PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
15950210-11	2005	Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols.	9,10-phenanthrenequinone	6-13	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	23-28
17847711-2	2007	9,10-Phenanthrenequinone (9,10-PQ) and 1,2-naphthoquinone (1,2-NQ), which are contained in diesel exhaust particles (DEPs), potently inhibited 20alpha-HSD activity in liver cytosol.	9,10-phenanthrenequinone	0-24	aldo-keto reductase family 1, member C18	Mus musculus	143-154
17847711-2	2007	9,10-Phenanthrenequinone (9,10-PQ) and 1,2-naphthoquinone (1,2-NQ), which are contained in diesel exhaust particles (DEPs), potently inhibited 20alpha-HSD activity in liver cytosol.	9,10-phenanthrenequinone	26-33	aldo-keto reductase family 1, member C18	Mus musculus	143-154
17082565-6	2007	We found that both acenaphthenequinone (AcQ) and 9,10-phenanthrenequinone (PQ) enhanced ROS generation and that AcQ translocated NF-kappaB from the cytosol to the nucleus.	9,10-phenanthrenequinone	75-77	nuclear factor kappa B subunit 1	Homo sapiens	129-138
16164454-9	2005	PQ exhibited adjuvant activity for the allergen-specific production of IgG1 and IgE.	9,10-phenanthrenequinone	0-2	LOC105243590	Mus musculus	71-75
15950210-0	2005	The interactions of 9,10-phenanthrenequinone with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a potential site for toxic actions.	9,10-phenanthrenequinone	20-44	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	50-90
15950210-0	2005	The interactions of 9,10-phenanthrenequinone with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a potential site for toxic actions.	9,10-phenanthrenequinone	20-44	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	92-97
15950210-3	2005	As part of a continuing study of the interactions of quinones with biological systems, we have examined the susceptibility of GAPDH to inactivation by 9,10-phenanthrenequinone (9,10-PQ).	9,10-phenanthrenequinone	151-175	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	126-131
15950210-3	2005	As part of a continuing study of the interactions of quinones with biological systems, we have examined the susceptibility of GAPDH to inactivation by 9,10-phenanthrenequinone (9,10-PQ).	9,10-phenanthrenequinone	177-184	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	126-131
15950210-5	2005	In this study, the effects of 9,10-PQ on GAPDH were examined in detail under aerobic and anaerobic conditions so that the role of oxygen could be distinguished from the direct effects of the quinone.	9,10-phenanthrenequinone	30-37	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	41-46
15950210-6	2005	The results indicate that, in the presence of the reducing agent DTT, GAPDH inhibition by 9,10-PQ under aerobic conditions was mostly indirect and comparable to the direct actions of exogenously-added H2O2 on this enzyme.	9,10-phenanthrenequinone	90-97	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	70-75
15950210-7	2005	GAPDH was also inhibited by 9,10-PQ anaerobically, but in a somewhat more complex manner.	9,10-phenanthrenequinone	28-35	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-5
15950210-11	2005	Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols.	9,10-phenanthrenequinone	6-13	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	115-120
15950210-11	2005	Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols.	9,10-phenanthrenequinone	6-13	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	115-120
12604216-8	2003	Bacterially expressed recombinant HTSP protein showed small but significant activity towards 9,10-phenanthrenequinone among the putative substrates so far tested.	9,10-phenanthrenequinone	93-117	aldo-keto reductase family 1 member E2	Homo sapiens	34-38
15629867-0	2005	9,10-Phenanthraquinone in diesel exhaust particles downregulates Cu,Zn-SOD and HO-1 in human pulmonary epithelial cells: intracellular iron scavenger 1,10-phenanthroline affords protection against apoptosis.	9,10-phenanthrenequinone	0-22	superoxide dismutase 1	Homo sapiens	65-74
15629867-0	2005	9,10-Phenanthraquinone in diesel exhaust particles downregulates Cu,Zn-SOD and HO-1 in human pulmonary epithelial cells: intracellular iron scavenger 1,10-phenanthroline affords protection against apoptosis.	9,10-phenanthrenequinone	0-22	heme oxygenase 1	Homo sapiens	79-83
15629867-1	2005	9,10-Phenanthraquinone (PQ), a major quinone contained in diesel exhaust particles and atmospheric PM(2.5), undergoes one-electron reduction by flavin enzymes such as NADPH-cytochrome P450 reductase, leading to production of reactive oxygen species in vitro.	9,10-phenanthrenequinone	0-22	cytochrome p450 oxidoreductase	Homo sapiens	167-198
15629867-1	2005	9,10-Phenanthraquinone (PQ), a major quinone contained in diesel exhaust particles and atmospheric PM(2.5), undergoes one-electron reduction by flavin enzymes such as NADPH-cytochrome P450 reductase, leading to production of reactive oxygen species in vitro.	9,10-phenanthrenequinone	24-26	cytochrome p450 oxidoreductase	Homo sapiens	167-198
15629867-7	2005	Furthermore, treatment of A549 cells with 10-20 microM PQ for 12 h specifically down-regulated protein levels of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) and heme oxygenase-1 (HO-1) by more than 50%.	9,10-phenanthrenequinone	55-57	superoxide dismutase 1	Homo sapiens	113-139
15629867-7	2005	Furthermore, treatment of A549 cells with 10-20 microM PQ for 12 h specifically down-regulated protein levels of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) and heme oxygenase-1 (HO-1) by more than 50%.	9,10-phenanthrenequinone	55-57	superoxide dismutase 1	Homo sapiens	141-150
15629867-7	2005	Furthermore, treatment of A549 cells with 10-20 microM PQ for 12 h specifically down-regulated protein levels of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) and heme oxygenase-1 (HO-1) by more than 50%.	9,10-phenanthrenequinone	55-57	heme oxygenase 1	Homo sapiens	156-172
15629867-7	2005	Furthermore, treatment of A549 cells with 10-20 microM PQ for 12 h specifically down-regulated protein levels of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) and heme oxygenase-1 (HO-1) by more than 50%.	9,10-phenanthrenequinone	55-57	heme oxygenase 1	Homo sapiens	174-178
15629867-9	2005	The inhibitor of Cu,Zn-SOD, diethyldithiocarbamate, enhanced the toxic effects of 5 microM PQ.	9,10-phenanthrenequinone	91-93	superoxide dismutase 1	Homo sapiens	17-26
15629867-10	2005	The present findings suggest that PQ causes iron-mediated oxidative damage that is exacerbated by the concomitant down-regulation of Cu,Zn-SOD.	9,10-phenanthrenequinone	34-36	superoxide dismutase 1	Homo sapiens	133-142
15669044-8	2005	Phenanthraquinone induced the lung expression of interleukin (IL)-5 and eotaxin 48 h and 24 h after the challenge, respectively.	9,10-phenanthrenequinone	0-17	interleukin 5	Mus musculus	49-67
15669044-8	2005	Phenanthraquinone induced the lung expression of interleukin (IL)-5 and eotaxin 48 h and 24 h after the challenge, respectively.	9,10-phenanthrenequinone	0-17	chemokine (C-C motif) ligand 11	Mus musculus	72-79
