E (HBB: c.79G>A) in Thailand.	2,6-Dichloroindophenol	31-35	hemoglobin subunit beta	Homo sapiens	129-132
31081204-7	2019	As expected, substrate-reduced Dld2 very slowly reacted with oxygen or the artificial electron acceptor 2,6-dichlorophenol indophenol.	2,6-Dichloroindophenol	104-133	D-lactate dehydrogenase	Saccharomyces cerevisiae S288C	31-35
31915438-1	2019	In the present work, the usefulness of cetyltrimethylammonium bromide-modified palm oil fiber (CTAB-modified POF) for the removal of indigo carmine (IC) and 2,6-dichlorophenolindophenol (2,6-DCPIP) from aqueous solutions was investigated.	2,6-Dichloroindophenol	157-185	POF1B actin binding protein	Homo sapiens	109-112
31915438-1	2019	In the present work, the usefulness of cetyltrimethylammonium bromide-modified palm oil fiber (CTAB-modified POF) for the removal of indigo carmine (IC) and 2,6-dichlorophenolindophenol (2,6-DCPIP) from aqueous solutions was investigated.	2,6-Dichloroindophenol	187-196	POF1B actin binding protein	Homo sapiens	109-112
31915438-3	2019	The adsorption studies of IC and 2,6-DCPIP were performed in batch mode using CTAB-modified POF.	2,6-Dichloroindophenol	33-42	POF1B actin binding protein	Homo sapiens	92-95
30267443-8	2019	Reduced Irc15p is oxidized by several artificial electron acceptors such as potassium ferricyanide, 2,6-dichlorophenol-indophenol, 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide, and menadione.	2,6-Dichloroindophenol	100-129	Irc15p	Saccharomyces cerevisiae S288C	8-14
29487133-5	2018	We found that the most potent BLVRB inhibitors contain a tricyclic hydrocarbon core structure similar to the isoalloxazine ring of flavin mononucleotide and that both xanthene- and acridine-based compounds inhibit BLVRB"s flavin and dichlorophenolindophenol (DCPIP) reductase functions.	2,6-Dichloroindophenol	233-257	biliverdin reductase B	Homo sapiens	30-35
30532176-4	2018	In this study, the M. gallisepticum pyruvate dehydrogenase E1 alpha subunit (PDHA) and beta subunit (PDHB) were expressed in Escherichia coli, and their enzymatic activities were identified based on 2,6-dichlorophenol indophenol reduction.	2,6-Dichloroindophenol	199-228	pyruvate dehydrogenase (lipoamide) beta	Gallus gallus	101-105
29487133-5	2018	We found that the most potent BLVRB inhibitors contain a tricyclic hydrocarbon core structure similar to the isoalloxazine ring of flavin mononucleotide and that both xanthene- and acridine-based compounds inhibit BLVRB"s flavin and dichlorophenolindophenol (DCPIP) reductase functions.	2,6-Dichloroindophenol	259-264	biliverdin reductase B	Homo sapiens	30-35
26091888-8	2015	In addition, comparison with DESI-MS analyses (the Zare and Latour laboratories published results suggesting accessible reaction times <1 ms) of the reduction of dichlorophenolindophenol by L-ascorbic acid suggest that TM (1) -DESI can access reaction times less than 1 ms.	2,6-Dichloroindophenol	165-189	desumoylating isopeptidase 2	Homo sapiens	29-33
26091888-8	2015	In addition, comparison with DESI-MS analyses (the Zare and Latour laboratories published results suggesting accessible reaction times <1 ms) of the reduction of dichlorophenolindophenol by L-ascorbic acid suggest that TM (1) -DESI can access reaction times less than 1 ms.	2,6-Dichloroindophenol	165-189	desumoylating isopeptidase 2	Homo sapiens	230-234
21034357-0	2011	DCPIP (2,6-dichlorophenolindophenol) as a genotype-directed redox chemotherapeutic targeting NQO1*2 breast carcinoma.	2,6-Dichloroindophenol	0-5	NAD(P)H quinone dehydrogenase 1	Homo sapiens	93-97
23535164-7	2013	Succinate dehydrogenase activity was measured by spectrophotometric analysis of 2,6-dichloroindophenol reduction for 20 minutes as the relative change in absorbance over time.	2,6-Dichloroindophenol	80-102	aminoadipate-semialdehyde synthase	Mus musculus	0-23