15669044-9	2005	These results indicate that intratracheal exposure to phenanthraquinone induces recruitment of inflammatory cells, at least partly, through the local expression of IL-5 and eotaxin.	9,10-phenanthrenequinone	54-71	interleukin 5	Mus musculus	164-168
15669044-9	2005	These results indicate that intratracheal exposure to phenanthraquinone induces recruitment of inflammatory cells, at least partly, through the local expression of IL-5 and eotaxin.	9,10-phenanthrenequinone	54-71	chemokine (C-C motif) ligand 11	Mus musculus	173-180
15310246-2	2004	PHCR has the ability to catalyze efficiently the reduction of 9,10-phenanthrenequinone (PQ) contained in diesel exhaust particles (DEPs).	9,10-phenanthrenequinone	62-86	dehydrogenase/reductase SDR family member 4	Sus scrofa	0-4
15310246-2	2004	PHCR has the ability to catalyze efficiently the reduction of 9,10-phenanthrenequinone (PQ) contained in diesel exhaust particles (DEPs).	9,10-phenanthrenequinone	88-90	dehydrogenase/reductase SDR family member 4	Sus scrofa	0-4
15310246-6	2004	These results indicate that PQ inhibits the reduction of 4-BP and all-trans-retinal by acting PHCR present in pig heart cytosol.	9,10-phenanthrenequinone	28-30	dehydrogenase/reductase SDR family member 4	Sus scrofa	94-98
15310246-8	2004	The absorbance of cytochrome c at 550 nm was increased with the time by adding PQ, and the increased absorbance was decreased in the presence of superoxide dismutase.	9,10-phenanthrenequinone	79-81	cytochrome c	Sus scrofa	18-30
15310246-10	2004	On the basis of these results, it is concluded that PQ not only inhibits the reduction of 4-BP and all-trans-retinal catalyzed by PHCR but also mediates superoxide formation through its redox cycling involved in PHCR.	9,10-phenanthrenequinone	52-54	dehydrogenase/reductase SDR family member 4	Sus scrofa	130-134
15310246-10	2004	On the basis of these results, it is concluded that PQ not only inhibits the reduction of 4-BP and all-trans-retinal catalyzed by PHCR but also mediates superoxide formation through its redox cycling involved in PHCR.	9,10-phenanthrenequinone	52-54	dehydrogenase/reductase SDR family member 4	Sus scrofa	212-216
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	263-280	nitric oxide synthase 3	Rattus norvegicus	290-305
11404275-0	2001	Phenanthraquinone inhibits eNOS activity and suppresses vasorelaxation.	9,10-phenanthrenequinone	0-17	nitric oxide synthase 3	Rattus norvegicus	27-31
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	263-280	nitric oxide synthase 3	Rattus norvegicus	307-311
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	34-51	nitric oxide synthase 1	Rattus norvegicus	129-159
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	34-51	nitric oxide synthase 1	Rattus norvegicus	161-165
11404275-8	2001	The present findings suggest that phenanthraquinone has a potent inhibitory action on eNOS activity via a similar mechanism reported for nNOS, thereby causing the suppression of NO-mediated vasorelaxation and elevation of blood pressure.	9,10-phenanthrenequinone	34-51	nitric oxide synthase 3	Rattus norvegicus	86-90
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	34-51	nitric oxide synthase 3	Rattus norvegicus	290-305
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	34-51	nitric oxide synthase 3	Rattus norvegicus	307-311
11404275-8	2001	The present findings suggest that phenanthraquinone has a potent inhibitory action on eNOS activity via a similar mechanism reported for nNOS, thereby causing the suppression of NO-mediated vasorelaxation and elevation of blood pressure.	9,10-phenanthrenequinone	34-51	nitric oxide synthase 1	Rattus norvegicus	137-141
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	263-280	nitric oxide synthase 1	Rattus norvegicus	129-159
11356112-3	2001	A number of 9,10-phenanthrenediones were identified that reversibly inhibited CD45-mediated p-nitrophenyl phosphate (pNPP) hydrolysis.	9,10-phenanthrenequinone	12-35	protein tyrosine phosphatase receptor type C	Homo sapiens	78-82
11404275-2	2001	Since we reported previously that phenanthraquinone, an environmental chemical contained in diesel exhaust particles, suppresses neuronal nitric oxide synthase (nNOS) activity by shunting electrons away from the normal catalytic pathway, it was hypothesized that phenanthraquinone inhibits endothelial NOS (eNOS) activity and affects vascular tone.	9,10-phenanthrenequinone	263-280	nitric oxide synthase 1	Rattus norvegicus	161-165
9692994-4	1998	Surprisingly, Y55F and Y55S mutants of 3alpha-HSD reduced 9,10-PQ with high kcat values.	9,10-phenanthrenequinone	58-65	aldo-keto reductase family 1 member C4	Homo sapiens	39-49
10510318-4	1999	Also, AKR7A2 was found to exhibit a narrow substrate specificity, with activity being restricted to succinic semialdehyde (SSA), 2-nitrobenzaldehyde, pyridine-2-aldehyde, isatin, 1,2-naphthoquinone (1,2-NQ) and 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	211-235	aldo-keto reductase family 7 member A2	Homo sapiens	6-12
10622721-2	1999	The human PGFS catalyzed the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2.	9,10-phenanthrenequinone	74-93	aldo-keto reductase family 1 member C3	Homo sapiens	10-14
10622721-2	1999	The human PGFS catalyzed the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2.	9,10-phenanthrenequinone	95-97	aldo-keto reductase family 1 member C3	Homo sapiens	10-14
9625728-5	1998	Partial purification of the enzymes which are responsible for reducing PQ in 20000g supernatant of rat cerebellum by anion-exchange column chromatography indicated that one catalyst for PQ reduction was nNOS.	9,10-phenanthrenequinone	71-73	nitric oxide synthase 1	Rattus norvegicus	203-207
9625728-7	1998	nNOS effectively reduced the quinones as well as PQ causing a marked decrease in the production of NO from l-arginine, while 1, 4-benzoquinone, 9,10-anthraquinone, mitomycin C, and lapachol, which show negligible inhibitory action on nNOS activity, were poor substrates for the enzyme on reduction.	9,10-phenanthrenequinone	49-51	nitric oxide synthase 1	Rattus norvegicus	0-4
9625728-5	1998	Partial purification of the enzymes which are responsible for reducing PQ in 20000g supernatant of rat cerebellum by anion-exchange column chromatography indicated that one catalyst for PQ reduction was nNOS.	9,10-phenanthrenequinone	186-188	nitric oxide synthase 1	Rattus norvegicus	203-207
9625728-7	1998	nNOS effectively reduced the quinones as well as PQ causing a marked decrease in the production of NO from l-arginine, while 1, 4-benzoquinone, 9,10-anthraquinone, mitomycin C, and lapachol, which show negligible inhibitory action on nNOS activity, were poor substrates for the enzyme on reduction.	9,10-phenanthrenequinone	49-51	nitric oxide synthase 1	Rattus norvegicus	234-238