21296895-4	2011	Lung homogenate cytosol NQO1 activities were 97 +- 11, 54 +- 6, and 5 +- 1 (SE) nmol dichlorophenolindophenol reduced min(-1) mg protein(-1) for NQO1(+/+), NQO1(+/-), and NQO1(-/-) lungs, respectively.	2,6-Dichloroindophenol	85-109	NAD(P)H dehydrogenase, quinone 1	Mus musculus	24-28
21296895-4	2011	Lung homogenate cytosol NQO1 activities were 97 +- 11, 54 +- 6, and 5 +- 1 (SE) nmol dichlorophenolindophenol reduced min(-1) mg protein(-1) for NQO1(+/+), NQO1(+/-), and NQO1(-/-) lungs, respectively.	2,6-Dichloroindophenol	85-109	NAD(P)H dehydrogenase, quinone 1	Mus musculus	145-149
21296895-4	2011	Lung homogenate cytosol NQO1 activities were 97 +- 11, 54 +- 6, and 5 +- 1 (SE) nmol dichlorophenolindophenol reduced min(-1) mg protein(-1) for NQO1(+/+), NQO1(+/-), and NQO1(-/-) lungs, respectively.	2,6-Dichloroindophenol	85-109	NAD(P)H dehydrogenase, quinone 1	Mus musculus	145-149
21296895-4	2011	Lung homogenate cytosol NQO1 activities were 97 +- 11, 54 +- 6, and 5 +- 1 (SE) nmol dichlorophenolindophenol reduced min(-1) mg protein(-1) for NQO1(+/+), NQO1(+/-), and NQO1(-/-) lungs, respectively.	2,6-Dichloroindophenol	85-109	NAD(P)H dehydrogenase, quinone 1	Mus musculus	145-149
26547963-4	2015	It was found that the sensitivity of cells to the cytotoxic effect of DCPIP was inversely proportional to the basal level of DT-diaphorase activity and accompanied by its activation with subsequent inhibition at non-toxic and toxic concentrations, respectively.	2,6-Dichloroindophenol	70-75	NAD(P)H quinone dehydrogenase 1	Rattus norvegicus	125-138
24595403-2	2014	Cytokinin dehydrogenase from Zea mays (ZmCKX1) was immobilised concurrently with electrodeposition of a silica gel film on the surface of a Pt microelectrode, which was further functionalized by free electron mediator 2,6-dichlorophenolindophenol (DCPIP) in supporting electrolyte to give a bioactive film capable of selective oxidative cleavage of the N6- side chain of cytokinins.	2,6-Dichloroindophenol	218-246	cytokinin dehydrogenase 1	Zea mays	39-45
24595403-2	2014	Cytokinin dehydrogenase from Zea mays (ZmCKX1) was immobilised concurrently with electrodeposition of a silica gel film on the surface of a Pt microelectrode, which was further functionalized by free electron mediator 2,6-dichlorophenolindophenol (DCPIP) in supporting electrolyte to give a bioactive film capable of selective oxidative cleavage of the N6- side chain of cytokinins.	2,6-Dichloroindophenol	248-253	cytokinin dehydrogenase 1	Zea mays	39-45
21034357-0	2011	DCPIP (2,6-dichlorophenolindophenol) as a genotype-directed redox chemotherapeutic targeting NQO1*2 breast carcinoma.	2,6-Dichloroindophenol	7-35	NAD(P)H quinone dehydrogenase 1	Homo sapiens	93-97
21034357-4	2011	In a panel of cultured breast carcinoma cell lines and NQO1-transfectants with differential NQO1 expression levels, homozygous NQO1*2 MDA-MB231 cells were hypersensitive to DCPIP-induced caspase-independent cell death that occurred after early onset of oxidative stress with glutathione depletion and loss of genomic integrity.	2,6-Dichloroindophenol	173-178	NAD(P)H quinone dehydrogenase 1	Homo sapiens	55-59
21034357-4	2011	In a panel of cultured breast carcinoma cell lines and NQO1-transfectants with differential NQO1 expression levels, homozygous NQO1*2 MDA-MB231 cells were hypersensitive to DCPIP-induced caspase-independent cell death that occurred after early onset of oxidative stress with glutathione depletion and loss of genomic integrity.	2,6-Dichloroindophenol	173-178	NAD(P)H quinone dehydrogenase 1	Homo sapiens	92-96
21034357-4	2011	In a panel of cultured breast carcinoma cell lines and NQO1-transfectants with differential NQO1 expression levels, homozygous NQO1*2 MDA-MB231 cells were hypersensitive to DCPIP-induced caspase-independent cell death that occurred after early onset of oxidative stress with glutathione depletion and loss of genomic integrity.	2,6-Dichloroindophenol	173-178	NAD(P)H quinone dehydrogenase 1	Homo sapiens	92-96