9625728-8	1998	These results indicate that PQ and other quinones used in the present study interact with the NADPH-cytochrome P450 reductase domain on nNOS and thus probably inhibit NO formation by shunting electrons away from the normal catalytic pathway.	9,10-phenanthrenequinone	28-30	nitric oxide synthase 1	Rattus norvegicus	136-140
9625728-6	1998	Reductase activity of PQ by purified nNOS required CaCl2/calmodulin and was markedly suppressed by the flavoprotein inhibitor diphenyleneiodonium but not by l-nitroarginine which is a specific inhibitor for NO formation.	9,10-phenanthrenequinone	22-24	nitric oxide synthase 1	Rattus norvegicus	37-41
9625728-6	1998	Reductase activity of PQ by purified nNOS required CaCl2/calmodulin and was markedly suppressed by the flavoprotein inhibitor diphenyleneiodonium but not by l-nitroarginine which is a specific inhibitor for NO formation.	9,10-phenanthrenequinone	22-24	calmodulin 1	Rattus norvegicus	57-67
8665510-5	1996	The immunodepletion experiments also revealed the presence of at least one other inducible carbonyl-reducing enzyme that, like AFAR, can metabolize 9,10-phenanthraquinone.	9,10-phenanthrenequinone	148-170	aldo-keto reductase family 7 member A3	Rattus norvegicus	127-131
1378964-3	1992	Synthesized GAA was separated by HPLC and detected fluorometrically after reacting with 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	88-112	alpha glucosidase	Rattus norvegicus	12-15
8579568-1	1996	Guinea pig lens zeta-crystallin showed hyperbolic saturation curves with 9,10-phenanthrenequinone (PAQ).	9,10-phenanthrenequinone	73-97	quinone oxidoreductase	Cavia porcellus	16-31
8579568-1	1996	Guinea pig lens zeta-crystallin showed hyperbolic saturation curves with 9,10-phenanthrenequinone (PAQ).	9,10-phenanthrenequinone	99-102	quinone oxidoreductase	Cavia porcellus	16-31
8579568-3	1996	Whereas camel lens zeta-crystallin showed hyperbolic saturation curves only with PAQ and NADPH, but slightly segmoidal with juglone.	9,10-phenanthrenequinone	81-84	quinone oxidoreductase	Cavia porcellus	19-34
8579568-5	1996	The catalytic center activity (Kcat) values indicated that camel zeta-crystallin catalyzed the reduction of PAQ more efficiently than the guinea pig lens zeta-crystallin, although the Km values of the two enzymes for this quinone were very similar.	9,10-phenanthrenequinone	108-111	quinone oxidoreductase	Cavia porcellus	65-80
7811392-6	1994	A number of phenanthrene derivatives having a 9-hydroxy or 9-keto substituent, namely phenanthrenequinone, 6(5H)-phenanthridinone and 9-phenanthrol are potent inhibitors of bovine heart cAK (IC50 values 8, 10 and 10 microM, respectively) and of MLCK (IC50 values 6, 53 and 10 microM, respectively).	9,10-phenanthrenequinone	86-105	myosin light chain kinase, smooth muscle	Bos taurus	245-249
8615688-4	1996	Since 19 alpha-estradiol is a competitive inhibitor of 9,10-phenanthrenequinone by the 17beta-hydroxysteroid dehydrogenase, it is likely that both reactions occur at the same active site on the enzyme.	9,10-phenanthrenequinone	55-79	hydroxysteroid 17-beta dehydrogenase 7	Homo sapiens	87-122
8526867-2	1995	This enzyme, designated AFAR, displays high activity towards dicarbonyl-containing compounds with ketone groups on adjacent carbon atoms; 9,10-phenanthrenequinone, acenaphthenequinone and camphorquinone were found to be good substrates.	9,10-phenanthrenequinone	138-162	aldo-keto reductase family 7 member A3	Rattus norvegicus	24-28
8526867-5	1995	Determination of the apparent Km reveals that AFAR has highest affinity for 9,10-phenanthrenequinone and succinic semialdehyde, and low affinity for glyoxal and DL-glyceraldehyde.	9,10-phenanthrenequinone	76-100	aldo-keto reductase family 7 member A3	Rattus norvegicus	46-50
7515872-3	1994	Transfection of the 3 alpha-HSD cDNA in Simian COS7 cells resulted in the expression of an immunoreactive protein to the antibodies against the purified enzyme, and the transfected cells exhibited activities for not only 7 alpha-hydroxy-5 beta-cholestan-3-one, the intermediate of bile acid biosynthesis, but also steroid hormones and 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	335-359	aldo-keto reductase family 1, member C14	Rattus norvegicus	20-31
7685581-3	1993	In a buffer containing 1% albumin and 10 microM quinone, 9,10-phenanthrenequinone is reduced most rapidly by the carbonyl reductase, 2-methyl-1,4-naphthoquinone is reduced most rapidly by the rat enzyme, and 3,6-pyrenequinone is reduced most rapidly by the Clostridium enzyme.	9,10-phenanthrenequinone	57-81	dehydrogenase/reductase 4	Rattus norvegicus	113-131
34391839-0	2021	9,10-Phenanthrenequinone provokes dysfunction of brain endothelial barrier through down-regulating expression of claudin-5.	9,10-phenanthrenequinone	0-24	claudin 5	Homo sapiens	113-122
34391839-5	2021	Immunofluorescence observation and Western blotting analysis also revealed that the 9,10-PQ treatment remarkably down-regulated the intercellular localization and expression of claudin-5 (CLDN5), a tight junctional protein that plays a key role in function of the blood-brain barrier, and the down-regulation was markedly recovered by pretreatment with a proteasome inhibitor Z-Leu-Leu-Leu-CHO.	9,10-phenanthrenequinone	84-91	claudin 5	Homo sapiens	177-186
34391839-5	2021	Immunofluorescence observation and Western blotting analysis also revealed that the 9,10-PQ treatment remarkably down-regulated the intercellular localization and expression of claudin-5 (CLDN5), a tight junctional protein that plays a key role in function of the blood-brain barrier, and the down-regulation was markedly recovered by pretreatment with a proteasome inhibitor Z-Leu-Leu-Leu-CHO.	9,10-phenanthrenequinone	84-91	claudin 5	Homo sapiens	188-193
34391839-6	2021	This result may indicate that sublethal concentrations of 9,10-PQ facilitate the dysfunction of the endothelial cell barrier through lowering in the expression and proteasomal proteolysis of CLDN5.	9,10-phenanthrenequinone	58-65	claudin 5	Homo sapiens	191-196
34391839-7	2021	The treatment with 9,10-PQ promoted nitric oxide (NO) production presumably through the induction of inducible NO synthase.	9,10-phenanthrenequinone	19-26	nitric oxide synthase 2	Homo sapiens	101-122
34391839-8	2021	In addition, the 9,10-PQ-mediated down-regulation of CLDN5 was ameliorated and deteriorated by pretreating with a scavenger and donor, respectively, of NO.	9,10-phenanthrenequinone	17-24	claudin 5	Homo sapiens	53-58
34391839-9	2021	Similarly to the 9,10-PQ treatment, treatment with a donor of peroxynitrite, a highly reactive oxidant formed by the reaction of NO and superoxide anion, resulted in the marked reduction of CLDN5 expression and elevation of 26S proteasome-based proteolytic activities.	9,10-phenanthrenequinone	17-24	claudin 5	Homo sapiens	190-195
7108550-1	1982	Guanidino compounds in CSF of 57 human subjects were determined fluorometrically after reaction with phenanthrenequinone in alkali solution, using HPLC.	9,10-phenanthrenequinone	101-120	colony stimulating factor 2	Homo sapiens	23-26
6584903-6	1984	For example, phenanthrenequinone was converted to a nonmutagenic metabolite in a cytochrome P-450-dependent reaction, whereas danthron was converted to a highly mutagenic metabolite.	9,10-phenanthrenequinone	13-32	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	81-97
2910843-12	1989	The PGH2 9,11-endoperoxide reductase activity of aldehyde reductase was not affected in the presence of a substrate such as p-nitrobenzaldehyde, DL-glyceraldehyde, or 9,10-phenanthrenequinone, suggesting that PGH2 9,11-endoperoxide and other substrates are reduced at different active site(s).	9,10-phenanthrenequinone	167-191	aldo-keto reductase family 1 member A1	Homo sapiens	49-67
33483563-6	2021	Substrate screening suggested that VAT-1 possesses oxidoreductase activity against quinones such as 1,2-naphthoquinone and 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	123-147	vesicle amine transport 1	Homo sapiens	35-40
33483563-6	2021	Substrate screening suggested that VAT-1 possesses oxidoreductase activity against quinones such as 1,2-naphthoquinone and 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	123-147	thioredoxin reductase 1	Homo sapiens	51-65
32493877-7	2020	Pretreatment with polyethylene glycol conjugated with CAT (PEG-CAT) abolished 9,10-PQ-generated H2O2 production and significantly blocked the activation of EGFR-ERK1/2 signaling by 9,10-PQ, indicating the involvement of H2O2 in the activation because scavenging agents for hydroxyl radicals had no effect on the redox signal activation.	9,10-phenanthrenequinone	181-188	epidermal growth factor receptor	Homo sapiens	156-160
32493877-0	2020	Redox cycling of 9,10-phenanthrenequinone activates epidermal growth factor receptor signaling through S-oxidation of protein tyrosine phosphatase 1B.	9,10-phenanthrenequinone	17-41	epidermal growth factor receptor	Homo sapiens	52-84
32493877-0	2020	Redox cycling of 9,10-phenanthrenequinone activates epidermal growth factor receptor signaling through S-oxidation of protein tyrosine phosphatase 1B.	9,10-phenanthrenequinone	17-41	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	118-149
32493877-3	2020	The current study examined whether 9,10-PQ could activate epidermal growth factor receptor (EGFR) signaling in A431 cells through S-oxidation of its negative regulators such as protein tyrosine phosphatase (PTP) 1B.	9,10-phenanthrenequinone	35-42	epidermal growth factor receptor	Homo sapiens	58-90
32493877-3	2020	The current study examined whether 9,10-PQ could activate epidermal growth factor receptor (EGFR) signaling in A431 cells through S-oxidation of its negative regulators such as protein tyrosine phosphatase (PTP) 1B.	9,10-phenanthrenequinone	35-42	epidermal growth factor receptor	Homo sapiens	92-96
32493877-4	2020	9,10-PQ oxidized recombinant human PTP1B at Cys215 and inhibited its catalytic activity, an effect that was blocked by catalase (CAT), whereas cis-9,10-dihydroxy-9,10-dihydrophenanthrene (DDP), which lacks redox cycling activity, had no effect on PTP1B activity.	9,10-phenanthrenequinone	0-7	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	35-40
32493877-4	2020	9,10-PQ oxidized recombinant human PTP1B at Cys215 and inhibited its catalytic activity, an effect that was blocked by catalase (CAT), whereas cis-9,10-dihydroxy-9,10-dihydrophenanthrene (DDP), which lacks redox cycling activity, had no effect on PTP1B activity.	9,10-phenanthrenequinone	0-7	catalase	Homo sapiens	119-127
32493877-4	2020	9,10-PQ oxidized recombinant human PTP1B at Cys215 and inhibited its catalytic activity, an effect that was blocked by catalase (CAT), whereas cis-9,10-dihydroxy-9,10-dihydrophenanthrene (DDP), which lacks redox cycling activity, had no effect on PTP1B activity.	9,10-phenanthrenequinone	0-7	catalase	Homo sapiens	129-132
32493877-4	2020	9,10-PQ oxidized recombinant human PTP1B at Cys215 and inhibited its catalytic activity, an effect that was blocked by catalase (CAT), whereas cis-9,10-dihydroxy-9,10-dihydrophenanthrene (DDP), which lacks redox cycling activity, had no effect on PTP1B activity.	9,10-phenanthrenequinone	0-7	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	247-252
32493877-5	2020	Exposure of A431 cells to 9,10-PQ, but not DDP, activated signaling through EGFR and its downstream extracellular signal-regulated kinase 1/2 (ERK1/2), coupled with a decrease of cellular PTP activity.	9,10-phenanthrenequinone	26-33	epidermal growth factor receptor	Homo sapiens	76-80
32493877-5	2020	Exposure of A431 cells to 9,10-PQ, but not DDP, activated signaling through EGFR and its downstream extracellular signal-regulated kinase 1/2 (ERK1/2), coupled with a decrease of cellular PTP activity.	9,10-phenanthrenequinone	26-33	mitogen-activated protein kinase 1	Homo sapiens	100-141
32493877-5	2020	Exposure of A431 cells to 9,10-PQ, but not DDP, activated signaling through EGFR and its downstream extracellular signal-regulated kinase 1/2 (ERK1/2), coupled with a decrease of cellular PTP activity.	9,10-phenanthrenequinone	26-33	mitogen-activated protein kinase 3	Homo sapiens	143-149
32493877-6	2020	Immunoprecipitation and UPLC-MSE revealed that PTP1B easily undergoes oxidation during exposure of A431 cells to 9,10-PQ.	9,10-phenanthrenequinone	113-120	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	47-52
32493877-7	2020	Pretreatment with polyethylene glycol conjugated with CAT (PEG-CAT) abolished 9,10-PQ-generated H2O2 production and significantly blocked the activation of EGFR-ERK1/2 signaling by 9,10-PQ, indicating the involvement of H2O2 in the activation because scavenging agents for hydroxyl radicals had no effect on the redox signal activation.	9,10-phenanthrenequinone	78-85	catalase	Homo sapiens	54-57
32493877-7	2020	Pretreatment with polyethylene glycol conjugated with CAT (PEG-CAT) abolished 9,10-PQ-generated H2O2 production and significantly blocked the activation of EGFR-ERK1/2 signaling by 9,10-PQ, indicating the involvement of H2O2 in the activation because scavenging agents for hydroxyl radicals had no effect on the redox signal activation.	9,10-phenanthrenequinone	78-85	catalase	Homo sapiens	59-66
32493877-7	2020	Pretreatment with polyethylene glycol conjugated with CAT (PEG-CAT) abolished 9,10-PQ-generated H2O2 production and significantly blocked the activation of EGFR-ERK1/2 signaling by 9,10-PQ, indicating the involvement of H2O2 in the activation because scavenging agents for hydroxyl radicals had no effect on the redox signal activation.	9,10-phenanthrenequinone	181-188	catalase	Homo sapiens	54-57
32493877-7	2020	Pretreatment with polyethylene glycol conjugated with CAT (PEG-CAT) abolished 9,10-PQ-generated H2O2 production and significantly blocked the activation of EGFR-ERK1/2 signaling by 9,10-PQ, indicating the involvement of H2O2 in the activation because scavenging agents for hydroxyl radicals had no effect on the redox signal activation.	9,10-phenanthrenequinone	181-188	catalase	Homo sapiens	59-66