19394313-0	2009	Antimelanoma activity of the redox dye DCPIP (2,6-dichlorophenolindophenol) is antagonized by NQO1.	2,6-Dichloroindophenol	39-44	NAD(P)H quinone dehydrogenase 1	Homo sapiens	94-98
20625147-5	2010	Moreover, 2,6-dichlorophenolindophenol (DCIP), a reducing agent that accepts electrons from the ETC coupled to H(+) extrusion, made P. aeruginosa susceptible to hLf and hTf in anaerobiosis.	2,6-Dichloroindophenol	10-38	HLF transcription factor, PAR bZIP family member	Homo sapiens	161-164
20625147-5	2010	Moreover, 2,6-dichlorophenolindophenol (DCIP), a reducing agent that accepts electrons from the ETC coupled to H(+) extrusion, made P. aeruginosa susceptible to hLf and hTf in anaerobiosis.	2,6-Dichloroindophenol	40-44	HLF transcription factor, PAR bZIP family member	Homo sapiens	161-164
19487014-2	2009	The substrate of acetylthiocholine is hydrolysed by the cholinesterase (ChE) from soil animal pheretima, and the produced thiocholine reacts with the 2,6-DCIP to give obvious shift of electrochemical signal.	2,6-Dichloroindophenol	150-158	butyrylcholinesterase	Homo sapiens	56-70
19487014-2	2009	The substrate of acetylthiocholine is hydrolysed by the cholinesterase (ChE) from soil animal pheretima, and the produced thiocholine reacts with the 2,6-DCIP to give obvious shift of electrochemical signal.	2,6-Dichloroindophenol	150-158	butyrylcholinesterase	Homo sapiens	72-75
19883924-4	2010	The recombinant enzymes reduced cytochrome c, ferricyanide and dichlorophenolindophenol (DCPIP) in an NADPH-dependent manner, and supported the activity of CYP73A25, a cinnamate 4-hydroxylase of cotton.	2,6-Dichloroindophenol	63-87	cytochrome c	Gossypium hirsutum	32-44
19883924-4	2010	The recombinant enzymes reduced cytochrome c, ferricyanide and dichlorophenolindophenol (DCPIP) in an NADPH-dependent manner, and supported the activity of CYP73A25, a cinnamate 4-hydroxylase of cotton.	2,6-Dichloroindophenol	89-94	cytochrome c	Gossypium hirsutum	32-44
19394313-0	2009	Antimelanoma activity of the redox dye DCPIP (2,6-dichlorophenolindophenol) is antagonized by NQO1.	2,6-Dichloroindophenol	46-74	NAD(P)H quinone dehydrogenase 1	Homo sapiens	94-98
19394313-4	2009	In A375 cells displaying low NQO1 activity, DCPIP induced apoptosis with procaspase-3 and PARP cleavage, whereas G361 cells expressing high levels of enzymatically active NQO1 were resistant to DCPIP-cytotoxicity.	2,6-Dichloroindophenol	44-49	NAD(P)H quinone dehydrogenase 1	Homo sapiens	29-33
19394313-4	2009	In A375 cells displaying low NQO1 activity, DCPIP induced apoptosis with procaspase-3 and PARP cleavage, whereas G361 cells expressing high levels of enzymatically active NQO1 were resistant to DCPIP-cytotoxicity.	2,6-Dichloroindophenol	44-49	caspase 3	Homo sapiens	73-85
19394313-4	2009	In A375 cells displaying low NQO1 activity, DCPIP induced apoptosis with procaspase-3 and PARP cleavage, whereas G361 cells expressing high levels of enzymatically active NQO1 were resistant to DCPIP-cytotoxicity.	2,6-Dichloroindophenol	44-49	collagen type XI alpha 2 chain	Homo sapiens	90-94
19394313-6	2009	DCPIP-cytotoxicity was associated with the induction of oxidative stress and rapid depletion of glutathione in A375 and NQO1-modulated G361 cells.	2,6-Dichloroindophenol	0-5	NAD(P)H quinone dehydrogenase 1	Homo sapiens	120-124
19394313-9	2009	These findings suggest feasibility of targeting tumors that display low NQO1 enzymatic activity using DCPIP.	2,6-Dichloroindophenol	102-107	NAD(P)H quinone dehydrogenase 1	Homo sapiens	72-76
19381374-4	2009	DCIP UVB dosimeter films exhibit a response that is related to the irradiance level and duration of UVB exposure, the level of SnO(2) present and to a lesser extent the level of glycerol present.	2,6-Dichloroindophenol	0-4	strawberry notch homolog 1	Homo sapiens	127-130
11772017-1	2002	The neuronal nitric oxide synthase (nNOS) basal and calmodulin- (CaM-) stimulated reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) follow ping-pong mechanisms [Wolthers and Schimerlik (2001) Biochemistry 40, 4722-4737].	2,6-Dichloroindophenol	95-117	nitric oxide synthase 1	Homo sapiens	36-40