32493877-7	2020	Pretreatment with polyethylene glycol conjugated with CAT (PEG-CAT) abolished 9,10-PQ-generated H2O2 production and significantly blocked the activation of EGFR-ERK1/2 signaling by 9,10-PQ, indicating the involvement of H2O2 in the activation because scavenging agents for hydroxyl radicals had no effect on the redox signal activation.	9,10-phenanthrenequinone	181-188	mitogen-activated protein kinase 3	Homo sapiens	161-167
33268681-0	2020	Redox cycling of 9,10-phenanthrenequinone activates epidermal growth factor receptor signaling through S-oxidation of protein tyrosine phosphatase 1B.	9,10-phenanthrenequinone	17-41	epidermal growth factor receptor	Homo sapiens	52-84
29108775-0	2018	Facilitation of 9,10-phenanthrenequinone-elicited neuroblastoma cell apoptosis by NAD(P)H:quinone oxidoreductase 1.	9,10-phenanthrenequinone	16-40	NAD(P)H quinone dehydrogenase 1	Homo sapiens	82-114
31357365-7	2019	For quinones, it varied from 1.12 mug L-1 (1,4-naphthoquinone) to 1.70 mug L-1(9,10-phenanthrenequinone).	9,10-phenanthrenequinone	79-103	immunoglobulin kappa variable 1-16	Homo sapiens	75-78
30719914-4	2019	No reaction occurred when 9,10-PQ was incubated with Na2S; however, when 5 muM 9,10-PQ was incubated with either 250 muM Na2S2 or Na2S4, we detected extensive consumption of dissolved oxygen (84 muM).	9,10-phenanthrenequinone	79-86	latexin	Homo sapiens	75-78
30719914-4	2019	No reaction occurred when 9,10-PQ was incubated with Na2S; however, when 5 muM 9,10-PQ was incubated with either 250 muM Na2S2 or Na2S4, we detected extensive consumption of dissolved oxygen (84 muM).	9,10-phenanthrenequinone	79-86	latexin	Homo sapiens	117-120
30719914-4	2019	No reaction occurred when 9,10-PQ was incubated with Na2S; however, when 5 muM 9,10-PQ was incubated with either 250 muM Na2S2 or Na2S4, we detected extensive consumption of dissolved oxygen (84 muM).	9,10-phenanthrenequinone	79-86	latexin	Homo sapiens	117-120
29108775-3	2018	SK-N-SH cell treatment with a lethal concentration of PQ facilitated ROS production within 6 h. The treatment also promoted formation of 8-hydroxy-deoxyguanosine, p53 activation, elevation of Bax/Bcl-2 ratio, lowering of mitochondrial membrane potential, and resultant activation of caspase-9 and caspase-3, inferring that ROS production, DNA damage and mitochondrial dysfunction are crucial processes of the PQ-triggered SK-N-SH cell apoptosis.	9,10-phenanthrenequinone	54-56	tumor protein p53	Homo sapiens	163-166
29108775-10	2018	Taken together, PQ exposure produces large amounts of ROS in neuroblastoma cells via NQO1 up-regulation and resultant acceleration of its redox-cycling, followed by activation of the ROS-dependent apoptotic mechanism.	9,10-phenanthrenequinone	16-18	NAD(P)H quinone dehydrogenase 1	Homo sapiens	85-89
29108775-3	2018	SK-N-SH cell treatment with a lethal concentration of PQ facilitated ROS production within 6 h. The treatment also promoted formation of 8-hydroxy-deoxyguanosine, p53 activation, elevation of Bax/Bcl-2 ratio, lowering of mitochondrial membrane potential, and resultant activation of caspase-9 and caspase-3, inferring that ROS production, DNA damage and mitochondrial dysfunction are crucial processes of the PQ-triggered SK-N-SH cell apoptosis.	9,10-phenanthrenequinone	54-56	BCL2 associated X, apoptosis regulator	Homo sapiens	192-195
29108775-3	2018	SK-N-SH cell treatment with a lethal concentration of PQ facilitated ROS production within 6 h. The treatment also promoted formation of 8-hydroxy-deoxyguanosine, p53 activation, elevation of Bax/Bcl-2 ratio, lowering of mitochondrial membrane potential, and resultant activation of caspase-9 and caspase-3, inferring that ROS production, DNA damage and mitochondrial dysfunction are crucial processes of the PQ-triggered SK-N-SH cell apoptosis.	9,10-phenanthrenequinone	54-56	BCL2 apoptosis regulator	Homo sapiens	196-201
29108775-3	2018	SK-N-SH cell treatment with a lethal concentration of PQ facilitated ROS production within 6 h. The treatment also promoted formation of 8-hydroxy-deoxyguanosine, p53 activation, elevation of Bax/Bcl-2 ratio, lowering of mitochondrial membrane potential, and resultant activation of caspase-9 and caspase-3, inferring that ROS production, DNA damage and mitochondrial dysfunction are crucial processes of the PQ-triggered SK-N-SH cell apoptosis.	9,10-phenanthrenequinone	54-56	caspase 9	Homo sapiens	283-292
29108775-3	2018	SK-N-SH cell treatment with a lethal concentration of PQ facilitated ROS production within 6 h. The treatment also promoted formation of 8-hydroxy-deoxyguanosine, p53 activation, elevation of Bax/Bcl-2 ratio, lowering of mitochondrial membrane potential, and resultant activation of caspase-9 and caspase-3, inferring that ROS production, DNA damage and mitochondrial dysfunction are crucial processes of the PQ-triggered SK-N-SH cell apoptosis.	9,10-phenanthrenequinone	54-56	caspase 3	Homo sapiens	297-306
28992312-6	2017	Linoleic and oleic acids also inhibited AKR1C3-mediated metabolism of 9,10-phenanthrenequinone in colon DLD1 cells.	9,10-phenanthrenequinone	70-94	aldo-keto reductase family 1 member C3	Homo sapiens	40-46
32264381-5	2017	On the other hand, modification of an electron-withdrawing moiety such as an indolium moiety on the same phenanthrenequinone imidazole-core provided a new material PID, which exhibited favorable TP emission, indicating that phenanthrenequinone imidazole derivatives could be exploited as TP materials.	9,10-phenanthrenequinone	105-124	metastasis associated 1 family member 2	Homo sapiens	164-167
32264381-5	2017	On the other hand, modification of an electron-withdrawing moiety such as an indolium moiety on the same phenanthrenequinone imidazole-core provided a new material PID, which exhibited favorable TP emission, indicating that phenanthrenequinone imidazole derivatives could be exploited as TP materials.	9,10-phenanthrenequinone	224-243	metastasis associated 1 family member 2	Homo sapiens	164-167
28805980-0	2017	An environmental pollutant, 9,10-phenanthrenequinone, activates human TRPA1 via critical cysteines 621 and 665.	9,10-phenanthrenequinone	28-52	transient receptor potential cation channel subfamily A member 1	Homo sapiens	70-75
28805980-2	2017	In our recent study, 9, 10-phenanthrenequinone (9,10-PQ) is the most potent irritant for activation of NRF2 among 1395 cigarette smoke components and it may be, therefore, important to find its additional targets.	9,10-phenanthrenequinone	21-46	NFE2 like bZIP transcription factor 2	Homo sapiens	103-107
28805980-2	2017	In our recent study, 9, 10-phenanthrenequinone (9,10-PQ) is the most potent irritant for activation of NRF2 among 1395 cigarette smoke components and it may be, therefore, important to find its additional targets.	9,10-phenanthrenequinone	48-55	NFE2 like bZIP transcription factor 2	Homo sapiens	103-107
28805980-3	2017	Here, we show that 9,10-PQ functions as an activator of TRPA1 in human embryonic kidney (HEK) cells expressing human wild-type TRPA1 (HEK-wTRPA1) and human alveolar A549 (A549) cells.	9,10-phenanthrenequinone	19-26	transient receptor potential cation channel subfamily A member 1	Homo sapiens	56-61
28805980-3	2017	Here, we show that 9,10-PQ functions as an activator of TRPA1 in human embryonic kidney (HEK) cells expressing human wild-type TRPA1 (HEK-wTRPA1) and human alveolar A549 (A549) cells.	9,10-phenanthrenequinone	19-26	transient receptor potential cation channel subfamily A member 1	Homo sapiens	127-132
28805980-12	2017	Our findings demonstrate that 9,10-PQ activation of human TRA1 is dependent on cysteine residues 621 and 665.	9,10-phenanthrenequinone	30-37	phospholipid scramblase 4	Homo sapiens	58-62
28595002-6	2017	Using 9,10-phenanthrenequinone as the substrate, quinone redox cycling was found to inhibit DCXR reduction of l-xylulose and diacetyl.	9,10-phenanthrenequinone	6-30	dicarbonyl and L-xylulose reductase	Homo sapiens	92-96
27103119-3	2016	In comparison, the reaction of trans-[Ru(III)(PQ (-))(PPh3)2Cl2] (PQ), a 9,10-phenanthrenequinone (PQ) analogue of affords only trans-[Ru(III)(PQ)(PPh3)2Cl2](+)Br3(-) ((+)Br3(-)).	9,10-phenanthrenequinone	46-48	caveolin 1	Homo sapiens	54-58
29187913-8	2017	The o-MOCA was optimized and its performance evaluated using the 9,10-phenanthraquinone (PQ) as a standard redox-active compound.	9,10-phenanthrenequinone	65-87	dedicator of cytokinesis 3	Homo sapiens	6-10
29187913-8	2017	The o-MOCA was optimized and its performance evaluated using the 9,10-phenanthraquinone (PQ) as a standard redox-active compound.	9,10-phenanthrenequinone	89-91	dedicator of cytokinesis 3	Homo sapiens	6-10
29187913-9	2017	Laboratory testing shows minimum interferences or carryover between consecutive samples, low blanks, and a reproducible, linear response between the DTT consumption rate (nmol min-1) and PQ concentration (muM).	9,10-phenanthrenequinone	187-189	CD59 molecule (CD59 blood group)	Homo sapiens	176-181
29187913-9	2017	Laboratory testing shows minimum interferences or carryover between consecutive samples, low blanks, and a reproducible, linear response between the DTT consumption rate (nmol min-1) and PQ concentration (muM).	9,10-phenanthrenequinone	187-189	latexin	Homo sapiens	205-208
27103119-3	2016	In comparison, the reaction of trans-[Ru(III)(PQ (-))(PPh3)2Cl2] (PQ), a 9,10-phenanthrenequinone (PQ) analogue of affords only trans-[Ru(III)(PQ)(PPh3)2Cl2](+)Br3(-) ((+)Br3(-)).	9,10-phenanthrenequinone	46-48	caveolin 1	Homo sapiens	147-151
27103119-3	2016	In comparison, the reaction of trans-[Ru(III)(PQ (-))(PPh3)2Cl2] (PQ), a 9,10-phenanthrenequinone (PQ) analogue of affords only trans-[Ru(III)(PQ)(PPh3)2Cl2](+)Br3(-) ((+)Br3(-)).	9,10-phenanthrenequinone	73-97	caveolin 1	Homo sapiens	54-58
27103119-3	2016	In comparison, the reaction of trans-[Ru(III)(PQ (-))(PPh3)2Cl2] (PQ), a 9,10-phenanthrenequinone (PQ) analogue of affords only trans-[Ru(III)(PQ)(PPh3)2Cl2](+)Br3(-) ((+)Br3(-)).	9,10-phenanthrenequinone	66-68	caveolin 1	Homo sapiens	54-58
27103119-3	2016	In comparison, the reaction of trans-[Ru(III)(PQ (-))(PPh3)2Cl2] (PQ), a 9,10-phenanthrenequinone (PQ) analogue of affords only trans-[Ru(III)(PQ)(PPh3)2Cl2](+)Br3(-) ((+)Br3(-)).	9,10-phenanthrenequinone	66-68	caveolin 1	Homo sapiens	147-151
24273736-3	2013	In this study, we examined feasibility of using tanshinones, a novel class of phenanthrenequinone-based cytoprotective Nrf2 inducers derived from the medicinal plant Salvia miltiorrhiza, for protection of cultured human skin cells and reconstructed human skin against solar simulated UV.	9,10-phenanthrenequinone	78-97	NFE2 like bZIP transcription factor 2	Homo sapiens	119-123
24646012-9	2014	The identification of 9,10-catechol conjugates supports metabolic detoxification of phenanthrene-9,10-quinone through interception of redox cycling by UGT, COMT, and SULT isozymes and indicates the possible use of phenanthrene-9,10-catechol conjugates as biomarkers of human exposure to oxygenated PAH.	9,10-phenanthrenequinone	84-109	UDP glucuronosyltransferase family 1 member A complex locus	Homo sapiens	151-154
24646012-9	2014	The identification of 9,10-catechol conjugates supports metabolic detoxification of phenanthrene-9,10-quinone through interception of redox cycling by UGT, COMT, and SULT isozymes and indicates the possible use of phenanthrene-9,10-catechol conjugates as biomarkers of human exposure to oxygenated PAH.	9,10-phenanthrenequinone	84-109	catechol-O-methyltransferase	Homo sapiens	156-160
26381591-3	2015	Therefore, a comprehensive analysis of the conformational structure and the solvent polarity induced energy level reordering of the two lowest triplet states of 9,10-phenanthrenequinone (PQ) was carried out using nanosecond-time-resolved absorption (ns-TRA), time-resolved resonance Raman (TR(3)) spectroscopy, and time dependent-density functional theory (TD-DFT) studies.	9,10-phenanthrenequinone	161-185	T cell receptor alpha locus	Homo sapiens	253-256
26381591-3	2015	Therefore, a comprehensive analysis of the conformational structure and the solvent polarity induced energy level reordering of the two lowest triplet states of 9,10-phenanthrenequinone (PQ) was carried out using nanosecond-time-resolved absorption (ns-TRA), time-resolved resonance Raman (TR(3)) spectroscopy, and time dependent-density functional theory (TD-DFT) studies.	9,10-phenanthrenequinone	187-189	T cell receptor alpha locus	Homo sapiens	253-256
25550200-2	2015	SPR also mediates chemical redox cycling, catalyzing one-electron reduction of redox-active chemicals, including quinones and bipyridinium herbicides (e.g., menadione, 9,10-phenanthrenequinone, and diquat); rapid reaction of the reduced radicals with molecular oxygen generates reactive oxygen species (ROS).	9,10-phenanthrenequinone	168-192	sepiapterin reductase	Rattus norvegicus	0-3
26190959-7	2014	A comprehensive analysis of the coupled chemo-enzymatic reactions revealed pronounced inhibition of hUGDH by NADH and UDP-xylose as well as an adequate oxygen supply for PQ re-oxidation as major bottlenecks of effective performance of the overall multi-step reaction system.	9,10-phenanthrenequinone	170-172	UDP-glucose 6-dehydrogenase	Homo sapiens	100-105
23640889-4	2013	In addition to reducing sepiapterin, SPR mediated chemical redox cycling of bipyridinium herbicides and various quinones; this activity was greatest for 1,2-naphthoquinone followed by 9,10-phenanthrenequinone, 1,4-naphthoquinone, menadione, and 2,3-dimethyl-1,4-naphthoquinone.	9,10-phenanthrenequinone	184-208	sepiapterin reductase	Homo sapiens	37-40
23475264-1	2013	Reactions of 9,10-phenanthrenequinone (PQ) in toluene with [M(II)(PPh3)3X2] at 298 K afford green complexes, trans-[M(PQ)(PPh3)2X2] (M = Ru, X = Cl, 1; M = Os, X = Br, 2) in moderate yields.	9,10-phenanthrenequinone	13-37	caveolin 1	Homo sapiens	66-70
23475264-1	2013	Reactions of 9,10-phenanthrenequinone (PQ) in toluene with [M(II)(PPh3)3X2] at 298 K afford green complexes, trans-[M(PQ)(PPh3)2X2] (M = Ru, X = Cl, 1; M = Os, X = Br, 2) in moderate yields.	9,10-phenanthrenequinone	13-37	caveolin 1	Homo sapiens	122-126