16249336-5	2005	The reduction of the artificial electron acceptors cytochrome c, 2,6-dichlorophenolindophenol, and ferricyanide was inhibited by the addition of any of these C termini to CYPOR, whereas the reduction of molecular O(2) was increased.	2,6-Dichloroindophenol	65-93	cytochrome p450 oxidoreductase	Homo sapiens	171-176
15706061-5	2004	The XTC-UC1 cell line exhibited enhanced activity with respect to control of dicoumarol-sensitive DCIP reduction, identified with membrane bound DT-diaphorase, whereas dicoumarol insensitive DCIP reduction was not significantly changed.	2,6-Dichloroindophenol	98-102	NAD(P)H quinone dehydrogenase 1	Homo sapiens	145-158
11772018-1	2002	The pH dependence of basal and calmodulin- (CaM-) stimulated neuronal nitric oxide synthase (nNOS) reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) was investigated.	2,6-Dichloroindophenol	112-134	calmodulin 1	Homo sapiens	31-41
11772018-1	2002	The pH dependence of basal and calmodulin- (CaM-) stimulated neuronal nitric oxide synthase (nNOS) reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) was investigated.	2,6-Dichloroindophenol	112-134	calmodulin 1	Homo sapiens	44-47
18980384-5	2008	The A129T MSR mutant transfers electrons to ferricyanide as efficiently as wild type MSR but the rate of cytochrome c, 2,6-dichloroindophenol, and menadione reduction is decreased 10-15 fold.	2,6-Dichloroindophenol	119-141	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	10-13
15812859-0	2005	Interference of laccase in determination of cellobiose dehydrogenase activity of Pleurotus ostreatus (Florida) using dichlorophenol indophenol as the electron acceptor.	2,6-Dichloroindophenol	117-142	choline dehydrogenase	Homo sapiens	44-68
15812859-6	2005	Therefore, caution is needed to measure CDH activity by monitoring DPIP reduction in a system where laccase is likely to be present.	2,6-Dichloroindophenol	67-71	choline dehydrogenase	Homo sapiens	40-43
15558951-1	2004	Succinate-cytochrome c reductase was inhibited in vitro and in vivo by phenobarbitone, aminophylline and neostigmine using both 2,6-dichlorophenolindophenol (DCIP) and cytochrome c (cyt c) as substrates.	2,6-Dichloroindophenol	128-156	cytochrome c, somatic	Homo sapiens	10-22
15558951-1	2004	Succinate-cytochrome c reductase was inhibited in vitro and in vivo by phenobarbitone, aminophylline and neostigmine using both 2,6-dichlorophenolindophenol (DCIP) and cytochrome c (cyt c) as substrates.	2,6-Dichloroindophenol	158-162	cytochrome c, somatic	Homo sapiens	10-22
12637268-7	2003	Hydrogen peroxide partially inactivated the molybdenum center of XOR, as shown by a parallel decrease in XOR-catalyzed xanthine oxidation and dichlorophenolindophenol reduction.	2,6-Dichloroindophenol	142-166	xanthine dehydrogenase	Homo sapiens	65-68
11772018-1	2002	The pH dependence of basal and calmodulin- (CaM-) stimulated neuronal nitric oxide synthase (nNOS) reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) was investigated.	2,6-Dichloroindophenol	112-134	nitric oxide synthase 1	Homo sapiens	93-97
11772018-1	2002	The pH dependence of basal and calmodulin- (CaM-) stimulated neuronal nitric oxide synthase (nNOS) reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) was investigated.	2,6-Dichloroindophenol	136-140	calmodulin 1	Homo sapiens	31-41
11772018-1	2002	The pH dependence of basal and calmodulin- (CaM-) stimulated neuronal nitric oxide synthase (nNOS) reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) was investigated.	2,6-Dichloroindophenol	136-140	calmodulin 1	Homo sapiens	44-47
11772018-1	2002	The pH dependence of basal and calmodulin- (CaM-) stimulated neuronal nitric oxide synthase (nNOS) reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) was investigated.	2,6-Dichloroindophenol	136-140	nitric oxide synthase 1	Homo sapiens	93-97
11772017-1	2002	The neuronal nitric oxide synthase (nNOS) basal and calmodulin- (CaM-) stimulated reduction of 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) follow ping-pong mechanisms [Wolthers and Schimerlik (2001) Biochemistry 40, 4722-4737].	2,6-Dichloroindophenol	119-123	nitric oxide synthase 1	Homo sapiens	36-40
10978532-5	2000	The protein has glycolate oxidase activity in vitro, as measured by the reduction of 2, 6-dichlorophenolindophenol in the presence of flavin mononucleotide and glycolate.	2,6-Dichloroindophenol	85-114	hydroxyacid oxidase 2	Homo sapiens	16-33
9305729-4	1997	The nitrate reductase contains 1 mol FAD per mole of enzyme and also reduces cytochrome c or dichlorophenol indophenol with NADH as the electron donor.	2,6-Dichloroindophenol	93-118	cytochrome c, somatic	Homo sapiens	77-89
10232828-3	1999	These reductions are inhibited by the thiol blocking agent N-ethylmaleimide and by the strong inhibitors of the thioredoxin reductase (TR) 2-chloro-2,4-nitrobenzene and 2,6-dichloroindophenol.	2,6-Dichloroindophenol	169-191	peroxiredoxin 5	Homo sapiens	112-133
10232828-3	1999	These reductions are inhibited by the thiol blocking agent N-ethylmaleimide and by the strong inhibitors of the thioredoxin reductase (TR) 2-chloro-2,4-nitrobenzene and 2,6-dichloroindophenol.	2,6-Dichloroindophenol	169-191	peroxiredoxin 5	Homo sapiens	135-137
10333077-1	1999	The commonly used assay for measuring cellobiose dehydrogenase (CDH) activity, based on the reduction of dichlorophenol-indophenol (DCIP), has been adapted to measure this enzyme activity in the presence of laccase, which is often formed concurrently with CDH by a number of fungi.	2,6-Dichloroindophenol	105-130	choline dehydrogenase	Homo sapiens	38-62
10333077-1	1999	The commonly used assay for measuring cellobiose dehydrogenase (CDH) activity, based on the reduction of dichlorophenol-indophenol (DCIP), has been adapted to measure this enzyme activity in the presence of laccase, which is often formed concurrently with CDH by a number of fungi.	2,6-Dichloroindophenol	105-130	choline dehydrogenase	Homo sapiens	64-67
10333077-1	1999	The commonly used assay for measuring cellobiose dehydrogenase (CDH) activity, based on the reduction of dichlorophenol-indophenol (DCIP), has been adapted to measure this enzyme activity in the presence of laccase, which is often formed concurrently with CDH by a number of fungi.	2,6-Dichloroindophenol	132-136	choline dehydrogenase	Homo sapiens	38-62
10333077-1	1999	The commonly used assay for measuring cellobiose dehydrogenase (CDH) activity, based on the reduction of dichlorophenol-indophenol (DCIP), has been adapted to measure this enzyme activity in the presence of laccase, which is often formed concurrently with CDH by a number of fungi.	2,6-Dichloroindophenol	132-136	choline dehydrogenase	Homo sapiens	64-67
10333077-1	1999	The commonly used assay for measuring cellobiose dehydrogenase (CDH) activity, based on the reduction of dichlorophenol-indophenol (DCIP), has been adapted to measure this enzyme activity in the presence of laccase, which is often formed concurrently with CDH by a number of fungi.	2,6-Dichloroindophenol	132-136	choline dehydrogenase	Homo sapiens	256-259
10198089-2	1999	Acyl-coenzyme A dehydrogenase (ACAD) (EC 1.3.99.2,3) activity was detected in purified mitochondria from maize (Zea mays L.) root tips and from embryonic axes of early-germinating sunflower (Helianthus annuus L.) seeds, using as the enzyme assay the reduction of 2,6-dichlorophenolindophenol, with phenazine methosulfate as the intermediate electron carrier.	2,6-Dichloroindophenol	264-292	acyl-CoA dehydrogenase short chain	Homo sapiens	32-36
9073351-3	1997	This is followed by specific counterstaining of glutathione reductase with dichlorophenolindophenol/nitroblue tetrazolium.	2,6-Dichloroindophenol	75-99	glutathione-disulfide reductase	Homo sapiens	48-69