23475264-1	2013	Reactions of 9,10-phenanthrenequinone (PQ) in toluene with [M(II)(PPh3)3X2] at 298 K afford green complexes, trans-[M(PQ)(PPh3)2X2] (M = Ru, X = Cl, 1; M = Os, X = Br, 2) in moderate yields.	9,10-phenanthrenequinone	39-41	caveolin 1	Homo sapiens	66-70
23475264-1	2013	Reactions of 9,10-phenanthrenequinone (PQ) in toluene with [M(II)(PPh3)3X2] at 298 K afford green complexes, trans-[M(PQ)(PPh3)2X2] (M = Ru, X = Cl, 1; M = Os, X = Br, 2) in moderate yields.	9,10-phenanthrenequinone	39-41	caveolin 1	Homo sapiens	122-126
23475264-2	2013	Reaction of anhydrous RhCl3 with PQ and PPh3 in boiling ethanol affords the dark brown paramagnetic complex, cis-[Rh(PQ)(PPh3)2Cl2] (3) in good yields.	9,10-phenanthrenequinone	33-35	caveolin 1	Homo sapiens	121-125
22925602-2	2012	9,10-Phenanthrenequinone (9,10-PQ), a major quinone in diesel exhaust particles, produces ROS in redox cycling following two-electron reduction by NAD(P)H:quinone oxidoreductase 1 (NQO1), which has been considered as a cause of its cyto- and genotoxicity.	9,10-phenanthrenequinone	0-24	NAD(P)H quinone dehydrogenase 1	Homo sapiens	147-179
22925602-2	2012	9,10-Phenanthrenequinone (9,10-PQ), a major quinone in diesel exhaust particles, produces ROS in redox cycling following two-electron reduction by NAD(P)H:quinone oxidoreductase 1 (NQO1), which has been considered as a cause of its cyto- and genotoxicity.	9,10-phenanthrenequinone	0-24	NAD(P)H quinone dehydrogenase 1	Homo sapiens	181-185
22925602-2	2012	9,10-Phenanthrenequinone (9,10-PQ), a major quinone in diesel exhaust particles, produces ROS in redox cycling following two-electron reduction by NAD(P)H:quinone oxidoreductase 1 (NQO1), which has been considered as a cause of its cyto- and genotoxicity.	9,10-phenanthrenequinone	26-33	NAD(P)H quinone dehydrogenase 1	Homo sapiens	147-179
22925602-2	2012	9,10-Phenanthrenequinone (9,10-PQ), a major quinone in diesel exhaust particles, produces ROS in redox cycling following two-electron reduction by NAD(P)H:quinone oxidoreductase 1 (NQO1), which has been considered as a cause of its cyto- and genotoxicity.	9,10-phenanthrenequinone	26-33	NAD(P)H quinone dehydrogenase 1	Homo sapiens	181-185
22925602-3	2012	In this study, we show that NAC unexpectedly augments the toxicity of 9,10-PQ in cells with low NQO1 activity.	9,10-phenanthrenequinone	70-77	X-linked Kx blood group	Homo sapiens	28-31
22925602-3	2012	In this study, we show that NAC unexpectedly augments the toxicity of 9,10-PQ in cells with low NQO1 activity.	9,10-phenanthrenequinone	70-77	NAD(P)H quinone dehydrogenase 1	Homo sapiens	96-100
22925602-5	2012	In the skin cells, the cytotoxicity of 9,10-PQ was significantly enhanced by addition of NAC.	9,10-phenanthrenequinone	39-46	X-linked Kx blood group	Homo sapiens	89-92
22925602-9	2012	The results suggested that dual effects of NAC on the cyto- and genotoxicity of 9,10-PQ were dependent on tissue-specific NQO1 activity.	9,10-phenanthrenequinone	80-87	X-linked Kx blood group	Homo sapiens	43-46
22925602-9	2012	The results suggested that dual effects of NAC on the cyto- and genotoxicity of 9,10-PQ were dependent on tissue-specific NQO1 activity.	9,10-phenanthrenequinone	80-87	NAD(P)H quinone dehydrogenase 1	Homo sapiens	122-126
22281686-8	2012	The exposure of A549 cells to 9,10-PQ provokes viability loss, which is significantly protected by the addition of the AKR1C3 inhibitor and antioxidant enzyme and by the removal of the surfactants from the culture medium.	9,10-phenanthrenequinone	30-37	aldo-keto reductase family 1 member C3	Homo sapiens	119-125
22975515-4	2012	Flow cytometric analyses of U937 cells after long-term exposure to 9,10-PQ revealed induction of differentiation that was evidenced by increasing expression of CD11b/CD18, a cell-surface marker for monocytic differentiation into macrophages.	9,10-phenanthrenequinone	67-74	integrin subunit alpha M	Homo sapiens	160-165
22975515-4	2012	Flow cytometric analyses of U937 cells after long-term exposure to 9,10-PQ revealed induction of differentiation that was evidenced by increasing expression of CD11b/CD18, a cell-surface marker for monocytic differentiation into macrophages.	9,10-phenanthrenequinone	67-74	integrin subunit beta 2	Homo sapiens	166-170
22975515-6	2012	The 9,10-PQ treatment increased the expression of aldo-keto reductase (AKR) 1C3, which reached a peak at 1 to 2 d post-treatment and then declined.	9,10-phenanthrenequinone	4-11	aldo-keto reductase family 1 member C3	Homo sapiens	50-79
22975515-7	2012	The bell-shaped curve of the AKR1C3 expression by 9,10-PQ resembled that caused by phorbol 12-myristate 13-acetate, a differentiation inducer.	9,10-phenanthrenequinone	50-57	aldo-keto reductase family 1 member C3	Homo sapiens	29-35
22975515-8	2012	Additionally, the concomitant treatment with tolfenamic acid, a selective AKR1C3 inhibitor, sensitized the differentiation induced by 9,10-PQ.	9,10-phenanthrenequinone	134-141	aldo-keto reductase family 1 member C3	Homo sapiens	74-80
22975515-9	2012	These results suggest that ROS formation during 9,10-PQ treatment acutely leads to apoptosis of U937 cells and the initiation of monocytic differentiation, which proceeds after the provisional overexpression of AKR1C3.	9,10-phenanthrenequinone	48-55	aldo-keto reductase family 1 member C3	Homo sapiens	211-217
18571493-4	2008	Human DHRS4 reduced various aromatic ketones and alpha-dicarbonyl compounds including cytotoxic 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	96-120	dehydrogenase/reductase 4	Homo sapiens	6-11
21623689-3	2011	The 9,10-PQ-mediated CHOP induction was strengthened by a proteasome inhibitor (MG132) and the MG132-induced cell sensitization to the 9,10-PQ toxicity was abolished by a ROS inhibitor, suggesting that ROS generation and consequent proteasomal dysfunction are responsible for the CHOP up-regulation caused by 9,10-PQ.	9,10-phenanthrenequinone	4-11	DNA-damage inducible transcript 3	Rattus norvegicus	21-25
21623689-3	2011	The 9,10-PQ-mediated CHOP induction was strengthened by a proteasome inhibitor (MG132) and the MG132-induced cell sensitization to the 9,10-PQ toxicity was abolished by a ROS inhibitor, suggesting that ROS generation and consequent proteasomal dysfunction are responsible for the CHOP up-regulation caused by 9,10-PQ.	9,10-phenanthrenequinone	4-11	DNA-damage inducible transcript 3	Rattus norvegicus	280-284
21623689-3	2011	The 9,10-PQ-mediated CHOP induction was strengthened by a proteasome inhibitor (MG132) and the MG132-induced cell sensitization to the 9,10-PQ toxicity was abolished by a ROS inhibitor, suggesting that ROS generation and consequent proteasomal dysfunction are responsible for the CHOP up-regulation caused by 9,10-PQ.	9,10-phenanthrenequinone	135-142	DNA-damage inducible transcript 3	Rattus norvegicus	280-284
21623689-3	2011	The 9,10-PQ-mediated CHOP induction was strengthened by a proteasome inhibitor (MG132) and the MG132-induced cell sensitization to the 9,10-PQ toxicity was abolished by a ROS inhibitor, suggesting that ROS generation and consequent proteasomal dysfunction are responsible for the CHOP up-regulation caused by 9,10-PQ.	9,10-phenanthrenequinone	135-142	DNA-damage inducible transcript 3	Rattus norvegicus	280-284
19442656-0	2009	Involvement of an aldo-keto reductase (AKR1C3) in redox cycling of 9,10-phenanthrenequinone leading to apoptosis in human endothelial cells.	9,10-phenanthrenequinone	67-91	aldo-keto reductase family 1 member C3	Homo sapiens	39-45
19442656-4	2009	Comparison of mRNA expression levels and kinetic constants in the 9,10-PQ reduction among 10 human reductases suggests that aldo-keto reductase 1C3 (AKR1C3) is a 9,10-PQ reductase in HAECs.	9,10-phenanthrenequinone	66-73	aldo-keto reductase family 1 member C3	Homo sapiens	124-147
19442656-4	2009	Comparison of mRNA expression levels and kinetic constants in the 9,10-PQ reduction among 10 human reductases suggests that aldo-keto reductase 1C3 (AKR1C3) is a 9,10-PQ reductase in HAECs.	9,10-phenanthrenequinone	66-73	aldo-keto reductase family 1 member C3	Homo sapiens	149-155
19442656-5	2009	In in vitro 9,10-PQ reduction by AKR1C3, the reduced product 9,10-dihydroxyphenanthrene and superoxide anions were formed, suggesting the enzymatic two-electron reduction of 9,10-PQ that thereby causes oxidative stress through its redox cycling.	9,10-phenanthrenequinone	12-19	aldo-keto reductase family 1 member C3	Homo sapiens	33-39
19442656-5	2009	In in vitro 9,10-PQ reduction by AKR1C3, the reduced product 9,10-dihydroxyphenanthrene and superoxide anions were formed, suggesting the enzymatic two-electron reduction of 9,10-PQ that thereby causes oxidative stress through its redox cycling.	9,10-phenanthrenequinone	174-181	aldo-keto reductase family 1 member C3	Homo sapiens	33-39
19442656-6	2009	In addition, the participation of AKR1C3 in 9,10-PQ-redox cycling was confirmed by the data that AKR1C3 overexpression in endothelial cells augmented the ROS generation and cytotoxicity by 9,10-PQ, and the ROS scavengers inhibited the toxic effects.	9,10-phenanthrenequinone	44-51	aldo-keto reductase family 1 member C3	Homo sapiens	34-40
19442656-6	2009	In addition, the participation of AKR1C3 in 9,10-PQ-redox cycling was confirmed by the data that AKR1C3 overexpression in endothelial cells augmented the ROS generation and cytotoxicity by 9,10-PQ, and the ROS scavengers inhibited the toxic effects.	9,10-phenanthrenequinone	44-51	aldo-keto reductase family 1 member C3	Homo sapiens	97-103
19442656-6	2009	In addition, the participation of AKR1C3 in 9,10-PQ-redox cycling was confirmed by the data that AKR1C3 overexpression in endothelial cells augmented the ROS generation and cytotoxicity by 9,10-PQ, and the ROS scavengers inhibited the toxic effects.	9,10-phenanthrenequinone	189-196	aldo-keto reductase family 1 member C3	Homo sapiens	34-40
19442656-6	2009	In addition, the participation of AKR1C3 in 9,10-PQ-redox cycling was confirmed by the data that AKR1C3 overexpression in endothelial cells augmented the ROS generation and cytotoxicity by 9,10-PQ, and the ROS scavengers inhibited the toxic effects.	9,10-phenanthrenequinone	189-196	aldo-keto reductase family 1 member C3	Homo sapiens	97-103
19442656-7	2009	Pretreatment of the overexpressing cells with AKR1C3 inhibitors, flufenamic acid and indomethacin, suppressed the 9,10-PQ-induced GSH depletion.	9,10-phenanthrenequinone	114-121	aldo-keto reductase family 1 member C3	Homo sapiens	46-52
19442656-8	2009	These results suggest that AKR1C3 is a key enzyme in the initial step of 9,10-PQ-induced cytotoxicity in HAECs.	9,10-phenanthrenequinone	73-80	aldo-keto reductase family 1 member C3	Homo sapiens	27-33
19000905-6	2008	We further demonstrate that the in vitro quinone reduction by CBR4 generates superoxide through the redox cycling, and suggest that the enzyme may be involved in the induction of apoptosis by cytotoxic 9,10-phenanthrenequinone.	9,10-phenanthrenequinone	202-226	carbonyl reductase 4	Homo sapiens	62-66
18294972-10	2008	In addition, deletion of the transcription factor Nrf2 decreased PQHG formation and increased PQ-mediated toxicity of mouse primary hepatocytes.	9,10-phenanthrenequinone	65-67	nuclear factor, erythroid derived 2, like 2	Mus musculus	50-54
18206670-0	2008	L-Xylulose reductase is involved in 9,10-phenanthrenequinone-induced apoptosis in human T lymphoma cells.	9,10-phenanthrenequinone	36-60	dicarbonyl and L-xylulose reductase	Homo sapiens	0-20
18206670-6	2008	Surprisingly, the ROS generation and cytotoxicity by 9,10-PQ were augmented in an XR-transformed cell line.	9,10-phenanthrenequinone	53-60	dicarbonyl and L-xylulose reductase	Homo sapiens	82-84
18206670-7	2008	XR indeed reduced 9,10-PQ and produced superoxide anion through redox cycling.	9,10-phenanthrenequinone	18-25	dicarbonyl and L-xylulose reductase	Homo sapiens	0-2
18206670-9	2008	Moreover, the 9,10-PQ-induced apoptosis was partially inhibited by the pretreatment with XR-specific inhibitors.	9,10-phenanthrenequinone	14-21	dicarbonyl and L-xylulose reductase	Homo sapiens	89-91
17950253-4	2008	We tested NSAIDs and NSAID analogues for inhibition of the reduction of 9,10-phenanthrenequinone (PQ) catalyzed by AKR1C3 and the closely related isoforms AKR1C1 and AKR1C2.	9,10-phenanthrenequinone	72-96	aldo-keto reductase family 1 member C3	Homo sapiens	115-121
17950253-4	2008	We tested NSAIDs and NSAID analogues for inhibition of the reduction of 9,10-phenanthrenequinone (PQ) catalyzed by AKR1C3 and the closely related isoforms AKR1C1 and AKR1C2.	9,10-phenanthrenequinone	72-96	aldo-keto reductase family 1 member C1	Homo sapiens	155-161
17950253-4	2008	We tested NSAIDs and NSAID analogues for inhibition of the reduction of 9,10-phenanthrenequinone (PQ) catalyzed by AKR1C3 and the closely related isoforms AKR1C1 and AKR1C2.	9,10-phenanthrenequinone	72-96	aldo-keto reductase family 1 member C2	Homo sapiens	166-172
17950253-4	2008	We tested NSAIDs and NSAID analogues for inhibition of the reduction of 9,10-phenanthrenequinone (PQ) catalyzed by AKR1C3 and the closely related isoforms AKR1C1 and AKR1C2.	9,10-phenanthrenequinone	98-100	aldo-keto reductase family 1 member C3	Homo sapiens	115-121
17950253-4	2008	We tested NSAIDs and NSAID analogues for inhibition of the reduction of 9,10-phenanthrenequinone (PQ) catalyzed by AKR1C3 and the closely related isoforms AKR1C1 and AKR1C2.	9,10-phenanthrenequinone	98-100	aldo-keto reductase family 1 member C1	Homo sapiens	155-161
17950253-4	2008	We tested NSAIDs and NSAID analogues for inhibition of the reduction of 9,10-phenanthrenequinone (PQ) catalyzed by AKR1C3 and the closely related isoforms AKR1C1 and AKR1C2.	9,10-phenanthrenequinone	98-100	aldo-keto reductase family 1 member C2	Homo sapiens	166-172
17950253-9	2008	The pattern of inhibition of AKR1C3 by indomethacin and CBM was uncompetitive versus PQ, but competitive versus Delta(4)-androstene-3,17-dione, indicating that two different inhibitory complexes form during the ordered bi bi reactions.	9,10-phenanthrenequinone	85-87	aldo-keto reductase family 1 member C3	Homo sapiens	29-35